PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19664055-5 2009 Arylamine N-acetyltransferase 1 (NAT1) is a xenobiotic-metabolizing enzyme that biotransforms aromatic amine drugs and carcinogens. aromatic amine 94-108 N-acetyltransferase 1 Homo sapiens 0-31 19664055-5 2009 Arylamine N-acetyltransferase 1 (NAT1) is a xenobiotic-metabolizing enzyme that biotransforms aromatic amine drugs and carcinogens. aromatic amine 94-108 N-acetyltransferase 1 Homo sapiens 33-37 21193389-9 2011 Analysis of the chondroitin/dermatan sulfate fraction by chondroitinase ACII digestion showed dermatan sulfate storage, consistent with inhibition of iduronate 2-sulfatase. Dermatan Sulfate 28-44 iduronate 2-sulfatase Homo sapiens 150-171 20821239-1 2011 Endothelial cell-specific molecule-1 (ESM-1) is a secretory proteoglycan comprising a mature polypeptide of 165 amino acids and a single dermatan sulfate. Dermatan Sulfate 137-153 endothelial cell specific molecule 1 Homo sapiens 0-36 21624210-2 2011 IDUA is one of the enzymes involved in degradation of glycosaminoglycans heparan sulphate and dermatan sulphate. Dermatan Sulfate 94-111 alpha-L-iduronidase Homo sapiens 0-4 21378286-1 2011 The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS). Dermatan Sulfate 175-191 arylsulfatase B Homo sapiens 28-61 21378286-1 2011 The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS). Dermatan Sulfate 175-191 arylsulfatase B Homo sapiens 63-67 21378286-1 2011 The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS). Dermatan Sulfate 175-191 arylsulfatase B Homo sapiens 69-72 21378286-1 2011 The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS). Dermatan Sulfate 193-195 arylsulfatase B Homo sapiens 28-61 21378286-1 2011 The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS). Dermatan Sulfate 193-195 arylsulfatase B Homo sapiens 63-67 21378286-1 2011 The enzyme arylsulfatase B (N-acetylgalactosamine-4-sulfatase; ARSB; ASB) removes 4-sulfate groups from the sulfated glycosaminoglycans (sGAG) chondroitin-4-sulfate (C4S) and dermatan sulfate (DS). Dermatan Sulfate 193-195 arylsulfatase B Homo sapiens 69-72 20821239-1 2011 Endothelial cell-specific molecule-1 (ESM-1) is a secretory proteoglycan comprising a mature polypeptide of 165 amino acids and a single dermatan sulfate. Dermatan Sulfate 137-153 endothelial cell specific molecule 1 Homo sapiens 38-43 21062008-4 2010 Using a gel mobility shift assay, we found that HBD2 bound to a range of GAGs including heparin/heparan sulfate (HS), dermatan sulfate (DS), and chondroitin sulfate. Dermatan Sulfate 118-134 defensin beta 4A Homo sapiens 48-52 20980181-2 2011 MPS VI is characterized by an absence or deficiency of N-acetylgalactosamine 4-sulfatase (arylsulfatase B) resulting in accumulation of dermatan sulfate. Dermatan Sulfate 136-152 arylsulfatase B Homo sapiens 55-88 20980181-2 2011 MPS VI is characterized by an absence or deficiency of N-acetylgalactosamine 4-sulfatase (arylsulfatase B) resulting in accumulation of dermatan sulfate. Dermatan Sulfate 136-152 arylsulfatase B Homo sapiens 90-105 22303797-8 2011 MPS I is a progressive disease, in which tissue accummulation of heparan and dermatan sulphate result from defective activity or lack of alpha-L-iduronidase. Dermatan Sulfate 77-94 alpha-L-iduronidase Homo sapiens 137-156 21514431-0 2011 Dermatan sulfate interacts with dead cells and regulates CD5(+) B-cell fate: implications for a key role in autoimmunity. Dermatan Sulfate 0-16 CD5 molecule Homo sapiens 57-60 21062008-4 2010 Using a gel mobility shift assay, we found that HBD2 bound to a range of GAGs including heparin/heparan sulfate (HS), dermatan sulfate (DS), and chondroitin sulfate. Dermatan Sulfate 136-138 defensin beta 4A Homo sapiens 48-52 20670608-1 2010 Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS). Dermatan Sulfate 182-198 coagulation factor II, thrombin Homo sapiens 35-43 20670608-1 2010 Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS). Dermatan Sulfate 182-198 serpin family D member 1 Homo sapiens 63-82 20670608-1 2010 Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS). Dermatan Sulfate 182-198 serpin family D member 1 Homo sapiens 84-88 20670608-1 2010 Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS). Dermatan Sulfate 200-202 coagulation factor II, thrombin Homo sapiens 35-43 20670608-1 2010 Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS). Dermatan Sulfate 200-202 serpin family D member 1 Homo sapiens 63-82 20670608-1 2010 Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS). Dermatan Sulfate 200-202 serpin family D member 1 Homo sapiens 84-88 20581009-0 2010 Characterization and binding activity of the chondroitin/dermatan sulfate chain from Endocan, a soluble endothelial proteoglycan. Dermatan Sulfate 57-73 endothelial cell specific molecule 1 Homo sapiens 85-92 20581009-1 2010 Endocan is a recently identified soluble chondroitin/dermatan sulfate (CS/DS) proteoglycan. Dermatan Sulfate 53-69 endothelial cell specific molecule 1 Homo sapiens 0-7 20842734-9 2010 Our findings confirm that the EDS-variant associated with CHST14 mutations forms a clinical spectrum, which we propose to coin as "musculocontractural EDS" and which results from a defect in dermatan sulfate biosynthesis, perturbing collagen assembly. Dermatan Sulfate 191-207 carbohydrate sulfotransferase 14 Homo sapiens 58-64 20439988-0 2010 Mice deficient in N-acetylgalactosamine 4-sulfate 6-o-sulfotransferase are unable to synthesize chondroitin/dermatan sulfate containing N-acetylgalactosamine 4,6-bissulfate residues and exhibit decreased protease activity in bone marrow-derived mast cells. Dermatan Sulfate 108-124 carbohydrate sulfotransferase 15 Mus musculus 18-70 21123810-0 2010 Replacing the enzyme alpha-L-iduronidase at birth ameliorates symptoms in the brain and periphery of dogs with mucopolysaccharidosis type I. Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disease caused by loss of activity of alpha-l-iduronidase and attendant accumulation of the glycosaminoglycans dermatan sulfate and heparan sulfate. Dermatan Sulfate 312-328 alpha-L-iduronidase Canis lupus familiaris 21-40 20584902-9 2010 Computational chemistry using molecular modeling and calculations of the electrostatic potential of the hexasaccharide and two pleiotrophin-binding octasaccharides previously isolated from CS/DS hybrid chains of embryonic pig brain identified an electronegative zone potentially involved in the molecular recognition of the oligosaccharides by pleiotrophin. Dermatan Sulfate 192-194 pleiotrophin Sus scrofa 127-139 20584902-1 2010 Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain. Dermatan Sulfate 136-152 pleiotrophin Sus scrofa 11-23 20584902-1 2010 Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain. Dermatan Sulfate 136-152 hepatocyte growth factor Sus scrofa 28-52 20584902-1 2010 Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain. Dermatan Sulfate 136-152 hepatocyte growth factor Sus scrofa 54-57 20584902-1 2010 Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain. Dermatan Sulfate 154-156 pleiotrophin Sus scrofa 11-23 20584902-1 2010 Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain. Dermatan Sulfate 154-156 hepatocyte growth factor Sus scrofa 28-52 20584902-1 2010 Endogenous pleiotrophin and hepatocyte growth factor (HGF) mediate the neurite outgrowth-promoting activity of chondroitin sulfate (CS)/dermatan sulfate (DS) hybrid chains isolated from embryonic pig brain. Dermatan Sulfate 154-156 hepatocyte growth factor Sus scrofa 54-57 20584902-3 2010 In this study, pleiotrophin- and HGF-binding domains in shark skin CS/DS were investigated. Dermatan Sulfate 70-72 pleiotrophin Sus scrofa 15-27 20584902-3 2010 In this study, pleiotrophin- and HGF-binding domains in shark skin CS/DS were investigated. Dermatan Sulfate 70-72 hepatocyte growth factor Sus scrofa 33-36 20584902-4 2010 A high affinity CS/DS fraction was isolated using a pleiotrophin-immobilized column. Dermatan Sulfate 19-21 pleiotrophin Sus scrofa 52-64 20584902-5 2010 It showed marked neurite outgrowth-promoting activity and strong inhibitory activity against the binding of pleiotrophin to immobilized CS/DS chains from embryonic pig brain. Dermatan Sulfate 139-141 pleiotrophin Sus scrofa 108-120 20584902-8 2010 It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity. Dermatan Sulfate 91-93 hepatocyte growth factor Sus scrofa 58-61 20584902-8 2010 It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity. Dermatan Sulfate 197-199 hepatocyte growth factor Sus scrofa 58-61 20584902-8 2010 It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity. Dermatan Sulfate 197-199 pleiotrophin Sus scrofa 122-134 20584902-8 2010 It displayed a potent inhibitory effect on the binding of HGF to immobilized shark skin CS/DS chains, suggesting that the pleiotrophin- and HGF-binding domains at least partially overlap in the CS/DS chains involved in the neuritogenic activity. Dermatan Sulfate 197-199 hepatocyte growth factor Sus scrofa 140-143 20043808-4 2010 Pretreatment of the 42-residue Abeta fragment (Abeta1-42) with the ubiquitous brain carbohydrates, glucose, fructose, and the GAG chondroitin sulfate B (CSB) inhibits Abeta1-42-induced apoptosis and reduces the peptide neurotoxicity on neuroblastoma cells, a cytoprotective effect that is partially reverted by AGE inhibitors such as pyridoxamine and L-carnosine. Dermatan Sulfate 130-151 amyloid beta precursor protein Homo sapiens 31-36 20043808-4 2010 Pretreatment of the 42-residue Abeta fragment (Abeta1-42) with the ubiquitous brain carbohydrates, glucose, fructose, and the GAG chondroitin sulfate B (CSB) inhibits Abeta1-42-induced apoptosis and reduces the peptide neurotoxicity on neuroblastoma cells, a cytoprotective effect that is partially reverted by AGE inhibitors such as pyridoxamine and L-carnosine. Dermatan Sulfate 153-156 amyloid beta precursor protein Homo sapiens 31-36 20533528-4 2010 CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS). Dermatan Sulfate 197-213 carbohydrate sulfotransferase 14 Homo sapiens 0-6 20533528-4 2010 CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS). Dermatan Sulfate 197-213 carbohydrate sulfotransferase 14 Homo sapiens 48-53 20533528-4 2010 CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS). Dermatan Sulfate 215-217 carbohydrate sulfotransferase 14 Homo sapiens 0-6 20533528-4 2010 CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS). Dermatan Sulfate 215-217 carbohydrate sulfotransferase 14 Homo sapiens 48-53 20439988-2 2010 N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of N-acetylgalactosamine 4-sulfate in CS or DS to yield GalNAc(4,6-SO(4)) residues. Dermatan Sulfate 187-189 carbohydrate sulfotransferase 15 Mus musculus 0-52 20439988-2 2010 N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of N-acetylgalactosamine 4-sulfate in CS or DS to yield GalNAc(4,6-SO(4)) residues. Dermatan Sulfate 187-189 carbohydrate sulfotransferase 15 Mus musculus 54-66 20652491-1 2010 Mucopolysaccharidosis type II (MPS II; Hunter syndrome) is an X-linked inherited disorder caused by a deficiency of the enzyme iduronate-2-sulfatase (IDS), which results in the lysosomal accumulation of glycosaminoglycans (GAG) such as dermatan and heparan sulfate. Dermatan Sulfate 236-244 iduronate 2-sulfatase Homo sapiens 127-148 20652491-1 2010 Mucopolysaccharidosis type II (MPS II; Hunter syndrome) is an X-linked inherited disorder caused by a deficiency of the enzyme iduronate-2-sulfatase (IDS), which results in the lysosomal accumulation of glycosaminoglycans (GAG) such as dermatan and heparan sulfate. Dermatan Sulfate 236-244 iduronate 2-sulfatase Homo sapiens 150-153 20162367-0 2010 Dermatan sulfate and heparan sulfate as a biomarker for mucopolysaccharidosis I. Mucopolysaccharidosis I (MPS I) is an autosomal recessive disorder caused by deficiency of alpha-L-iduronidase leading to accumulation of its catabolic substrates, dermatan sulfate (DS) and heparan sulfate (HS), in lysosomes. Dermatan Sulfate 0-16 alpha-L-iduronidase Homo sapiens 172-191 20152898-1 2010 The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI. Dermatan Sulfate 170-186 arylsulfatase B Homo sapiens 11-26 20152898-1 2010 The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI. Dermatan Sulfate 170-186 arylsulfatase B Homo sapiens 28-61 20152898-1 2010 The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI. Dermatan Sulfate 170-186 arylsulfatase B Homo sapiens 63-66 20152898-1 2010 The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI. Dermatan Sulfate 170-186 arylsulfatase B Homo sapiens 68-72 20152898-1 2010 The enzyme arylsulfatase B (N-acetylgalactosamine 4-sulfatase; ASB; ARSB), which removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate (C4S;CSA) and dermatan sulfate, has cellular effects, beyond those associated with the lysosomal storage disease mucopolysaccharidosis VI. Dermatan Sulfate 170-186 complement C4A (Rodgers blood group) Homo sapiens 157-160 20385007-10 2010 Over 130 ARSB mutations have been reported, causing absent or reduced arylsulfatase B (N-acetylgalactosamine 4-sulfatase) activity and interrupted dermatan sulfate and chondroitin sulfate degradation. Dermatan Sulfate 147-163 arylsulfatase B Homo sapiens 9-13 20001848-9 2010 However, contrasts in the mechanical properties of the MDCN tissue suggest that the dermatan sulfate chains on decorin influences the organization/maturation and resultant mechanical properties of the matrix by as an yet-unidentified regulatory mechanism. Dermatan Sulfate 84-100 decorin Mus musculus 111-118 20439988-5 2010 In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS. Dermatan Sulfate 64-66 carbohydrate sulfotransferase 15 Mus musculus 3-15 20439988-5 2010 In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS. Dermatan Sulfate 64-66 carbohydrate sulfotransferase 15 Mus musculus 107-119 20439988-5 2010 In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS. Dermatan Sulfate 219-221 carbohydrate sulfotransferase 15 Mus musculus 3-15 20439988-5 2010 In GalNAc4S-6ST-null mice, GalNAc(4,6-SO(4)) residues in CS and DS disappeared completely, indicating that GalNAc4S-6ST should be a sole enzyme responsible for the synthesis of GalNAc(4,6-SO(4)) residues in both CS and DS. Dermatan Sulfate 219-221 carbohydrate sulfotransferase 15 Mus musculus 107-119 20439988-6 2010 IdoA-GalNAc(4,6-SO(4)) units that account for approximately 40% of total disaccharide units of DS in the liver of the wild-type mice disappeared in the liver DS of GalNAc4S-6ST-null mice without reduction of IdoA content. Dermatan Sulfate 95-97 carbohydrate sulfotransferase 15 Mus musculus 164-176 20439988-6 2010 IdoA-GalNAc(4,6-SO(4)) units that account for approximately 40% of total disaccharide units of DS in the liver of the wild-type mice disappeared in the liver DS of GalNAc4S-6ST-null mice without reduction of IdoA content. Dermatan Sulfate 158-160 carbohydrate sulfotransferase 15 Mus musculus 164-176 19751987-3 2010 alpha-l-iduronidase (encoded by the IDUA gene) is a lysosomal enzyme that participates in the degradation of dermatan sulfate and heparan sulfate. Dermatan Sulfate 109-125 iduronidase, alpha-L Mus musculus 0-19 19751987-3 2010 alpha-l-iduronidase (encoded by the IDUA gene) is a lysosomal enzyme that participates in the degradation of dermatan sulfate and heparan sulfate. Dermatan Sulfate 109-125 iduronidase, alpha-L Mus musculus 36-40 20807649-3 2010 ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS). Dermatan Sulfate 292-308 carbohydrate sulfotransferase 14 Homo sapiens 64-70 19682969-1 2009 A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519). Dermatan Sulfate 178-194 arylsulfatase B Homo sapiens 103-118 19682969-1 2009 A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519). Dermatan Sulfate 178-194 arylsulfatase B Homo sapiens 122-125 19682969-1 2009 A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519). Dermatan Sulfate 196-198 arylsulfatase B Homo sapiens 103-118 19682969-1 2009 A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human fibroblasts (GM00519). Dermatan Sulfate 196-198 arylsulfatase B Homo sapiens 122-125 19682969-3 2009 ASB-deficient cells accumulate DS and CS, which may be partially hydrolyzed by other lysosomal hydrolases, with the reactions stopping if a GalNAc-4S residue is reached on the nonreducing end of the oligosaccharide. Dermatan Sulfate 31-33 arylsulfatase B Homo sapiens 0-3 19682969-7 2009 The assay measures depletion of DS/CS independently of their molecular size or processing state; in this approach, all DS- and CS-like substances accumulating in the absence of ASB activity are considered to be natural substrates of the enzyme. Dermatan Sulfate 32-34 arylsulfatase B Homo sapiens 177-180 20004762-3 2009 The CHST14 gene encodes N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1), which catalyzes 4-O sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate. Dermatan Sulfate 225-241 carbohydrate sulfotransferase 14 Homo sapiens 4-10 20004762-3 2009 The CHST14 gene encodes N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1), which catalyzes 4-O sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate. Dermatan Sulfate 225-241 carbohydrate sulfotransferase 8 Homo sapiens 24-68 20004762-3 2009 The CHST14 gene encodes N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1), which catalyzes 4-O sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate. Dermatan Sulfate 225-241 carbohydrate sulfotransferase 14 Homo sapiens 70-75 20004762-4 2009 Mass spectrometry of glycosaminoglycans from a patient"s fibroblasts revealed absence of dermatan sulfate and excess of chondroitin sulfate, showing that 4-O sulfation by CHST14 is essential for dermatan sulfate formation in vivo. Dermatan Sulfate 195-211 carbohydrate sulfotransferase 14 Homo sapiens 171-177 19337786-6 2009 Decorin, a member of the small leucine-rich proteoglycan gene family, is composed of a core protein and a dermatan/chondroitin sulfate chain. Dermatan Sulfate 106-114 decorin Mus musculus 0-7 20807649-3 2010 ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS). Dermatan Sulfate 292-308 carbohydrate sulfotransferase 8 Homo sapiens 88-132 20807649-3 2010 ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS). Dermatan Sulfate 292-308 carbohydrate sulfotransferase 14 Homo sapiens 134-139 20807649-3 2010 ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS). Dermatan Sulfate 310-312 carbohydrate sulfotransferase 14 Homo sapiens 64-70 20807649-3 2010 ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS). Dermatan Sulfate 310-312 carbohydrate sulfotransferase 8 Homo sapiens 88-132 20807649-3 2010 ATCS is caused by homozygous nonsense and missense mutations in CHST14 which encodes an N-acetylgalactosamine 4-O-sulfotransferase 1 (D4ST1) that catalyzes the 4-O-sulfation of N-acetylgalactosamine in the repeating iduronic acid-alpha-1,3-N-acetylgalactosamine disaccharide sequence to form dermatan sulfate (DS). Dermatan Sulfate 310-312 carbohydrate sulfotransferase 14 Homo sapiens 134-139 20807652-3 2010 Endothelial injury allows circulating HCII to enter the vessel wall, where it binds to DS and presumably becomes activated. Dermatan Sulfate 87-89 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 38-42 20807652-7 2010 These observations suggest that a major function of the HCII-DS system is to regulate the physiologic response to arterial injury. Dermatan Sulfate 61-63 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 56-60 19631712-10 2009 In fibrosis affected palmar fascia DS/CS proteoglycans are able to form with PDGF-BB supramolecular complexes also including other matrix components such as type III collagen and fibronectin which bind the growth factor covalently. Dermatan Sulfate 35-37 fibronectin 1 Homo sapiens 179-190 19661164-4 2009 In this study, dermatan sulfate structure was evaluated after downregulating or increasing dermatan 4-O-sulfotransferase 1 (D4ST-1) expression. Dermatan Sulfate 15-31 carbohydrate sulfotransferase 14 Homo sapiens 124-130 19661164-7 2009 Analysis of the dermatan sulfate chains showed that D4ST-1 is essential for the biosynthesis of the disulfated structure iduronic acid-2-O-sulfate-N-acetylgalactosamine-4-O-sulfate, thus confirmed to be strictly connected with the iduronic acid blocks. Dermatan Sulfate 16-32 carbohydrate sulfotransferase 14 Homo sapiens 52-58 19661164-9 2009 In conclusion, D4ST-1 is a key enzyme and is indispensable in the formation of important functional domains in dermatan sulfate and cannot be compensated by other 4-O-sulfotransferases. Dermatan Sulfate 111-127 carbohydrate sulfotransferase 14 Homo sapiens 15-21 19516009-13 2009 Increased expression of chondroitin sulfate in retina and dermatan sulfate in choroid reflects the effects of injury and fibrosis using high doses of anti-TNF-alpha. Dermatan Sulfate 58-74 tumor necrosis factor Homo sapiens 155-164 19088176-6 2009 CD16(-) NK cells bound maximally to dermatan sulfate (DS), which was diminished by enzymatic pretreatment with dermatanase and chondroitinase ABC, but not with chondroitinase ACII. Dermatan Sulfate 36-52 Fc gamma receptor IIIa Homo sapiens 0-4 19602578-1 2009 Iduronate-2-sulfatase (IDS) is a lysosomal enzyme expressed in pancreatic islets responsible for the degradation of proteoglycans such as perlecan and dermatan sulfate. Dermatan Sulfate 151-167 iduronate 2-sulfatase Homo sapiens 0-21 19602578-1 2009 Iduronate-2-sulfatase (IDS) is a lysosomal enzyme expressed in pancreatic islets responsible for the degradation of proteoglycans such as perlecan and dermatan sulfate. Dermatan Sulfate 151-167 iduronate 2-sulfatase Homo sapiens 23-26 19542224-4 2009 New partners of endostatin include glycosaminoglycans (chondroitin and dermatan sulfate), matricellular proteins (thrombospondin-1 and SPARC), collagens (I, IV, and VI), the amyloid peptide Abeta-(1-42), and transglutaminase-2. Dermatan Sulfate 71-87 collagen type XVIII alpha 1 chain Homo sapiens 16-26 19834056-5 2009 As excess heparan and dermatan sulfates inhibit type II collagen degradation by cathepsin K and the spatial overlap between cathepsin K and heparan sulfate strongly increased in MPS I mice, the build up of subepiphyseal cartilage is speculated to be a direct consequence of cathepsin K inhibition by MPS I-associated GAGs. Dermatan Sulfate 22-39 cathepsin K Mus musculus 80-91 19687302-0 2009 Dermatan sulfate epimerase 1-deficient mice have reduced content and changed distribution of iduronic acids in dermatan sulfate and an altered collagen structure in skin. Dermatan Sulfate 111-127 dermatan sulfate epimerase Mus musculus 0-28 19687302-1 2009 Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Dermatan Sulfate 107-123 dermatan sulfate epimerase Mus musculus 0-28 19687302-1 2009 Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Dermatan Sulfate 107-123 dermatan sulfate epimerase Mus musculus 30-37 19687302-1 2009 Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Dermatan Sulfate 107-123 dermatan sulfate epimerase-like Mus musculus 43-50 19687302-3 2009 The numbers of long blocks of adjacent iduronic acids are greatly decreased in skin decorin and biglycan chondroitin/dermatan sulfate, along with a parallel decrease in iduronic-2-O-sulfated-galactosamine-4-O-sulfated structures. Dermatan Sulfate 117-133 biglycan Mus musculus 96-104 19687302-6 2009 The lack of DS-epi1 affects the chondroitin/dermatan sulfate in many proteoglycans, and the consequences for skin collagen structure were initially analyzed. Dermatan Sulfate 44-60 dermatan sulfate epimerase Mus musculus 12-19 19687302-8 2009 The altered chondroitin/dermatan sulfate chains carried by decorin in skin are likely to affect collagen fibril formation and reduce the tensile strength of DS-epi1-null skin. Dermatan Sulfate 24-40 dermatan sulfate epimerase Mus musculus 157-164 19088176-6 2009 CD16(-) NK cells bound maximally to dermatan sulfate (DS), which was diminished by enzymatic pretreatment with dermatanase and chondroitinase ABC, but not with chondroitinase ACII. Dermatan Sulfate 54-56 Fc gamma receptor IIIa Homo sapiens 0-4 19152659-0 2009 FGF-10 and specific structural elements of dermatan sulfate size and sulfation promote maximal keratinocyte migration and cellular proliferation. Dermatan Sulfate 43-59 fibroblast growth factor 10 Homo sapiens 0-6 19019854-7 2009 The CCD, like the full-length ANGPTL4, binds to heparan and dermatan sulfates in surface plasmon resonance assays and inhibits endothelial cell adhesion, motility, and tubule-like formation. Dermatan Sulfate 60-77 angiopoietin like 4 Homo sapiens 30-37 19004834-7 2009 The presence of chondroitin and dermatan sulfate on CD44 standard and variant isoforms facilitates fibrin recognition. Dermatan Sulfate 32-48 CD44 molecule (Indian blood group) Homo sapiens 52-56 19152659-5 2009 Structural variants of DS between 10 and 20 disaccharides containing iduronic acid showed maximal capacity to enable FGF-10 receptor stimulation. Dermatan Sulfate 23-25 fibroblast growth factor 10 Homo sapiens 117-123 18499864-0 2008 The ligand-binding profile of HARE: hyaluronan and chondroitin sulfates A, C, and D bind to overlapping sites distinct from the sites for heparin, acetylated low-density lipoprotein, dermatan sulfate, and CS-E. Dermatan Sulfate 183-199 stabilin 2 Homo sapiens 30-34 18971786-2 2008 BACKGROUND: HCII inhibits thrombin activity by binding to dermatan sulfate and has been shown to be a novel and independent risk factor for atherosclerosis. Dermatan Sulfate 58-74 serpin family D member 1 Homo sapiens 12-16 18971786-2 2008 BACKGROUND: HCII inhibits thrombin activity by binding to dermatan sulfate and has been shown to be a novel and independent risk factor for atherosclerosis. Dermatan Sulfate 58-74 coagulation factor II, thrombin Homo sapiens 26-34 18499864-1 2008 The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products. Dermatan Sulfate 159-175 stabilin 2 Homo sapiens 46-50 18499864-1 2008 The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products. Dermatan Sulfate 159-175 stabilin 2 Homo sapiens 53-63 18499864-1 2008 The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products. Dermatan Sulfate 177-179 stabilin 2 Homo sapiens 46-50 18499864-1 2008 The hyaluronic acid receptor for endocytosis (HARE)/ Stabilin-2 is the primary systemic scavenger receptor for hyaluronan (HA), the chondroitin sulfates (CS), dermatan sulfate (DS), and nonglycosaminoglycan (GAG) ligands such as acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides, and advanced glycation end products. Dermatan Sulfate 177-179 stabilin 2 Homo sapiens 53-63 18499864-9 2008 For example, Hep binding to HARE was competed by DS, CS-E, AcLDL, and dextran sulfate, but not by other CS types, HA, dextran, or heparosan. Dermatan Sulfate 49-51 stabilin 2 Homo sapiens 28-32 18281504-0 2008 Vascular dermatan sulfate regulates the antithrombotic activity of heparin cofactor II. Dermatan Sulfate 9-25 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 67-86 18406185-1 2008 Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy syndrome) is an autosomal recessive lysosomal disorder caused by deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), which is required for the degradation of dermatan sulfate. Dermatan Sulfate 211-227 arylsulfatase B Homo sapiens 128-161 18406185-1 2008 Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy syndrome) is an autosomal recessive lysosomal disorder caused by deficiency of N-acetylgalactosamine-4-sulfatase (ARSB), which is required for the degradation of dermatan sulfate. Dermatan Sulfate 211-227 arylsulfatase B Homo sapiens 163-167 18486607-2 2008 The deficiency of ARSB leads to an accumulation of dermatan sulfate (DS) in lysosomes and gross excretion in the urine. Dermatan Sulfate 51-67 arylsulfatase B Homo sapiens 18-22 18486607-2 2008 The deficiency of ARSB leads to an accumulation of dermatan sulfate (DS) in lysosomes and gross excretion in the urine. Dermatan Sulfate 69-71 arylsulfatase B Homo sapiens 18-22 18413232-0 2008 Plasma kallikrein is activated on dermatan sulfate and cleaves factor H. Dermatan Sulfate 34-50 kallikrein B1 Homo sapiens 0-17 18413232-1 2008 When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem. Dermatan Sulfate 34-50 complement factor H Homo sapiens 125-133 18413232-1 2008 When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem. Dermatan Sulfate 34-50 complement factor H Homo sapiens 169-177 18413232-1 2008 When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem. Dermatan Sulfate 183-199 complement factor H Homo sapiens 125-133 18413232-1 2008 When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem. Dermatan Sulfate 183-199 complement factor H Homo sapiens 169-177 18413232-1 2008 When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem. Dermatan Sulfate 183-199 complement factor H Homo sapiens 125-133 18413232-1 2008 When human plasma is applied to a dermatan sulfate column, amidase activity is detected in the bound fraction and complement factor H is cleaved [A. Saito, H. Munakata, Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H, J. Biochem. Dermatan Sulfate 183-199 complement factor H Homo sapiens 169-177 19707363-1 2008 Mucopolysaccharidosis type II (MPS II, Hunter syndrome) is a heterogeneous, progressive X-linked recessively inherited lysosomal storage disease that is caused by a deficiency of the enzyme iduronate-2-sulfatase, resulting in abnormal tissue accumulation of the glycosaminoglycans, dermatan sulfate and heparan sulfate. Dermatan Sulfate 282-298 iduronate 2-sulfatase Homo sapiens 190-211 18281504-2 2008 Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo. Dermatan Sulfate 0-16 coagulation factor II Mus musculus 82-90 18281504-2 2008 Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo. Dermatan Sulfate 0-16 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 94-98 18281504-2 2008 Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo. Dermatan Sulfate 0-16 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 207-211 18281504-2 2008 Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo. Dermatan Sulfate 18-20 coagulation factor II Mus musculus 82-90 18281504-2 2008 Dermatan sulfate (DS) and heparan sulfate (HS) increase the rate of inhibition of thrombin by HCII in vitro, but it is unknown whether vascular glycosaminoglycans play a role in the antithrombotic effect of HCII in vivo. Dermatan Sulfate 18-20 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 94-98 18281504-4 2008 When HCII was incubated with frozen sections of the mouse carotid artery, it bound specifically to DS in the adventitia. Dermatan Sulfate 99-101 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 5-9 18281504-6 2008 These results support the hypothesis that HCII interacts with DS in the vessel wall after disruption of the endothelium and that this interaction regulates thrombus formation in vivo. Dermatan Sulfate 62-64 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 42-46 17672828-1 2008 MPS VI (mucopolysaccharidosis type VI) is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase [ASB (arylsulfatase B)] impairs the stepwise degradation of the GAG (glycosaminoglycan) dermatan sulfate. Dermatan Sulfate 234-250 arylsulfatase B Homo sapiens 112-145 17672828-1 2008 MPS VI (mucopolysaccharidosis type VI) is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase [ASB (arylsulfatase B)] impairs the stepwise degradation of the GAG (glycosaminoglycan) dermatan sulfate. Dermatan Sulfate 234-250 arylsulfatase B Homo sapiens 147-150 17672828-1 2008 MPS VI (mucopolysaccharidosis type VI) is a lysosomal storage disease in which deficient activity of the enzyme N-acetylgalactosamine 4-sulfatase [ASB (arylsulfatase B)] impairs the stepwise degradation of the GAG (glycosaminoglycan) dermatan sulfate. Dermatan Sulfate 234-250 arylsulfatase B Homo sapiens 152-167 18156656-1 2008 Dermatan sulfate is a glycosaminoglycan that selectively inhibits the action of thrombin through interaction with heparin cofactor II. Dermatan Sulfate 0-16 coagulation factor II, thrombin Bos taurus 80-88 18156656-1 2008 Dermatan sulfate is a glycosaminoglycan that selectively inhibits the action of thrombin through interaction with heparin cofactor II. Dermatan Sulfate 0-16 serpin family D member 1 Bos taurus 114-133 18156656-4 2008 Previous studies have showed that dermatan sulfate derived from porcine/bovine intestinal mucosa/skin or marine invertebrates is capable of stimulating heparin cofactor II-mediated thrombin inhibition in vitro. Dermatan Sulfate 34-50 serpin family D member 1 Bos taurus 152-171 18156656-4 2008 Previous studies have showed that dermatan sulfate derived from porcine/bovine intestinal mucosa/skin or marine invertebrates is capable of stimulating heparin cofactor II-mediated thrombin inhibition in vitro. Dermatan Sulfate 34-50 coagulation factor II, thrombin Bos taurus 181-189 18156656-7 2008 Heparin cofactor II/dermatan sulfate-mediated thrombin inhibition measured in vitro revealed activity comparable to or higher than the commercial standard with 2-fold differences observed between some tissues. Dermatan Sulfate 20-36 serpin family D member 1 Bos taurus 0-19 18156656-7 2008 Heparin cofactor II/dermatan sulfate-mediated thrombin inhibition measured in vitro revealed activity comparable to or higher than the commercial standard with 2-fold differences observed between some tissues. Dermatan Sulfate 20-36 coagulation factor II, thrombin Bos taurus 46-54 18446715-2 2008 Unlike unfractionated heparin (UFH), DS selectively inhibits thrombin, does not inhibit factor Xa, is effective on both free and fibrin-bound thrombin and does not interfere with platelets. Dermatan Sulfate 37-39 coagulation factor II, thrombin Homo sapiens 61-69 18446715-2 2008 Unlike unfractionated heparin (UFH), DS selectively inhibits thrombin, does not inhibit factor Xa, is effective on both free and fibrin-bound thrombin and does not interfere with platelets. Dermatan Sulfate 37-39 coagulation factor II, thrombin Homo sapiens 142-150 17955027-1 2008 Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement. Dermatan Sulfate 132-148 arylsulfatase B Rattus norvegicus 69-84 17706452-5 2008 Heparin capably restored their growth, and unexpectedly exogenous chondroitin sulfate to WM9 and both chondroitin sulfate and dermatan sulfate to M5 cells allowed FGF-2 mitogenic stimulation. Dermatan Sulfate 126-142 fibroblast growth factor 2 Homo sapiens 163-168 17706452-6 2008 Furthermore, in WM9 cells the degradation of membrane-bound chondroitin/dermatan sulfate stimulates basal growth and even enhances FGF-2 stimulation. Dermatan Sulfate 72-88 fibroblast growth factor 2 Homo sapiens 131-136 17706452-8 2008 Both the amounts of chondroitin/dermatan/heparan sulfate and their sulfation levels differed between the cell lines and were distinctly modulated by FGF-2. Dermatan Sulfate 32-40 fibroblast growth factor 2 Homo sapiens 149-154 17706452-9 2008 In this study, we show that chondroitin/dermatan sulfate-containing proteoglycans, likely in cooperation with heparan sulfate, participate in metastatic melanoma cell FGF-2-induced mitogenic response, which represents a novel finding and establishes the central role of sulfated glycosaminoglycans on melanoma growth. Dermatan Sulfate 40-56 fibroblast growth factor 2 Homo sapiens 167-172 17955027-1 2008 Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement. Dermatan Sulfate 132-148 arylsulfatase B Rattus norvegicus 86-90 17955027-1 2008 Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement. Dermatan Sulfate 150-152 arylsulfatase B Rattus norvegicus 69-84 17955027-1 2008 Mucopolysaccharidosis VI (MPS VI) is caused by deficient activity of arylsulfatase B (ARSB), resulting in intralysosomal storage of dermatan sulfate (DS) and multisystem disease without central nervous system involvement. Dermatan Sulfate 150-152 arylsulfatase B Rattus norvegicus 86-90 17878401-1 2007 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin. Dermatan Sulfate 84-100 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 0-19 17936880-1 2008 INTRODUCTION: Dermatan sulfate, a sulfated glycosaminoglycan, acts as an anticoagulant by accelerating the inhibition of thrombin by heparin cofactor II. Dermatan Sulfate 14-30 coagulation factor II Rattus norvegicus 121-129 17936880-1 2008 INTRODUCTION: Dermatan sulfate, a sulfated glycosaminoglycan, acts as an anticoagulant by accelerating the inhibition of thrombin by heparin cofactor II. Dermatan Sulfate 14-30 serpin family D member 1 Rattus norvegicus 133-152 17936880-4 2008 RESULTS: After a single intravenous administration of low molecular dermatan sulfate in rats, fibrinolytic activity increased simultaneously with thrombin clotting time prolongation. Dermatan Sulfate 68-84 coagulation factor II Rattus norvegicus 146-154 17878401-1 2007 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin. Dermatan Sulfate 84-100 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 21-25 17878401-1 2007 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin. Dermatan Sulfate 84-100 coagulation factor II Mus musculus 61-69 17616540-1 2007 Hunter syndrome (or Mucopolysaccharidosis type II, MPS II) is an X-linked recessive disorder due to the deficiency of the iduronate-2-sulfatase (IDS) enzyme, resulting in the accumulation of heparan and dermatan sulfates in the lysosomes. Dermatan Sulfate 203-220 iduronate 2-sulfatase Homo sapiens 122-143 17616540-1 2007 Hunter syndrome (or Mucopolysaccharidosis type II, MPS II) is an X-linked recessive disorder due to the deficiency of the iduronate-2-sulfatase (IDS) enzyme, resulting in the accumulation of heparan and dermatan sulfates in the lysosomes. Dermatan Sulfate 203-220 iduronate 2-sulfatase Homo sapiens 145-148 16650906-1 2007 BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor. Dermatan Sulfate 82-98 serpin family D member 1 Homo sapiens 12-31 17474085-9 2007 We also showed for the first time that AS-A had a specific affinity for chondroitin sulfate B, a component of cumulus matrix proteoglycan networks; this might provide a mechanism of cumulus matrix destabilization induced by sperm surface AS-A. Dermatan Sulfate 72-93 arylsulfatase A Mus musculus 39-43 17474085-9 2007 We also showed for the first time that AS-A had a specific affinity for chondroitin sulfate B, a component of cumulus matrix proteoglycan networks; this might provide a mechanism of cumulus matrix destabilization induced by sperm surface AS-A. Dermatan Sulfate 72-93 arylsulfatase A Mus musculus 238-242 17500059-4 2007 Evaluation of the specificity of GD3G7 toward various glycosaminoglycan preparations showed that this antibody specifically reacted with squid CS-E (rich in the GlcUAbeta1-3GalNAc(4,6-O-sulfate) disaccharide unit E), hagfish CS-H (rich in the IdoUAalpha1-3GalNAc(4,6-O-sulfate) unit iE), and shark skin DS (rich in both E and iE units). Dermatan Sulfate 303-305 cystathionase (cystathionine gamma-lyase) Mus musculus 143-147 17459751-1 2007 Mucopolysaccharidosis II (MPS II; Hunter syndrome) is an X-linked metabolic disorder caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase (I2S), which catalyzes the catabolism of glycosaminoglycans (GAG) by cleaving the O-linked sulfate from dermatan sulfate and heparan sulfate. Dermatan Sulfate 258-274 iduronate 2-sulfatase Mus musculus 132-153 17459751-1 2007 Mucopolysaccharidosis II (MPS II; Hunter syndrome) is an X-linked metabolic disorder caused by a deficiency of the lysosomal enzyme iduronate-2-sulfatase (I2S), which catalyzes the catabolism of glycosaminoglycans (GAG) by cleaving the O-linked sulfate from dermatan sulfate and heparan sulfate. Dermatan Sulfate 258-274 iduronate 2-sulfatase Mus musculus 155-158 17324393-4 2007 Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken. Dermatan Sulfate 132-148 arylsulfatase B Homo sapiens 17-32 17324393-4 2007 Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken. Dermatan Sulfate 132-148 arylsulfatase B Homo sapiens 34-37 17324393-4 2007 Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken. Dermatan Sulfate 132-148 arylsulfatase B Homo sapiens 193-196 17324393-4 2007 Since the enzyme arylsulfatase B (ASB) catalyzes hydrolysis of the sulfate ester of N-acetylgalactosamine 4-sulfate, a component of dermatan sulfate and chondroitin A sulfate, determination of ASB activity in human airway epithelial cells, corrected and uncorrected for CFTR, was undertaken. Dermatan Sulfate 132-148 CF transmembrane conductance regulator Homo sapiens 270-274 17239341-2 2007 In the present study, DS demonstrated a high level of binding activity to receptor activator of NF-kappaB ligand (RANKL) and obstructed the binding of RANK to RANKL, determined using a quartz-crystal microbalance (QCM) technique. Dermatan Sulfate 22-24 tumor necrosis factor (ligand) superfamily, member 11 Mus musculus 114-119 17239341-2 2007 In the present study, DS demonstrated a high level of binding activity to receptor activator of NF-kappaB ligand (RANKL) and obstructed the binding of RANK to RANKL, determined using a quartz-crystal microbalance (QCM) technique. Dermatan Sulfate 22-24 tumor necrosis factor (ligand) superfamily, member 11 Mus musculus 159-164 17239341-4 2007 In addition, immunoblot analyses revealed that DS reduced the levels of phosphorylation of p38 mitogen-activated protein kinase and extracellular signal-regulated kinase protein in mouse osteoclast progenitor cells stimulated with RANKL. Dermatan Sulfate 47-49 tumor necrosis factor (ligand) superfamily, member 11 Mus musculus 231-236 17239341-5 2007 Together, these results indicate that DS regulates osteoclast formation through binding to RANKL and inhibition of signal transduction in osteoclast progenitor cells, suggesting that it has an important role in bone metabolism in pathological conditions. Dermatan Sulfate 38-40 tumor necrosis factor (ligand) superfamily, member 11 Mus musculus 91-96 18174963-1 2007 Hunter syndrome (mucopolysaccharidosis II, MPS II) is a rare X-linked lysosomal storage disorder caused by the deficiency of enzyme iduronate-2-sulfatase (I2S), which results in accumulation of undegraded dermatan and heparan sulfate in various tissues and organs. Dermatan Sulfate 205-213 iduronate 2-sulfatase Homo sapiens 132-153 18174963-1 2007 Hunter syndrome (mucopolysaccharidosis II, MPS II) is a rare X-linked lysosomal storage disorder caused by the deficiency of enzyme iduronate-2-sulfatase (I2S), which results in accumulation of undegraded dermatan and heparan sulfate in various tissues and organs. Dermatan Sulfate 205-213 iduronate 2-sulfatase Homo sapiens 155-158 17876721-2 2007 I2S catalyses a step in the catabolism of glycosaminoglycans (GAGs) dermatan sulfate and heparan sulfate, and when it is deficient or absent GAGs accumulate in tissues and organs. Dermatan Sulfate 68-84 iduronate 2-sulfatase Homo sapiens 0-3 17928217-3 2007 Hybrid chondroitin/dermatan sulfate chains are also involved in formation of the neural network by capturing and presenting heparin-binding growth factors like basic fibroblast growth factor, pleiotrophin, and hepatocyte growth factor to stem cells or neuronal cells. Dermatan Sulfate 19-35 pleiotrophin Homo sapiens 192-204 17928217-3 2007 Hybrid chondroitin/dermatan sulfate chains are also involved in formation of the neural network by capturing and presenting heparin-binding growth factors like basic fibroblast growth factor, pleiotrophin, and hepatocyte growth factor to stem cells or neuronal cells. Dermatan Sulfate 19-35 hepatocyte growth factor Homo sapiens 210-234 17239341-0 2007 Dermatan sulfate inhibits osteoclast formation by binding to receptor activator of NF-kappa B ligand. Dermatan Sulfate 0-16 tumor necrosis factor (ligand) superfamily, member 11 Mus musculus 61-100 17239341-2 2007 In the present study, DS demonstrated a high level of binding activity to receptor activator of NF-kappaB ligand (RANKL) and obstructed the binding of RANK to RANKL, determined using a quartz-crystal microbalance (QCM) technique. Dermatan Sulfate 22-24 tumor necrosis factor (ligand) superfamily, member 11 Mus musculus 74-112 17194895-1 2007 Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures. Dermatan Sulfate 314-330 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 0-19 17194895-1 2007 Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures. Dermatan Sulfate 314-330 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 21-25 17194895-1 2007 Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures. Dermatan Sulfate 314-330 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 213-217 17194895-1 2007 Heparin cofactor II (HCII) has several biochemical properties that distinguish it from other serpins: (1) it specifically inhibits thrombin; (2) the mechanism of inhibition involves binding of an acidic domain in HCII to thrombin exosite I; and (3) the rate of inhibition increases dramatically in the presence of dermatan sulfate molecules having specific structures. Dermatan Sulfate 314-330 coagulation factor II Mus musculus 221-229 17194895-3 2007 Studies with HCII knockout mice directly support the hypothesis that HCII interacts with dermatan sulfate in the arterial wall after endothelial injury and thereby exerts an antithrombotic effect. Dermatan Sulfate 89-105 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 13-17 17194895-3 2007 Studies with HCII knockout mice directly support the hypothesis that HCII interacts with dermatan sulfate in the arterial wall after endothelial injury and thereby exerts an antithrombotic effect. Dermatan Sulfate 89-105 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 69-73 17158902-2 2007 Alternatively spliced forms of CD97 bind integrins alpha5beta1 and alphavbeta3, decay accelerating factor, or dermatan sulfate. Dermatan Sulfate 110-126 adhesion G protein-coupled receptor E5 Mus musculus 31-35 16650906-1 2007 BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor. Dermatan Sulfate 82-98 serpin family D member 1 Homo sapiens 33-37 16650906-1 2007 BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor. Dermatan Sulfate 82-98 coagulation factor II, thrombin Homo sapiens 56-64 16690200-6 2006 Tumor-associated glycanated decorin was found to contain significant amounts of dermatan sulfate (DS) sequences. Dermatan Sulfate 80-96 decorin Homo sapiens 28-35 17222891-6 2007 In the presence of HCII, DSb, a slightly oversulfated DS, had the highest inhibitory effect, whereas heparin and DSd, the most oversulfated derivative, had lower potencies in this case. Dermatan Sulfate 25-27 serpin family D member 1 Homo sapiens 19-23 17222891-7 2007 These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII. Dermatan Sulfate 100-102 coagulation factor II, thrombin Homo sapiens 42-50 17222891-7 2007 These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII. Dermatan Sulfate 100-102 coagulation factor II, thrombin Homo sapiens 157-165 17222891-7 2007 These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII. Dermatan Sulfate 100-102 serpin family D member 1 Homo sapiens 188-192 17270255-1 2007 INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action. Dermatan Sulfate 14-30 serpin family C member 1 Homo sapiens 131-143 17270255-1 2007 INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action. Dermatan Sulfate 32-34 serpin family C member 1 Homo sapiens 131-143 17270255-8 2007 The facilitation of the conversion of Glu-plasminogen to plasmin in the presence of DS was confirmed by SDS-PAGE; high molecular weight-DS effect was greater than low molecular weight-DS in accordance with the chromogenic assays. Dermatan Sulfate 84-86 plasminogen Homo sapiens 42-49 16690200-6 2006 Tumor-associated glycanated decorin was found to contain significant amounts of dermatan sulfate (DS) sequences. Dermatan Sulfate 98-100 decorin Homo sapiens 28-35 16583246-3 2006 Compound heterozygous mutations in the B4GALT7 gene, resulting in aberrant glycosylation of the dermatan sulfate proteoglycan decorin, had been described in a single patient affected with the progeroid form of EDS. Dermatan Sulfate 96-112 beta-1,4-galactosyltransferase 7 Homo sapiens 39-46 16961606-10 2006 Additionally, odiparcil-induced heparin cofactor II (HCII)-dependent antithrombin activity was shown to be a function of dermatan sulfate-like GAG production. Dermatan Sulfate 121-137 serpin family D member 1 Rattus norvegicus 32-51 16961606-10 2006 Additionally, odiparcil-induced heparin cofactor II (HCII)-dependent antithrombin activity was shown to be a function of dermatan sulfate-like GAG production. Dermatan Sulfate 121-137 serpin family D member 1 Rattus norvegicus 53-57 16828054-5 2006 GAGs from different structure/origin (heparan sulfate, dermatan sulfate, and chondroitin sulfate) exert similar activity on OPG binding. Dermatan Sulfate 55-71 TNF receptor superfamily member 11b Homo sapiens 124-127 16899604-1 2006 PURPOSE: We evaluated the expression of endocan, a soluble lung- and kidney-selective endothelial cell-specific dermatan sulfate proteoglycan, in non-small cell lung tumors compared with normal lung and studied the significance of high levels of circulating endocan in patients with non-small cell lung cancer. Dermatan Sulfate 112-128 endothelial cell specific molecule 1 Homo sapiens 40-47 16624894-0 2006 N-Acetylgalactosamine 4,6-O-sulfate residues mediate binding and activation of heparin cofactor II by porcine mucosal dermatan sulfate. Dermatan Sulfate 118-134 serpin family D member 1 Homo sapiens 79-98 16624894-1 2006 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 0-16 coagulation factor II, thrombin Homo sapiens 52-60 16624894-1 2006 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 0-16 serpin family D member 1 Homo sapiens 64-83 16624894-1 2006 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 0-16 serpin family D member 1 Homo sapiens 85-89 16624894-1 2006 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 18-20 coagulation factor II, thrombin Homo sapiens 52-60 16624894-1 2006 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 18-20 serpin family D member 1 Homo sapiens 64-83 16624894-1 2006 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 18-20 serpin family D member 1 Homo sapiens 85-89 16624894-3 2006 DS from porcine intestinal mucosa has a much lower content of this disaccharide but activates HCII with potency similar to that of porcine skin DS. Dermatan Sulfate 0-2 serpin family D member 1 Homo sapiens 94-98 16624894-4 2006 Therefore, we sought to characterize oligosaccharides from porcine mucosal DS that interact with HCII. Dermatan Sulfate 75-77 serpin family D member 1 Homo sapiens 97-101 16624894-11 2006 These data support the hypothesis that modification of IdoA-->GalNAc4SO3 subunits in the DS polymer by either 2-O-sulfation of IdoA or 6-O-sulfation of GalNAc can generate molecules with HCII-binding sites and anticoagulant activity. Dermatan Sulfate 92-94 serpin family D member 1 Homo sapiens 190-194 16583246-8 2006 Glycosaminoglycan chains were of the dermatan/chondroitin sulfate type both in beta4GalT-7(Arg270Cys) and control cells, and epimerization was reduced for decorin and biglycan. Dermatan Sulfate 37-45 beta-1,4-galactosyltransferase 7 Homo sapiens 79-90 16489125-3 2006 The biological activities of DS have been attributed to its high content of IdoA(alpha1-3)GalNAc4S(beta1-4) disaccharide units. Dermatan Sulfate 29-31 adrenoceptor alpha 1D Homo sapiens 81-89 16489125-3 2006 The biological activities of DS have been attributed to its high content of IdoA(alpha1-3)GalNAc4S(beta1-4) disaccharide units. Dermatan Sulfate 29-31 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 99-106 16168566-1 2006 Endocan, previously called endothelial cell specific molecule-1, is a soluble proteoglycan of 50 kDa, constituted of a mature polypeptide of 165 amino acids and a single dermatan sulphate chain covalently linked to the serine residue at position 137. Dermatan Sulfate 170-187 endothelial cell specific molecule 1 Homo sapiens 0-7 16442510-0 2006 Thrombin inhibition by antithrombin in the presence of oversulfated dermatan sulfates. Dermatan Sulfate 68-85 coagulation factor II, thrombin Homo sapiens 0-8 16442510-0 2006 Thrombin inhibition by antithrombin in the presence of oversulfated dermatan sulfates. Dermatan Sulfate 68-85 serpin family C member 1 Homo sapiens 23-35 16442510-1 2006 DSS1 and DSS2 are two oversulfated dermatan sulfate derivatives with sulfur contents of 7.8% and 11.5%, respectively. Dermatan Sulfate 35-51 SEM1 26S proteasome subunit Homo sapiens 0-4 16339402-0 2006 Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II. Dermatan Sulfate 10-26 serpin family D member 1 Homo sapiens 84-103 16339402-4 2006 Dermatan sulfate (DS) specifically activates HCII and is abundant in the placenta, but the locations of DS and HCII in the placenta have not been determined. Dermatan Sulfate 0-16 serpin family D member 1 Homo sapiens 45-49 16339402-4 2006 Dermatan sulfate (DS) specifically activates HCII and is abundant in the placenta, but the locations of DS and HCII in the placenta have not been determined. Dermatan Sulfate 18-20 serpin family D member 1 Homo sapiens 45-49 16339402-6 2006 DS isolated from human placenta contains disaccharides implicated in activation of HCII and has anticoagulant activity similar to that of mucosal DS. Dermatan Sulfate 0-2 serpin family D member 1 Homo sapiens 83-87 16339402-8 2006 HCII colocalizes with DS in the walls of fetal blood vessels and is also present in syncytiotrophoblast cells. Dermatan Sulfate 22-24 serpin family D member 1 Homo sapiens 0-4 16339402-9 2006 Our data suggest that DS is in a position to activate HCII in the fetal blood vessels or in the stroma of placental villi after injury to the syncytiotrophoblast layer and thereby inhibit fibrin generation in the placenta. Dermatan Sulfate 22-24 serpin family D member 1 Homo sapiens 54-58 16533727-7 2006 In particular, the addition of DS resulted in increases of about 1.3-fold, 1.6-fold and 2.0-fold in the numbers of total cells, megakaryocytes and CFU-Meg, respectively, compared with the control culture stimulated by thrombopoietin alone after 9-12 days of serum-free liquid culture. Dermatan Sulfate 31-33 protein tyrosine phosphatase non-receptor type 4 Homo sapiens 151-154 16533727-7 2006 In particular, the addition of DS resulted in increases of about 1.3-fold, 1.6-fold and 2.0-fold in the numbers of total cells, megakaryocytes and CFU-Meg, respectively, compared with the control culture stimulated by thrombopoietin alone after 9-12 days of serum-free liquid culture. Dermatan Sulfate 31-33 thrombopoietin Homo sapiens 218-232 16674280-7 2006 Keratinocytes stained positive for PCNA (proliferation), K10 (suprabasal differentiation), and K16 (hyperproliferation) markers although cell morphology was poor for organotypical cultures on dermatan- loaded polypyrrole compared with de-epidermalized dermis. Dermatan Sulfate 192-200 keratin 16 Homo sapiens 95-98 16505484-0 2006 Biosynthesis of dermatan sulfate: chondroitin-glucuronate C5-epimerase is identical to SART2. Dermatan Sulfate 16-32 dermatan sulfate epimerase Homo sapiens 87-92 16505484-11 2006 NCAG1 also contains a putative chondroitin sulfate sulfotransferase domain and thus may be involved in dermatan sulfate biosynthesis. Dermatan Sulfate 103-119 dermatan sulfate epimerase like Homo sapiens 0-5 16168566-1 2006 Endocan, previously called endothelial cell specific molecule-1, is a soluble proteoglycan of 50 kDa, constituted of a mature polypeptide of 165 amino acids and a single dermatan sulphate chain covalently linked to the serine residue at position 137. Dermatan Sulfate 170-187 endothelial cell specific molecule 1 Homo sapiens 27-63 16120610-0 2005 Demonstration of the pleiotrophin-binding oligosaccharide sequences isolated from chondroitin sulfate/dermatan sulfate hybrid chains of embryonic pig brains. Dermatan Sulfate 102-118 pleiotrophin Mus musculus 21-33 16394262-6 2006 In addition, dermatan sulfate induces ICAM-1 expression on endothelial cells and also recruits leukocytes via selectin interactions. Dermatan Sulfate 13-29 intercellular adhesion molecule 1 Homo sapiens 38-44 16303928-9 2005 CONCLUSIONS: Opticin binds to heparin, HS, chondroitin 4-sulfate, and dermatan sulfate, the binding affinity being dependent on sulfation pattern and oligosaccharide chain length. Dermatan Sulfate 70-86 opticin Homo sapiens 13-20 16283671-3 2005 MPS type I (MPS I) is caused by low or undetectable activity of alpha-L-iduronidase, an enzyme involved in removing the terminal iduronic acid residues from heparan and dermatan sulfate. Dermatan Sulfate 169-185 alpha-L-iduronidase Homo sapiens 64-83 16120610-2 2005 CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor. Dermatan Sulfate 3-5 pleiotrophin Mus musculus 162-174 16120610-2 2005 CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor. Dermatan Sulfate 3-5 pleiotrophin Mus musculus 176-179 16120610-2 2005 CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor. Dermatan Sulfate 54-56 pleiotrophin Mus musculus 162-174 16120610-2 2005 CS/DS chains isolated from embryonic pig brains (E-CS/DS) promote the outgrowth of neurites in embryonic mouse hippocampal neurons in culture by interacting with pleiotrophin (PTN), a heparin-binding growth factor. Dermatan Sulfate 54-56 pleiotrophin Mus musculus 176-179 16120610-3 2005 Here, we analyzed oligosaccharides isolated from E-CS/DS, which showed that octasaccharides were the minimal size capable of interacting with PTN at a physiological salt concentration. Dermatan Sulfate 54-56 pleiotrophin Sus scrofa 142-145 16120610-8 2005 Thus, chain size and composition are crucial to the interaction with PTN, and PTN binds to multiple sequences in E-CS/DS chains with distinct affinity. Dermatan Sulfate 118-120 pleiotrophin Sus scrofa 78-81 16120610-9 2005 Notably, not only heparan sulfate but also CS/DS hybrid chain structures of mammalian brains contain a high degree of microheterogeneity with a cluster of oversulfated disaccharides and appear to play roles in regulating the functions of PTN. Dermatan Sulfate 46-48 pleiotrophin Homo sapiens 238-241 15854029-3 2005 Integrins alpha4beta1, alpha5beta1, and alphavbeta3 and dermatan sulfate CD44 were required for this invasive migration. Dermatan Sulfate 56-72 CD44 molecule (Indian blood group) Homo sapiens 73-77 15947088-1 2005 In mucopolysaccharidosis-I (MPS-I), alpha-L-iduronidase deficiency leads to progressive heparan sulfate (HS) and dermatan sulfate (DS) glycosaminoglycan (GAG) accumulation. Dermatan Sulfate 113-129 alpha-L-iduronidase Homo sapiens 36-55 15947088-1 2005 In mucopolysaccharidosis-I (MPS-I), alpha-L-iduronidase deficiency leads to progressive heparan sulfate (HS) and dermatan sulfate (DS) glycosaminoglycan (GAG) accumulation. Dermatan Sulfate 131-133 alpha-L-iduronidase Homo sapiens 36-55 15563459-0 2005 Structural and sequence motifs in dermatan sulfate for promoting fibroblast growth factor-2 (FGF-2) and FGF-7 activity. Dermatan Sulfate 34-50 fibroblast growth factor 2 Homo sapiens 65-91 15500445-2 2005 IDS (iduronate-2-sulphatase; EC 3.1.6.13) is a lysosomal exo-sulphatase that belongs to this protein family and is involved in the degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate. Dermatan Sulfate 190-207 iduronate 2-sulfatase Homo sapiens 0-3 15500445-2 2005 IDS (iduronate-2-sulphatase; EC 3.1.6.13) is a lysosomal exo-sulphatase that belongs to this protein family and is involved in the degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate. Dermatan Sulfate 190-207 iduronate 2-sulfatase Homo sapiens 5-27 15563459-0 2005 Structural and sequence motifs in dermatan sulfate for promoting fibroblast growth factor-2 (FGF-2) and FGF-7 activity. Dermatan Sulfate 34-50 fibroblast growth factor 2 Homo sapiens 93-98 15563459-0 2005 Structural and sequence motifs in dermatan sulfate for promoting fibroblast growth factor-2 (FGF-2) and FGF-7 activity. Dermatan Sulfate 34-50 fibroblast growth factor 7 Homo sapiens 104-109 15563459-5 2005 Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process. Dermatan Sulfate 0-16 fibroblast growth factor 2 Homo sapiens 101-127 15563459-5 2005 Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process. Dermatan Sulfate 0-16 fibroblast growth factor 2 Homo sapiens 129-134 15563459-5 2005 Dermatan sulfate is abundant in the wound environment and binds and activates growth factors such as fibroblast growth factor-2 (FGF-2) and FGF-7, which are present during the wound repair process. Dermatan Sulfate 0-16 fibroblast growth factor 7 Homo sapiens 140-145 15693006-11 2005 Dermatan sulfate was shown to be the ligand of the largest isoforms of EMR2 and CD97 in rheumatoid synovium. Dermatan Sulfate 0-16 adhesion G protein-coupled receptor E2 Homo sapiens 71-75 15693006-11 2005 Dermatan sulfate was shown to be the ligand of the largest isoforms of EMR2 and CD97 in rheumatoid synovium. Dermatan Sulfate 0-16 adhesion G protein-coupled receptor E5 Homo sapiens 80-84 15693006-13 2005 CONCLUSION: The EGF-TM7 receptors EMR2 and CD97 are abundantly expressed on myeloid cells in ST of RA patients where their cognate ligands dermatan sulfate and CD55 are detected. Dermatan Sulfate 139-155 adhesion G protein-coupled receptor E2 Homo sapiens 34-38 15693006-13 2005 CONCLUSION: The EGF-TM7 receptors EMR2 and CD97 are abundantly expressed on myeloid cells in ST of RA patients where their cognate ligands dermatan sulfate and CD55 are detected. Dermatan Sulfate 139-155 adhesion G protein-coupled receptor E5 Homo sapiens 43-47 15315969-1 2004 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin. Dermatan Sulfate 97-113 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 0-19 16435196-1 2005 Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI) is an autosomal recessive disorder caused by deficiency of N-acetylgalactosamine-4-sulphatase (ARSB),which leads to the lysosomal accumulation and excretion of dermatan sulphate (DS). Dermatan Sulfate 224-241 arylsulfatase B Homo sapiens 159-163 16435196-1 2005 Mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome, MPS VI) is an autosomal recessive disorder caused by deficiency of N-acetylgalactosamine-4-sulphatase (ARSB),which leads to the lysosomal accumulation and excretion of dermatan sulphate (DS). Dermatan Sulfate 243-245 arylsulfatase B Homo sapiens 159-163 16435198-2 2005 The deficiency of alpha-L-iduronidase (EC 1.2.3.76), one of the enzymes responsible for the degradation of glycosaminoglycans, results in accumulation of heparan and dermatan sulphate in these patients. Dermatan Sulfate 166-183 alpha-L-iduronidase Homo sapiens 18-37 16038721-2 2005 The rate of inactivation of thrombin by heparin cofactor II is increased in the presence of dermatan sulfate, which is produced by fibroblasts or smooth muscle cells. Dermatan Sulfate 92-108 coagulation factor II, thrombin Homo sapiens 28-36 15632143-0 2005 Heparin-binding growth factor, pleiotrophin, mediates neuritogenic activity of embryonic pig brain-derived chondroitin sulfate/dermatan sulfate hybrid chains. Dermatan Sulfate 127-143 pleiotrophin Sus scrofa 31-43 15632143-4 2005 Here we showed that pleiotrophin (PTN), a heparin-binding growth factor, produced mainly by glia cells, was the predominant binding partner for E-CS/DS in the membrane-associated protein fraction of neonatal rat brain. Dermatan Sulfate 149-151 pleiotrophin Rattus norvegicus 20-32 15632143-4 2005 Here we showed that pleiotrophin (PTN), a heparin-binding growth factor, produced mainly by glia cells, was the predominant binding partner for E-CS/DS in the membrane-associated protein fraction of neonatal rat brain. Dermatan Sulfate 149-151 pleiotrophin Rattus norvegicus 34-37 15632143-11 2005 Interaction analysis indicated that the 473HD epitope and PTN-binding domains in the E-CS/DS chains largely overlap. Dermatan Sulfate 90-92 pleiotrophin Sus scrofa 58-61 15632143-13 2005 Oversulfated disaccharides and nonconsecutive iduronic acid-containing units were the requirements for the E-CS/DS chains to bind PTN and to exhibit the neuritogenic activities. Dermatan Sulfate 112-114 pleiotrophin Sus scrofa 130-133 15749837-0 2005 Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H. Dermatan Sulfate 14-30 complement factor H Homo sapiens 0-8 15749837-0 2005 Factor H is a dermatan sulfate-binding protein: identification of a dermatan sulfate-mediated protease that cleaves factor H. Dermatan Sulfate 14-30 complement factor H Homo sapiens 116-124 15749837-1 2005 Dermatan sulfate mediates the blood coagulation cascade by binding to heparin cofactor II and potentiating the antithrombin activity. Dermatan Sulfate 0-16 serpin family C member 1 Homo sapiens 111-123 15749837-3 2005 When human plasma was applied on the dermatan sulfate column, factor H was bound and cleaved. Dermatan Sulfate 37-53 complement factor H Homo sapiens 62-70 15749837-7 2005 The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors. Dermatan Sulfate 17-33 complement factor H Homo sapiens 55-63 15749837-7 2005 The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors. Dermatan Sulfate 17-33 complement factor H Homo sapiens 255-263 15749837-7 2005 The finding that dermatan sulfate-mediated cleavage of factor H was inhibited by (p-amidinophenyl) methanesulfonyl fluoride, but not N-ethylmaleimide or EDTA, indicates that a serine protease in the plasma was activated on the dermatan sulfate column and factor H was cleaved without intervention of the plasma protease inhibitors. Dermatan Sulfate 227-243 complement factor H Homo sapiens 55-63 15635159-7 2005 On the other hand, SDS-polyacrylamide gel electrophoresis and Western blot analysis of the PG core proteins indicated that the Na-SP-releasable PGs are both a large heparan sulfate PG, perlecan, and a small chondroitin/dermatan sulfate PG, biglycan, without change in the size of the core proteins. Dermatan Sulfate 219-235 nuclear autoantigenic sperm protein Bos taurus 127-132 15315969-1 2004 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin. Dermatan Sulfate 97-113 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 21-25 15315969-1 2004 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin. Dermatan Sulfate 97-113 coagulation factor II Mus musculus 61-69 15315969-4 2004 Intravenous administration of porcine skin dermatan sulfate induced a dose-dependent prolongation of the carotid artery occlusion time in HCII(+/+) mice that was not observed in HCII(-/-) animals. Dermatan Sulfate 43-59 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 138-142 15315969-4 2004 Intravenous administration of porcine skin dermatan sulfate induced a dose-dependent prolongation of the carotid artery occlusion time in HCII(+/+) mice that was not observed in HCII(-/-) animals. Dermatan Sulfate 43-59 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 178-182 15315969-6 2004 Using invertebrate dermatan sulfate preparations, we showed that N-acetylgalactosamine-4-O-sulfate residues are required for the HCII-dependent antithrombotic effect. Dermatan Sulfate 19-35 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 129-133 15315969-7 2004 Furthermore, the invertebrate dermatan sulfates, which have higher charge densities than mammalian dermatan sulfate, slightly prolonged the thrombotic occlusion time of HCII(-/-) mice. Dermatan Sulfate 30-47 serpin family D member 1 Homo sapiens 169-173 15315969-7 2004 Furthermore, the invertebrate dermatan sulfates, which have higher charge densities than mammalian dermatan sulfate, slightly prolonged the thrombotic occlusion time of HCII(-/-) mice. Dermatan Sulfate 30-46 serpin family D member 1 Homo sapiens 169-173 15315969-8 2004 These results indicate that HCII mediates the antithrombotic effect of porcine skin dermatan sulfate after injury to the carotid arterial endothelium in mice, whereas more highly charged dermatan sulfates possess weak antithrombotic activity independent of HCII. Dermatan Sulfate 84-100 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 28-32 15324304-2 2004 We showed previously that C4ST-1 purified from rat chondrosarcoma and recombinant C4ST-1 both transfer sulphate efficiently to position 4 of the GalNAc residues of DSDS (desulphated dermatan sulphate). Dermatan Sulfate 182-199 carbohydrate sulfotransferase 11 Rattus norvegicus 26-32 15324304-2 2004 We showed previously that C4ST-1 purified from rat chondrosarcoma and recombinant C4ST-1 both transfer sulphate efficiently to position 4 of the GalNAc residues of DSDS (desulphated dermatan sulphate). Dermatan Sulfate 182-199 carbohydrate sulfotransferase 11 Rattus norvegicus 82-88 15203110-5 2004 Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation. Dermatan Sulfate 29-45 pleiotrophin Homo sapiens 58-62 15639191-1 2005 Mucopolysaccharidosis I is a lysosomal storage disorder caused by a deficiency of the lysosomal hydrolase alpha-l-iduronidase, which is required for the degradation of heparan sulphate and dermatan sulphate. Dermatan Sulfate 189-206 alpha-L-iduronidase Homo sapiens 106-125 15526370-0 2004 Effects of dermatan sulfate derivatives on platelet surface P-selectin expression and protein C activity in blood of inflammatory bowel disease patients. Dermatan Sulfate 11-27 selectin P Homo sapiens 60-70 15526370-1 2004 AIM: To investigate the effect of dermatan sulfate (DS) derivatives on platelet surface P-selectin expression and blood activated protein C (APC) activity in patients with inflammatory bowel disease (IBD), and to clarity the anti-inflammatory mechanism of DS derivatives. Dermatan Sulfate 34-50 selectin P Homo sapiens 88-98 15526370-1 2004 AIM: To investigate the effect of dermatan sulfate (DS) derivatives on platelet surface P-selectin expression and blood activated protein C (APC) activity in patients with inflammatory bowel disease (IBD), and to clarity the anti-inflammatory mechanism of DS derivatives. Dermatan Sulfate 52-54 selectin P Homo sapiens 88-98 15526370-6 2004 The effects of DS derivatives on P-selectin expression were assayed by ELISA method, and blood APC activity was assayed by the synthetic chromogenic substrate method. Dermatan Sulfate 15-17 selectin P Homo sapiens 33-43 15347686-9 2004 Syndecan-1 extracted from wounded mouse skin also displayed an increase in dermatan sulfate synthesis compared with unwounded skin. Dermatan Sulfate 75-91 syndecan 1 Mus musculus 0-10 15149955-1 2004 The lysosomal enzyme iduronate-2-sulfatase (IDS) is expressed in pancreatic islets and is responsible for degradation of proteoglycans, such as perlecan and dermatan sulfate. Dermatan Sulfate 157-173 iduronate 2-sulfatase Mus musculus 21-42 15203110-5 2004 Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation. Dermatan Sulfate 29-45 pleiotrophin Homo sapiens 110-114 15203110-5 2004 Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation. Dermatan Sulfate 29-45 plasminogen Homo sapiens 120-127 15148272-2 2004 Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls. Dermatan Sulfate 78-94 serpin family D member 1 Homo sapiens 8-27 15236403-1 2004 A defect of the lysosomal enzyme alpha-L-iduronidase (IDUA) interrupts heparan and dermatan sulfate degradation and causes neuropathology in children with severe forms of mucopolysaccharidosis type I (MPSI, Hurler syndrome). Dermatan Sulfate 83-99 alpha-L-iduronidase Homo sapiens 33-52 15236403-1 2004 A defect of the lysosomal enzyme alpha-L-iduronidase (IDUA) interrupts heparan and dermatan sulfate degradation and causes neuropathology in children with severe forms of mucopolysaccharidosis type I (MPSI, Hurler syndrome). Dermatan Sulfate 83-99 alpha-L-iduronidase Homo sapiens 54-58 15358546-4 2004 Both chondroitin sulfate and dermatan sulfate, in addition to heparin, were found to bind VWF equally well. Dermatan Sulfate 29-45 von Willebrand factor Homo sapiens 90-93 15148272-2 2004 Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls. Dermatan Sulfate 78-94 serpin family D member 1 Homo sapiens 29-33 15148272-2 2004 Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls. Dermatan Sulfate 78-94 coagulation factor II, thrombin Homo sapiens 44-52 15148272-2 2004 Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls. Dermatan Sulfate 78-94 serpin family D member 1 Homo sapiens 122-126 15148272-2 2004 Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls. Dermatan Sulfate 78-94 coagulation factor II, thrombin Homo sapiens 151-159 15009704-0 2004 Fibroblast invasive migration into fibronectin/fibrin gels requires a previously uncharacterized dermatan sulfate-CD44 proteoglycan. Dermatan Sulfate 97-113 fibronectin 1 Homo sapiens 35-46 14718373-2 2004 In a lysosomal storage disorder known as mucopolysaccharidosis I, caused by a deficiency of the exohydrolase alpha-l-iduronidase, fragments of two different glycosaminoglycans, dermatan sulfate and heparan sulfate, have been shown to accumulate. Dermatan Sulfate 177-193 alpha-L-iduronidase Homo sapiens 109-128 14744972-2 2004 Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action. Dermatan Sulfate 79-95 serpin family D member 1 Homo sapiens 8-27 14744972-2 2004 Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action. Dermatan Sulfate 79-95 serpin family D member 1 Homo sapiens 29-33 14744972-2 2004 Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action. Dermatan Sulfate 79-95 coagulation factor II, thrombin Homo sapiens 44-52 14744972-2 2004 Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action. Dermatan Sulfate 79-95 serpin family D member 1 Homo sapiens 143-147 14744972-2 2004 Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action. Dermatan Sulfate 79-95 coagulation factor II, thrombin Homo sapiens 193-201 15081804-1 2004 alpha-L-Iduronidase is a glycosyl hydrolase involved in the sequential degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate. Dermatan Sulfate 130-147 alpha-L-iduronidase Homo sapiens 0-19 15009704-0 2004 Fibroblast invasive migration into fibronectin/fibrin gels requires a previously uncharacterized dermatan sulfate-CD44 proteoglycan. Dermatan Sulfate 97-113 CD44 molecule (Indian blood group) Homo sapiens 114-118 15009704-5 2004 We found that dermatan sulfate was required for fibroblast migration into a fibronectin/fibrin gel. Dermatan Sulfate 14-30 fibronectin 1 Homo sapiens 76-87 14707087-3 2004 EGF-TM7 receptors bind cellular ligands as demonstrated by the interaction of CD97 with decay accelerating factor (CD55) and dermatan sulfate. Dermatan Sulfate 125-141 adhesion G protein-coupled receptor E1 Mus musculus 0-7 12799343-1 2003 Hybrid chondroitin/dermatan sulfate (CS/DS) glycosaminoglycan chains, derived from decorin secreted by human skin fibroblasts, were shown to interact with FGF-2, as did oligosaccharides derived therefrom by chondroitin B lyase digestion. Dermatan Sulfate 19-35 fibroblast growth factor 2 Homo sapiens 155-160 14704908-6 2004 RESULTS: Degradation of the samples with chondroitinases ABC, AC and B revealed that, in the aqueous humour from PEX eyes, collagen type IX and biglycan had a more dermatan sulphate than did normal eyes. Dermatan Sulfate 164-181 biglycan Homo sapiens 144-152 14634134-6 2003 The FAK-deficient mast cells had a reduction in the content of chondroitin/dermatan sulfate, the major glycosaminoglycan component of the granular matrix. Dermatan Sulfate 75-91 PTK2 protein tyrosine kinase 2 Mus musculus 4-7 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate 76-92 serpin family C member 1 Homo sapiens 214-230 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate 76-92 coagulation factor II, thrombin Homo sapiens 218-226 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate 76-92 serpin family D member 1 Homo sapiens 284-303 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate 76-92 serpin family D member 1 Homo sapiens 305-309 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate 76-92 coagulation factor II, thrombin Homo sapiens 270-278 15078125-2 2004 Although AT and HCII are structural homologs, only heparin binds to AT, and HCII has different binding sites for heparin and dermatan sulfate. Dermatan Sulfate 125-141 serpin family D member 1 Homo sapiens 76-80 15078125-3 2004 Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains. Dermatan Sulfate 179-195 serpin family D member 1 Homo sapiens 141-145 15078125-6 2004 Whereas it inactivates the binding site for AT causing a drop of the anticoagulant activity, it enhances the HCII-associated activity of both heparin and dermatan sulfate. Dermatan Sulfate 154-170 serpin family D member 1 Homo sapiens 109-113 14653390-4 2003 RESULTS: The results showed that IL-6 elicited an inhibitory effect on collagen and GAG levels in CLP fibroblasts by lowering hyaluronan and dermatan sulfate secretion. Dermatan Sulfate 141-157 interleukin 6 Homo sapiens 33-37 12933790-9 2003 The 175-kDa rHARE binds HA, dermatan sulfate, and chondroitin sulfates A, C, D, and E, but not chondroitin, heparin, heparan sulfate, or keratan sulfate. Dermatan Sulfate 28-44 stabilin 2 Rattus norvegicus 12-17 12886459-5 2003 On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Dermatan Sulfate 65-81 kallikrein related peptidase 4 Homo sapiens 110-120 12886459-4 2003 Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 microM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 microM) activation. Dermatan Sulfate 83-99 kallikrein related peptidase 4 Homo sapiens 187-197 12847091-1 2003 4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified. Dermatan Sulfate 102-104 carbohydrate sulfotransferase 14 Homo sapiens 195-201 12847091-1 2003 4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified. Dermatan Sulfate 102-104 carbohydrate sulfotransferase 11 Homo sapiens 207-249 12847091-1 2003 4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified. Dermatan Sulfate 102-104 carbohydrate sulfotransferase 11 Homo sapiens 251-264 12886459-5 2003 On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Dermatan Sulfate 65-81 serpin family C member 1 Homo sapiens 135-147 12730206-13 2003 Collectively, our results show that carbohydrate recognition domains of SP-D interact with the dermatan sulfate moiety of decorin via lectin activity and that the core protein of decorin binds the collagen-like region of SP-D in vitro, and these interactions may be operative in vivo. Dermatan Sulfate 95-111 surfactant protein D Homo sapiens 72-76 12798179-9 2003 The high sensitivity of the new method allows the determination of dermatan sulfate contaminations in a heparin raw sample down to 0.04% (w/w) and broadens the practical applicability of CE-LIF for the quantitation of the endogenous levels of glycosaminoglycans in animal samples and for pharmacokinetic control after therapeutical heparin administration. Dermatan Sulfate 67-83 LIF interleukin 6 family cytokine Homo sapiens 190-193 12796199-4 2003 Arylsulfatase B, also known as N-acetyl galactosamine 4-sulfatase, can degrade DS and chondroitin-4 sulfate. Dermatan Sulfate 79-81 arylsulfatase B Homo sapiens 0-15 12796199-4 2003 Arylsulfatase B, also known as N-acetyl galactosamine 4-sulfatase, can degrade DS and chondroitin-4 sulfate. Dermatan Sulfate 79-81 arylsulfatase B Homo sapiens 31-65 12531251-6 2003 Of particular, interest were the quite different sulphation profiles of CS and DS chains in HGC in which, non-sulphated and 6-sulphated disaccharide units were increased 10 and 4 times, respectively, in comparison to HNG. Dermatan Sulfate 79-81 neurogranin Homo sapiens 217-220 12716937-2 2003 MPS VII mice lack lysosomal beta-glucuronidase (GUSB) activity, leading to the accumulation of partially degraded chondroitin, dermatan, and heparan sulfates in most tissues. Dermatan Sulfate 127-135 glucuronidase, beta Mus musculus 28-46 12716937-2 2003 MPS VII mice lack lysosomal beta-glucuronidase (GUSB) activity, leading to the accumulation of partially degraded chondroitin, dermatan, and heparan sulfates in most tissues. Dermatan Sulfate 127-135 glucuronidase, beta Mus musculus 48-52 12653636-1 2003 Hepatocyte growth factor (HGF)/scatter factor (SF) is a unique growth factor, in that it binds both heparan sulphate (HS) and dermatan sulphate (DS). Dermatan Sulfate 126-143 hepatocyte growth factor Homo sapiens 26-29 12653636-1 2003 Hepatocyte growth factor (HGF)/scatter factor (SF) is a unique growth factor, in that it binds both heparan sulphate (HS) and dermatan sulphate (DS). Dermatan Sulfate 145-147 hepatocyte growth factor Homo sapiens 26-29 12818259-0 2003 Additive thrombin inhibition by fast moving heparin and dermatan sulfate explains the anticoagulant effect of sulodexide, a natural mixture of glycosaminoglycans. Dermatan Sulfate 56-72 coagulation factor II, thrombin Homo sapiens 9-17 12818259-10 2003 CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH. Dermatan Sulfate 131-133 coagulation factor II, thrombin Homo sapiens 13-21 12818259-10 2003 CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH. Dermatan Sulfate 131-133 serpin family D member 1 Homo sapiens 113-117 12730206-4 2003 The human decorin that co-purified with SP-D is a 130-150-kDa proteoglycan, which has a 46-kDa protein core and approximately 90-kDa dermatan sulfate chain. Dermatan Sulfate 133-149 surfactant protein D Homo sapiens 40-44 12731055-7 2003 Heparan sulfate and dermatan sulfate, but not chondroitin sulfate, also inhibited the actions of CCL11 and CCL13 in assays of cellular shape change and chemotaxis. Dermatan Sulfate 20-36 C-C motif chemokine ligand 11 Homo sapiens 97-102 12731055-7 2003 Heparan sulfate and dermatan sulfate, but not chondroitin sulfate, also inhibited the actions of CCL11 and CCL13 in assays of cellular shape change and chemotaxis. Dermatan Sulfate 20-36 C-C motif chemokine ligand 13 Homo sapiens 107-112 12752450-3 2003 Hence, S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs. Dermatan Sulfate 95-111 myomesin 2 Homo sapiens 75-84 12752450-3 2003 Hence, S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs. Dermatan Sulfate 113-115 myomesin 2 Homo sapiens 75-84 12752450-7 2003 Together with the finding that exogenous DS and HS could inhibit streptococcal adhesion, these data suggest that GAGs function as receptors in M protein-mediated adhesion of S. pyogenes. Dermatan Sulfate 41-43 myomesin 2 Homo sapiens 143-152 12522561-1 2003 Mucopolysaccharidosis VII (MPS VII) is an autosomal recessive disorder caused by the deficiency of beta-glucuronidase leading to the intralysosomal storage of heparan, dermatan, and chondroitin sulfate. Dermatan Sulfate 168-176 glucuronidase beta Homo sapiens 99-117 12603746-5 2003 Three B. burgdorferi surface proteins, Bgp, DbpA and DbpB, have been demonstrated previously to bind to GAGs or to GAG-containing molecules, and we show here that recombinant derivatives of each of these proteins were able to bind to purified heparin and dermatan sulphate. Dermatan Sulfate 255-272 Y-box binding protein 3 Homo sapiens 44-48 12603746-5 2003 Three B. burgdorferi surface proteins, Bgp, DbpA and DbpB, have been demonstrated previously to bind to GAGs or to GAG-containing molecules, and we show here that recombinant derivatives of each of these proteins were able to bind to purified heparin and dermatan sulphate. Dermatan Sulfate 255-272 Y-box binding protein 1 Homo sapiens 53-57 12527107-0 2003 Galectin 1 inhibits incorporation of vitronectin and chondroitin sulfate B into the extracellular matrix of human vascular smooth muscle cells. Dermatan Sulfate 53-74 galectin 1 Homo sapiens 0-10 12505197-0 2003 A role for chondroitin sulphate B in the activity of interleukin 12 in stimulating gamma-interferon secretion. Dermatan Sulfate 11-33 interferon gamma Mus musculus 83-99 12423248-4 2002 The heparin-resistant binding of [125I]bFGF to TM-BBB4 was significantly inhibited by a cationic polypeptide poly-L-lysine (300 micro m), and compounds which contain a sulfate moiety, e.g. heparin and chondroitin sulfate-B (each 10 micro g/mL). Dermatan Sulfate 201-222 fibroblast growth factor 2 Mus musculus 39-43 12529676-5 2003 Competition experiments showed that 125I-SDF-1 alpha binding to the BMEC cell line 4LHBMEC was inhibited by heparins, heparan sulfate (HS) intestinal mucosa, chondroitin and dermatan sulfate (CS/DS), but not by HS bovine kidney. Dermatan Sulfate 174-190 C-X-C motif chemokine ligand 12 Homo sapiens 41-46 15000815-1 2003 Mucopolysaccharidosis type VI, or Maroteaux-Lamy syndrome, is an autosomal recessive disease caused by the deficiency of arylsulfatase B (ARSB; N-acetyl-galactosamine-4-sulfatase, E.C.3.1.6.12), which is involved in the stepwise degradation of dermatan sulfate and chondroitin sulfate. Dermatan Sulfate 244-260 arylsulfatase B Homo sapiens 138-142 15000815-1 2003 Mucopolysaccharidosis type VI, or Maroteaux-Lamy syndrome, is an autosomal recessive disease caused by the deficiency of arylsulfatase B (ARSB; N-acetyl-galactosamine-4-sulfatase, E.C.3.1.6.12), which is involved in the stepwise degradation of dermatan sulfate and chondroitin sulfate. Dermatan Sulfate 244-260 arylsulfatase B Homo sapiens 144-178 12186633-2 2002 We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin. Dermatan Sulfate 88-110 prion protein Homo sapiens 32-35 12186633-2 2002 We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin. Dermatan Sulfate 88-110 prion protein Rattus norvegicus 37-41 12423630-3 2002 We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS). Dermatan Sulfate 305-321 chorionic somatomammotropin hormone 1 Homo sapiens 73-77 12423630-3 2002 We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS). Dermatan Sulfate 305-321 carbohydrate sulfotransferase 15 Homo sapiens 155-167 12423630-3 2002 We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS). Dermatan Sulfate 323-325 chorionic somatomammotropin hormone 1 Homo sapiens 73-77 12423630-3 2002 We report here the in vitro synthesis of CS-E from chondrotin sulfate A (CS-A) by the purified squid N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) which catalyzed transfer of sulfate from 3(")-phosphoadenosine-5(")-phosphosulfate to position 6 of GalNAc(4SO(4)) residues of CS-A and dermatan sulfate (DS). Dermatan Sulfate 323-325 carbohydrate sulfotransferase 15 Homo sapiens 155-167 12423630-6 2002 GalNAc4S-6ST also catalyzed the synthesis of oversulfated DS with GalNAc(4,6-SO(4)) residues from DS. Dermatan Sulfate 58-60 carbohydrate sulfotransferase 15 Homo sapiens 0-12 12423630-6 2002 GalNAc4S-6ST also catalyzed the synthesis of oversulfated DS with GalNAc(4,6-SO(4)) residues from DS. Dermatan Sulfate 98-100 carbohydrate sulfotransferase 15 Homo sapiens 0-12 12423630-7 2002 Squid GalNAc4S-6ST thus should provide a useful tool for preparing CS-E and oversulfated DS with a defined proportion of GalNAc(4,6-SO(4)) residues. Dermatan Sulfate 89-91 carbohydrate sulfotransferase 15 Homo sapiens 6-18 12215437-0 2002 Dermatan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7). Dermatan Sulfate 0-16 fibroblast growth factor 7 Homo sapiens 51-77 12215437-0 2002 Dermatan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7). Dermatan Sulfate 0-16 fibroblast growth factor 7 Homo sapiens 79-84 12215437-5 2002 FGF-7 did not support cell proliferation in the absence of glycosaminoglycan or with addition of heparan sulfate or chondroitin sulfate A/C but did stimulate BaF/KGFR division in the presence of dermatan sulfate or highly sulfated low molecular weight fractions of dermatan. Dermatan Sulfate 195-211 fibroblast growth factor 7 Homo sapiens 0-5 12215437-6 2002 Dermatan sulfate also enabled FGF-7-dependent phosphorylation of mitogen-activated protein kinase and promoted binding of radiolabeled FGF-7 to FGFR2 IIIb. Dermatan Sulfate 0-16 fibroblast growth factor 7 Homo sapiens 30-35 12215437-6 2002 Dermatan sulfate also enabled FGF-7-dependent phosphorylation of mitogen-activated protein kinase and promoted binding of radiolabeled FGF-7 to FGFR2 IIIb. Dermatan Sulfate 0-16 fibroblast growth factor 7 Homo sapiens 135-140 12215437-8 2002 Thus, dermatan sulfate, the predominant glycosaminoglycan in skin, is the principle cofactor for FGF-7. Dermatan Sulfate 6-22 fibroblast growth factor 7 Homo sapiens 97-102 13679662-1 2002 Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III. Dermatan Sulfate 0-17 coagulation factor II, thrombin Homo sapiens 94-102 13679662-1 2002 Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III. Dermatan Sulfate 0-17 serpin family C member 1 Homo sapiens 151-167 13679662-1 2002 Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III. Dermatan Sulfate 19-21 coagulation factor II, thrombin Homo sapiens 94-102 13679662-1 2002 Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III. Dermatan Sulfate 19-21 serpin family C member 1 Homo sapiens 151-167 13679662-2 2002 DS does not interact with other coagulation factors and, unlike heparin, is able to inactivate thrombin bound to fibrin or to the surface of an injured vessel. Dermatan Sulfate 0-2 coagulation factor II, thrombin Homo sapiens 95-103 12023510-8 2002 Hypoxia enhanced the effect of all TGF-beta isoforms, particularly that of TGF-beta3, on the secretion of hyaluronic acid and chondroitin and dermatan sulfates. Dermatan Sulfate 142-159 transforming growth factor beta 1 Homo sapiens 35-43 12060613-8 2002 The decorin component of tumor stroma was previously shown to contain high levels of chondroitin sulfate as opposed to dermatan sulfate side chains, and those molecules contained unusually high levels of O- and 6-sulfate linkages. Dermatan Sulfate 119-135 decorin Homo sapiens 4-11 12149217-8 2002 A drastic decrease (up to 500-fold) of the second-order rate constant pertaining to heparin cofactor II (HCII) interaction, especially in the presence of dermatan sulfate, was found for the FIIa-MT67 compared with FIIa-WT, suggesting a severe impairment of thrombin inhibition by HCII in vivo. Dermatan Sulfate 154-170 serpin family D member 1 Homo sapiens 84-103 12149217-8 2002 A drastic decrease (up to 500-fold) of the second-order rate constant pertaining to heparin cofactor II (HCII) interaction, especially in the presence of dermatan sulfate, was found for the FIIa-MT67 compared with FIIa-WT, suggesting a severe impairment of thrombin inhibition by HCII in vivo. Dermatan Sulfate 154-170 serpin family D member 1 Homo sapiens 105-109 12413592-6 2002 Dermatan sulfate (DSO4)-catalyzed HCII thrombin inhibition was unchanged in R93A/R97A/R101A thrombin compared to wild-type recombinant thrombin. Dermatan Sulfate 0-16 serpin family D member 1 Homo sapiens 34-38 12413592-6 2002 Dermatan sulfate (DSO4)-catalyzed HCII thrombin inhibition was unchanged in R93A/R97A/R101A thrombin compared to wild-type recombinant thrombin. Dermatan Sulfate 0-16 coagulation factor II, thrombin Homo sapiens 39-47 12095635-0 2002 Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition. Dermatan Sulfate 84-100 serpin family D member 1 Homo sapiens 49-68 12095635-0 2002 Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition. Dermatan Sulfate 84-100 coagulation factor II, thrombin Homo sapiens 110-118 12095635-1 2002 Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate. Dermatan Sulfate 92-108 coagulation factor II, thrombin Homo sapiens 14-22 12095635-1 2002 Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate. Dermatan Sulfate 92-108 serpin family D member 1 Homo sapiens 26-45 12095635-1 2002 Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate. Dermatan Sulfate 92-108 serpin family D member 1 Homo sapiens 47-51 12095635-3 2002 K101Q greatly reduced heparin cofactor activity and required a more than 10-fold higher concentration of dermatan sulfate to accelerate thrombin inhibition compared with wild-type recombinant HCII. Dermatan Sulfate 105-121 coagulation factor II, thrombin Homo sapiens 136-144 12095635-5 2002 These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition. Dermatan Sulfate 128-144 serpin family D member 1 Homo sapiens 69-73 12095635-5 2002 These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition. Dermatan Sulfate 128-144 coagulation factor II, thrombin Homo sapiens 157-165 12094292-5 2002 The inhibitory activity of Na-SP was the strongest when compared to that of heparan sulfate, heparin, dextran sulfate, dermatan sulfate, chondroitin sulfate A/C and hyaluronan. Dermatan Sulfate 119-135 nuclear autoantigenic sperm protein Bos taurus 27-32 11821431-0 2002 Oversulfated chondroitin/dermatan sulfates containing GlcAbeta1/IdoAalpha1-3GalNAc(4,6-O-disulfate) interact with L- and P-selectin and chemokines. Dermatan Sulfate 25-42 selectin P Homo sapiens 121-131 11821431-1 2002 We previously reported that versican, a large chondroitin/dermatan sulfate (CS/DS) proteoglycan, interacts through its CS/DS chains with adhesion molecules L- and P-selectin and CD44, as well as chemokines. Dermatan Sulfate 58-74 versican Homo sapiens 28-36 11788461-2 2002 Transforming growth factor (TGF)-beta1 has been identified in atherosclerotic vessels and has been shown to stimulate the synthesis of chondroitin sulfate- and dermatan sulfate-containing proteoglycans by arterial smooth muscle cells (ASMCs), but whether it promotes lipid retention has not been addressed. Dermatan Sulfate 160-176 transforming growth factor beta 1 Homo sapiens 0-38 11991744-3 2002 Cell attachment of the VLP is efficiently inhibited by soluble heparin and dextran sulfate and less efficiently abrogated by several other glycosaminoglycans (GAGs) including chondroitin sulfate A and chondroitin sulfate B (dermatan sulfate), as determined by deconvolution microscopic immunodetection of the viral gag protein and by quantitative binding studies of metabolically labeled (35)S-VLP. Dermatan Sulfate 201-222 VHL like Homo sapiens 23-26 11991744-3 2002 Cell attachment of the VLP is efficiently inhibited by soluble heparin and dextran sulfate and less efficiently abrogated by several other glycosaminoglycans (GAGs) including chondroitin sulfate A and chondroitin sulfate B (dermatan sulfate), as determined by deconvolution microscopic immunodetection of the viral gag protein and by quantitative binding studies of metabolically labeled (35)S-VLP. Dermatan Sulfate 224-240 VHL like Homo sapiens 23-26 11855549-1 2002 Decorin, a small proteoglycan containing a dermatan sulfate (DS) chain, is expressed abnormally in human colon cancer stroma. Dermatan Sulfate 43-59 decorin Homo sapiens 0-7 11855549-1 2002 Decorin, a small proteoglycan containing a dermatan sulfate (DS) chain, is expressed abnormally in human colon cancer stroma. Dermatan Sulfate 61-63 decorin Homo sapiens 0-7 11853965-8 2002 Dermatan sulfate (DS) was the predominant glycosaminoglycan (GAG) present on biglycan and decorin in both tissues. Dermatan Sulfate 0-16 biglycan Homo sapiens 77-85 11853965-8 2002 Dermatan sulfate (DS) was the predominant glycosaminoglycan (GAG) present on biglycan and decorin in both tissues. Dermatan Sulfate 18-20 biglycan Homo sapiens 77-85 11861306-6 2002 Exogenous IDUA expression led to a normalization of glycosaminoglycan storage in MPS-IH cells, as evidenced by a dramatic decrease in the amount of (35)SO(4) sequestered within the heparan sulfate and dermatan sulfate compartments of these cells. Dermatan Sulfate 201-217 alpha-L-iduronidase Homo sapiens 10-14 11572857-1 2001 N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of N-acetylgalactosamine 4-sulfate (GalNAc(4SO(4))) in chondroitin sulfate and dermatan sulfate. Dermatan Sulfate 222-238 carbohydrate sulfotransferase 15 Homo sapiens 54-66 11816710-3 2001 It inhibits thrombin due to the formation of a covalent complex with heparin cofactor II, as in the case of mammalian dermatan sulfate, but the effect occurs at lower concentrations for the invertebrate polysaccharide. Dermatan Sulfate 118-134 coagulation factor II, thrombin Homo sapiens 12-20 11805133-1 2002 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin. Dermatan Sulfate 97-113 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 0-19 11805133-1 2002 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin. Dermatan Sulfate 97-113 serine (or cysteine) peptidase inhibitor, clade D, member 1 Mus musculus 21-25 11805133-1 2002 Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin. Dermatan Sulfate 97-113 coagulation factor II Mus musculus 61-69 11590178-10 2001 The glycosaminoglycan component of endocan consists of a single DS chain covalently attached to serine 137. Dermatan Sulfate 64-66 endothelial cell specific molecule 1 Homo sapiens 35-42 11590178-12 2001 Moreover, DS chains purified from endocan mimicked the endocan-mediated increase of cell proliferation in the presence of HGF/SF. Dermatan Sulfate 10-12 endothelial cell specific molecule 1 Homo sapiens 34-41 11590178-12 2001 Moreover, DS chains purified from endocan mimicked the endocan-mediated increase of cell proliferation in the presence of HGF/SF. Dermatan Sulfate 10-12 endothelial cell specific molecule 1 Homo sapiens 55-62 11590178-12 2001 Moreover, DS chains purified from endocan mimicked the endocan-mediated increase of cell proliferation in the presence of HGF/SF. Dermatan Sulfate 10-12 hepatocyte growth factor Homo sapiens 122-128 11598131-9 2001 Similarly, WISP-1 interaction with human skin fibroblasts was inhibited by dermatan sulfate, decorin, and biglycan or by treatment of the cell surface with dermatan sulfate-specific lyases. Dermatan Sulfate 75-91 cellular communication network factor 4 Homo sapiens 11-17 11598131-9 2001 Similarly, WISP-1 interaction with human skin fibroblasts was inhibited by dermatan sulfate, decorin, and biglycan or by treatment of the cell surface with dermatan sulfate-specific lyases. Dermatan Sulfate 156-172 cellular communication network factor 4 Homo sapiens 11-17 11572857-6 2001 The recombinant protein expressed from the human GalNAc4S-6ST cDNA transferred sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 6 of the nonreducing terminal and internal GalNAc(4SO(4)) residues contained in chondroitin sulfate A and dermatan sulfate. Dermatan Sulfate 248-264 carbohydrate sulfotransferase 15 Homo sapiens 49-61 11668612-2 2001 Mutations in the 4S gene are responsible for 4S deficiency, which leads to the intralysosomal storage of partially degraded glycosaminoglycans, dermatan sulfate, and chondroitin 4-sulfate. Dermatan Sulfate 144-160 arylsulfatase B Homo sapiens 17-19 11668612-2 2001 Mutations in the 4S gene are responsible for 4S deficiency, which leads to the intralysosomal storage of partially degraded glycosaminoglycans, dermatan sulfate, and chondroitin 4-sulfate. Dermatan Sulfate 144-160 arylsulfatase B Homo sapiens 45-47 11414686-0 2001 The glucuronyl C5-epimerase activity is the limiting factor in the dermatan sulfate biosynthesis. Dermatan Sulfate 67-83 glucuronic acid epimerase Homo sapiens 4-27 12940068-6 2001 Chondroitin sulfate A and chondroitin sulfate B reduced cell surface apoE by 23.6% and 15.3% respectively while incubations with chondrointin sulfate C not effective. Dermatan Sulfate 26-47 apolipoprotein E Homo sapiens 69-73 11692908-8 2001 To reduce thrombin generation, i.e., the mechanism by which heparin-induced thrombocytopenia induces thrombotic events, intravenous treatment with dermatan sulphate and low-dose urokinase was initiated. Dermatan Sulfate 147-164 coagulation factor II, thrombin Homo sapiens 10-18 11414686-1 2001 An early step in the biosynthesis of dermatan sulfate is polymerization to chondroitin, which then is modified by the D-glucuronyl C5-epimerase and mainly 4-O-sulfotransferase. Dermatan Sulfate 37-53 glucuronic acid epimerase Homo sapiens 120-143 11414686-9 2001 The data indicate that the activity of the d-glucuronyl C5-epimerase is the main factor for formation of dermatan sulfate in tissues. Dermatan Sulfate 105-121 glucuronic acid epimerase Homo sapiens 45-68 11294849-0 2001 Molecular basis for the susceptibility of fibrin-bound thrombin to inactivation by heparin cofactor ii in the presence of dermatan sulfate but not heparin. Dermatan Sulfate 122-138 coagulation factor II, thrombin Homo sapiens 55-63 11294849-1 2001 Although fibrin-bound thrombin is resistant to inactivation by heparin.antithrombin and heparin.heparin cofactor II complexes, indirect studies in plasma systems suggest that the dermatan sulfate.heparin cofactor II complex can inhibit fibrin-bound thrombin. Dermatan Sulfate 179-195 coagulation factor II, thrombin Homo sapiens 22-30 11294849-5 2001 In contrast, dermatan sulfate binds to thrombin but does not bind to fibrin. Dermatan Sulfate 13-29 coagulation factor II, thrombin Homo sapiens 39-47 11294849-7 2001 thrombin.fibrin complex forms, without dermatan sulfate-mediated bridging of thrombin to fibrin, only two binary interactions exist (thrombin.fibrin and thrombin. Dermatan Sulfate 39-55 coagulation factor II, thrombin Homo sapiens 0-8 11294849-10 2001 This study explains why fibrin-bound thrombin is susceptible to inactivation by heparin cofactor II in the presence of dermatan sulfate but not heparin. Dermatan Sulfate 119-135 coagulation factor II, thrombin Homo sapiens 37-45 11925507-0 2001 Requirement of chondroitin sulfate/dermatan sulfate recognition in midkine-dependent migration of macrophages. Dermatan Sulfate 35-51 midkine Homo sapiens 67-74 11925507-3 2001 MK-induced migration of peritoneal exudate macrophages was inhibited by heparin, chondroitin sulfate E and dermatan sulfate, but not by chondroitin sulfate D or chondroitin 6-sulfate. Dermatan Sulfate 107-123 midkine Homo sapiens 0-2 11925507-6 2001 These results indicated that a chondroitin sulfate, i.e. an E-type oversulfated structure with dermatan sulfate domain, is involved in MK-induced migration of macrophages. Dermatan Sulfate 95-111 midkine Homo sapiens 135-137 11322944-4 2001 By solid-phase assays, we showed that dermatan sulfate chains of decorin bind to the heparin-binding site included within the fibronectin-type III domains 10 and 11 of TN-X. Dermatan Sulfate 38-54 tenascin XB Homo sapiens 168-172 11139592-4 2001 GalNAc-4-ST2 transfers sulfate to the C-4 hydroxyl of terminal beta1,4-linked GalNAc in the sequence GalNAc-beta1,4GlcNAcbeta-R found on N-linked oligosaccharides and nonterminal beta1,4-linked GalNAc in chondroitin and dermatan. Dermatan Sulfate 220-228 carbohydrate sulfotransferase 9 Homo sapiens 0-12 11322427-1 2001 PURPOSE: Maroteaux-Lamy syndrome is one of the mucopolysaccharidoses caused by enzyme deficiency (arylsulfatase B) that leads to incomplete degradation and storage of dermatan sulfate. Dermatan Sulfate 167-183 arylsulfatase B Homo sapiens 98-113 11405343-1 2001 Mucopolysaccharidosis type I is due to a deficiency of the lysosomal enzyme alpha-L-iduronidase (EC 3.2.1.76) and is associated with a defect in the catabolism of the glycosaminoglycans heparan and dermatan sulphate. Dermatan Sulfate 198-215 alpha-L-iduronidase Homo sapiens 76-95 11290371-1 2001 In the current study, two specific glycosaminoglycan lyases, chondroitinase AC and chondroitinase B, were utilized to examine the roles of chondroitin sulfates and dermatan sulfate in tumor metastasis and angiogenesis. Dermatan Sulfate 164-180 galactosamine (N-acetyl)-6-sulfatase Homo sapiens 83-97 11732625-3 2001 Insulin and WGA stimulated [3H]glucosamine incorporation into hyaluronic acid (HA) and heparan sulphate (HS) without any alteration of chondroitin sulphate (CS) and dermatan sulphate (DS) contents. Dermatan Sulfate 184-186 insulin Homo sapiens 0-7 11050699-0 2000 Pharmacodynamic study of low molecular weight dermatan sulphate (Desmin) after a single subcutaneous administration in patients with renal insufficiency. Dermatan Sulfate 46-63 desmin Homo sapiens 65-71 10974347-2 2000 In contrast, surface-bound thrombin is not resistant to inhibition by heparin cofactor II (HCII) and its acceleration of its inhibitory effect by dermatan sulfate. Dermatan Sulfate 146-162 prothrombin Oryctolagus cuniculus 27-35 10974347-4 2000 Recently, a novel HCII agonist, Intimatan, has been synthesized by site-specific sulphation of highly purified dermatan sulfate comprising primarily of L-iduronic acid-4-O-sulphated N-acetyl-D-galactosamine, yielding a 4, 6-O-disulphate compound on the galactopyranose ring with a lower molecular weight, higher solubility, and specific activity than its parent, dermatan sulfate. Dermatan Sulfate 111-127 heparin cofactor 2 Oryctolagus cuniculus 18-22 10974347-4 2000 Recently, a novel HCII agonist, Intimatan, has been synthesized by site-specific sulphation of highly purified dermatan sulfate comprising primarily of L-iduronic acid-4-O-sulphated N-acetyl-D-galactosamine, yielding a 4, 6-O-disulphate compound on the galactopyranose ring with a lower molecular weight, higher solubility, and specific activity than its parent, dermatan sulfate. Dermatan Sulfate 363-379 heparin cofactor 2 Oryctolagus cuniculus 18-22 10871629-1 2000 N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST), which transfers sulfate from 3"-phosphoadenosine 5"-phosphosulfate (PAPS) to position 6 of N-acetylgalactosamine 4-sulfate in chondroitin sulfate and dermatan sulfate, was purified 19,600-fold to apparent homogeneity from the squid cartilage. Dermatan Sulfate 219-235 carbohydrate sulfotransferase 15 Homo sapiens 54-66 10961890-6 2000 Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner. Dermatan Sulfate 59-75 interleukin 10 Homo sapiens 102-108 10961890-6 2000 Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner. Dermatan Sulfate 59-75 Fc gamma receptor IIIa Homo sapiens 131-135 10961890-6 2000 Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner. Dermatan Sulfate 59-75 Fc gamma receptor Ia Homo sapiens 140-144 11776053-16 2000 GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin. Dermatan Sulfate 19-35 serpin family C member 1 Homo sapiens 83-95 10963998-1 2000 Decorin and glypican are two examples of exclusively chondroitin/dermatan sulfate and heparan sulfate-substituted proteoglycans, respectively. Dermatan Sulfate 65-81 glypican 1 Homo sapiens 12-20 10866805-9 2000 These results suggest that midkine binds to a polysulfated domain in the chondroitin sulfate chain with a region of dermatan sulfate structure. Dermatan Sulfate 116-132 midkine Mus musculus 27-34 10781601-11 2000 These results indicate C4ST-1 and C4ST-2 play complementary roles in chondroitin and dermatan sulfate synthesis in different tissues. Dermatan Sulfate 85-101 carbohydrate sulfotransferase 11 Homo sapiens 23-29 10781601-11 2000 These results indicate C4ST-1 and C4ST-2 play complementary roles in chondroitin and dermatan sulfate synthesis in different tissues. Dermatan Sulfate 85-101 carbohydrate sulfotransferase 12 Homo sapiens 34-40 10749870-0 2000 Altered dermatan sulfate structure and reduced heparin cofactor II-stimulating activity of biglycan and decorin from human atherosclerotic plaque. Dermatan Sulfate 8-24 biglycan Homo sapiens 91-99 10749870-1 2000 Biglycan and decorin are small dermatan sulfate-containing proteoglycans in the extracellular matrix of the artery wall. Dermatan Sulfate 31-47 biglycan Homo sapiens 0-8 10749870-2 2000 The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall. Dermatan Sulfate 4-20 coagulation factor II, thrombin Homo sapiens 51-59 10749870-2 2000 The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall. Dermatan Sulfate 4-20 serpin family D member 1 Homo sapiens 74-93 10749870-2 2000 The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall. Dermatan Sulfate 4-20 serpin family D member 1 Homo sapiens 95-99 10773191-2 2000 Here we provide evidence that TN-R derived from adult mouse brain expresses chondroitin sulfate (CS) glycosaminoglycans (GAGs), i.e. C-6S and C-4S, that are recognized by the CS/dermatan sulfate-specific monoclonal antibodies 473 HD and CS-56. Dermatan Sulfate 178-194 tenascin R Mus musculus 30-34 10753952-1 2000 Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate. Dermatan Sulfate 188-204 serpin family D member 1 Homo sapiens 0-19 10753952-1 2000 Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate. Dermatan Sulfate 188-204 serpin family D member 1 Homo sapiens 21-25 10723065-4 2000 Here we provide first evidence that TN-R derived from whole rat brain or cultured oligodendrocytes expresses chondroitin sulfate (CS) glycosaminoglycans (GAGs), i.e., C-4S and C-6S, that are recognized by CS-56, a CS/dermatan sulfate-specific monoclonal antibody. Dermatan Sulfate 217-233 tenascin R Rattus norvegicus 36-40 10781601-7 2000 Surprisingly, proteins expressed by these cDNAs transferred sulfate to the C-4 position of N-acetylgalactosamine in chondroitin and desulfated dermatan sulfate, thus we named these two enzymes, chondroitin 4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2). Dermatan Sulfate 143-159 carbohydrate sulfotransferase 11 Homo sapiens 194-235 10781601-7 2000 Surprisingly, proteins expressed by these cDNAs transferred sulfate to the C-4 position of N-acetylgalactosamine in chondroitin and desulfated dermatan sulfate, thus we named these two enzymes, chondroitin 4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2). Dermatan Sulfate 143-159 carbohydrate sulfotransferase 11 Homo sapiens 237-243 10781601-7 2000 Surprisingly, proteins expressed by these cDNAs transferred sulfate to the C-4 position of N-acetylgalactosamine in chondroitin and desulfated dermatan sulfate, thus we named these two enzymes, chondroitin 4-O-sulfotransferase 1 and -2 (C4ST-1 and C4ST-2). Dermatan Sulfate 143-159 carbohydrate sulfotransferase 12 Homo sapiens 248-254 10781601-9 2000 Moreover, analysis of (35)S-labeled dermatan sulfate formed by C4ST-1 indicate that sulfation preferentially took place in GlcA-->GalNAc unit than in IdoA-->GalNAc unit, suggesting that 4-O-sulfation at N-acetylgalactosamine may precede epimerization of glucuronic acid to iduronic acid during dermatan sulfate biosynthesis. Dermatan Sulfate 36-52 carbohydrate sulfotransferase 11 Homo sapiens 63-69 10747885-1 2000 Hepatocyte growth factor/scatter factor (HGF/SF) is a heparan/dermatan sulfate-binding growth factor produced by stromal cells that acts as a paracrine effector on neighboring epithelia. Dermatan Sulfate 62-78 hepatocyte growth factor Homo sapiens 41-47 10706937-1 2000 Heparin cofactor II is postulated to be an extravascular thrombin inhibitor that is physiologically stimulated by dermatan sulfate. Dermatan Sulfate 114-130 serpin family D member 1 Rattus norvegicus 0-19 10706937-1 2000 Heparin cofactor II is postulated to be an extravascular thrombin inhibitor that is physiologically stimulated by dermatan sulfate. Dermatan Sulfate 114-130 coagulation factor II Rattus norvegicus 57-65 10702409-0 2000 Impaired elastogenesis in Hurler disease: dermatan sulfate accumulation linked to deficiency in elastin-binding protein and elastic fiber assembly. Dermatan Sulfate 42-58 elastin Homo sapiens 96-103 10702409-1 2000 Hurler disease resulting from a deficiency in alpha-L-iduronidase, which causes an accumulation of dermatan sulfate and heparan sulfate glycosaminoglycans, is characterized by connective tissue and skeletal deformations, cardiomyopathy, cardiac valve defects, and progressive coronary artery stenosis. Dermatan Sulfate 99-115 alpha-L-iduronidase Homo sapiens 46-65 10702409-3 2000 Our data suggest that dermatan sulfate-bearing moieties bind to and cause functional inactivation of the 67-kd elastin-binding protein, a molecular chaperone for tropoelastin, which normally facilitates its secretion and assembly into elastic fibers. Dermatan Sulfate 22-38 elastin Homo sapiens 111-118 10702409-3 2000 Our data suggest that dermatan sulfate-bearing moieties bind to and cause functional inactivation of the 67-kd elastin-binding protein, a molecular chaperone for tropoelastin, which normally facilitates its secretion and assembly into elastic fibers. Dermatan Sulfate 22-38 elastin Homo sapiens 162-174 10640393-7 2000 The slower migrating species is absent in normal ligaments and may represent a different glycoform (containing either a single or two short chondroitin/dermatan sulfate chains) of biglycan. Dermatan Sulfate 152-168 biglycan Oryctolagus cuniculus 180-188 10623797-6 2000 Enzyme treatment of mouse mast cells revealed that binding of IFN-gamma was predominantly to chondroitin sulfate B (dermatan sulfate). Dermatan Sulfate 93-114 interferon gamma Mus musculus 62-71 10623797-6 2000 Enzyme treatment of mouse mast cells revealed that binding of IFN-gamma was predominantly to chondroitin sulfate B (dermatan sulfate). Dermatan Sulfate 116-132 interferon gamma Mus musculus 62-71 10623797-7 2000 Binding of IFN-gamma to dermatan sulfate was confirmed by inhibition ELISA. Dermatan Sulfate 24-40 interferon gamma Mus musculus 11-20 10625699-8 2000 Specifically, TGF-beta(1) induced an accumulation of small chondroitin/dermatan sulfate PGs (CS/DSPGs) with core proteins of approximately 50 kDa in the medium of both dense and sparse cultures, but a cell layer-associated heparan sulfate PG with a core protein size of approximately 400 kDa accumulated only in dense cultures. Dermatan Sulfate 71-87 transforming growth factor beta 1 Bos taurus 14-25 10536375-11 1999 Overall, these results show that the inhibitory action of DCN is dependent of substratum binding, is differentially mediated by its glycosaminoglycan side chains (chondroitin-sulfate vs. dermatan-sulfate chains), and is independent of a steric hindrance effect exerted by its glycosaminoglycan side chains. Dermatan Sulfate 187-203 decorin Homo sapiens 58-61 10632469-2 1999 In an in vitro test, bovine intestine dermatan sulfate exhibited stronger effects on stimulation of heparin cofactor II and activation of Glu-plasminogen by tissue plasminogen activator. Dermatan Sulfate 38-54 serpin family D member 1 Bos taurus 100-119 10661319-8 1999 This coordinated distribution suggests that stromelysin-1 may have a functional role, being implicated in predentine in the degradation of chondroitin-4-sulphate/dermatan sulphate-containing proteoglycans, and consequently allowing keratan sulphate proteoglycan concentration to increase near the border where mineralization is initiated. Dermatan Sulfate 162-179 matrix metallopeptidase 3 Rattus norvegicus 44-57 10536375-7 1999 DCN bearing dermatan-sulfate chains (i.e., skin and cartilage DCN) was about 20-fold more effective in inhibiting cell migration than DCN bearing chondroitin-sulfate chains (i.e., bone DCN). Dermatan Sulfate 12-28 decorin Homo sapiens 0-3 10536375-7 1999 DCN bearing dermatan-sulfate chains (i.e., skin and cartilage DCN) was about 20-fold more effective in inhibiting cell migration than DCN bearing chondroitin-sulfate chains (i.e., bone DCN). Dermatan Sulfate 12-28 decorin Homo sapiens 62-65 10536375-7 1999 DCN bearing dermatan-sulfate chains (i.e., skin and cartilage DCN) was about 20-fold more effective in inhibiting cell migration than DCN bearing chondroitin-sulfate chains (i.e., bone DCN). Dermatan Sulfate 12-28 decorin Homo sapiens 62-65 10536375-9 1999 These data assert that the dermatan-sulfate chains of DCN are responsible for a negative influence on cell migration. Dermatan Sulfate 27-43 decorin Homo sapiens 54-57 10907447-3 1999 Included among these compounds are indirect thrombin inhibitors such as dermatan sulfate, heparanoids and low-molecular weight heparin. Dermatan Sulfate 72-88 coagulation factor II, thrombin Homo sapiens 44-52 11008173-1 2000 We have shown previously in the rat that biglycan, a recently discovered chondroitin sulfate proteoglycan, has neurotrophic effects which are mediated by its chondroitin/dermatan sulfate chains. Dermatan Sulfate 170-186 biglycan Rattus norvegicus 41-49 10600521-5 1999 In vitro, different glycosaminoglycans, such as dermatan sulfate and chondroitin sulfate-C, also induce a dimer assembly of HARP. Dermatan Sulfate 48-64 pleiotrophin Homo sapiens 124-128 10496984-0 1999 Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin. Dermatan Sulfate 178-194 tissue factor pathway inhibitor 2 Homo sapiens 23-56 10496984-0 1999 Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin. Dermatan Sulfate 178-194 tissue factor pathway inhibitor 2 Homo sapiens 102-108 10496984-0 1999 Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin. Dermatan Sulfate 178-194 tissue factor pathway inhibitor 2 Homo sapiens 232-238 10496984-0 1999 Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin. Dermatan Sulfate 178-194 plasminogen Homo sapiens 251-258 10496984-5 1999 We found that TFPI-2/MSPI bound specifically to heparin and dermatan sulfate. Dermatan Sulfate 60-76 tissue factor pathway inhibitor 2 Homo sapiens 14-20 10496984-7 1999 However, binding affinity for TFPI-2/MSPI with heparin was 250-300 times greater than that for TFPI-2/MSPI with dermatan sulfate. Dermatan Sulfate 112-128 tissue factor pathway inhibitor 2 Homo sapiens 95-101 10496984-12 1999 Collectively, our results demonstrate that conformation-dependent arginine-mediated ionic interactions are responsible for the TFPI-2/MSPI triplet binding to fibroblast ECM, heparin, and dermatan sulfate and that heparin augmented the rate of inhibition of plasmin by TFPI-2/MSPI. Dermatan Sulfate 187-203 tissue factor pathway inhibitor 2 Homo sapiens 127-133 10488098-0 1999 Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II. Dermatan Sulfate 27-43 coagulation factor II, thrombin Homo sapiens 66-74 10488098-0 1999 Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II. Dermatan Sulfate 27-43 serpin family D member 1 Homo sapiens 91-110 10488098-1 1999 Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin. Dermatan Sulfate 12-28 serpin family D member 1 Homo sapiens 38-57 10488098-1 1999 Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin. Dermatan Sulfate 12-28 serpin family D member 1 Homo sapiens 59-63 10488098-1 1999 Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin. Dermatan Sulfate 12-28 serpin family D member 1 Homo sapiens 124-128 10488098-1 1999 Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin. Dermatan Sulfate 12-28 coagulation factor II, thrombin Homo sapiens 153-161 10488098-7 1999 Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus. Dermatan Sulfate 40-56 serpin family D member 1 Homo sapiens 98-102 10488098-7 1999 Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus. Dermatan Sulfate 133-149 serpin family D member 1 Homo sapiens 98-102 10488098-7 1999 Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus. Dermatan Sulfate 133-149 serpin family D member 1 Homo sapiens 161-165 10456450-3 1999 Agents that selectively inhibit thrombin, such as dermatan sulphate, have potential for a favourable benefit-risk ratio in the prevention of this complication. Dermatan Sulfate 50-67 coagulation factor II, thrombin Homo sapiens 32-40 10596456-1 1999 BACKGROUND: The MPS-I is an autosomal recessive disorder caused by mutations in the IDUA gene that induce to a deficiency of glycosidase alpha-L-iduronidase that is required for degradation of heparan and dermatan sulfate. Dermatan Sulfate 205-221 alpha-L-iduronidase Homo sapiens 84-88 10596456-1 1999 BACKGROUND: The MPS-I is an autosomal recessive disorder caused by mutations in the IDUA gene that induce to a deficiency of glycosidase alpha-L-iduronidase that is required for degradation of heparan and dermatan sulfate. Dermatan Sulfate 205-221 alpha-L-iduronidase Homo sapiens 137-156 10494755-1 1999 Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate. Dermatan Sulfate 93-110 serpin family D member 1 Homo sapiens 0-19 10494755-1 1999 Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate. Dermatan Sulfate 93-110 serpin family D member 1 Homo sapiens 21-25 10494755-1 1999 Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate. Dermatan Sulfate 93-110 coagulation factor II, thrombin Homo sapiens 54-62 10187838-0 1999 Molecular cloning and characterization of a human uronyl 2-sulfotransferase that sulfates iduronyl and glucuronyl residues in dermatan/chondroitin sulfate. Dermatan Sulfate 126-134 uronyl 2-sulfotransferase Homo sapiens 50-75 10318803-8 1999 These results altogether indicate that EXTL2/EXTR2 encodes the alpha1,4-N-acetylhexosaminyltransferase that transfers GalNAc/GlcNAc to the tetrasaccharide representing the common glycosaminoglycan-protein linkage region and that is most likely the critical enzyme that determines and initiates the heparin/heparan sulfate synthesis, separating it from the chondroitin sulfate/dermatan sulfate synthesis. Dermatan Sulfate 376-392 exostosin like glycosyltransferase 2 Homo sapiens 39-44 10318803-8 1999 These results altogether indicate that EXTL2/EXTR2 encodes the alpha1,4-N-acetylhexosaminyltransferase that transfers GalNAc/GlcNAc to the tetrasaccharide representing the common glycosaminoglycan-protein linkage region and that is most likely the critical enzyme that determines and initiates the heparin/heparan sulfate synthesis, separating it from the chondroitin sulfate/dermatan sulfate synthesis. Dermatan Sulfate 376-392 exostosin like glycosyltransferase 2 Homo sapiens 45-50 10341217-1 1999 Hepatocyte growth factor interacts with both heparan and dermatan sulphates, in addition to its specific signalling receptor, Met. Dermatan Sulfate 57-75 hepatocyte growth factor Canis lupus familiaris 0-24 10209287-1 1999 A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 61-78 coagulation factor II, thrombin Homo sapiens 107-115 10209287-8 1999 These results suggest that, like dermatan sulphate and heparin, other polyanions stimulate HCII primarily by an allosteric mechanism requiring the N-terminal acidic domain. Dermatan Sulfate 33-50 serpin family D member 1 Homo sapiens 91-95 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. Dermatan Sulfate 88-104 serpin family C member 1 Homo sapiens 24-36 10225976-0 1999 Dermatan sulfate activates nuclear factor-kappab and induces endothelial and circulating intercellular adhesion molecule-1. Dermatan Sulfate 0-16 intercellular adhesion molecule 1 Homo sapiens 89-122 10225976-3 1999 Cultured human dermal microvascular endothelial cells exposed to DS responded with rapid nuclear translocation of nuclear factor-kappaB (NF-kappaB), increased expression of intercellular adhesion molecule-1 (ICAM-1) mRNA, and increased ICAM-1 cell surface protein. Dermatan Sulfate 65-67 intercellular adhesion molecule 1 Homo sapiens 173-206 10225976-3 1999 Cultured human dermal microvascular endothelial cells exposed to DS responded with rapid nuclear translocation of nuclear factor-kappaB (NF-kappaB), increased expression of intercellular adhesion molecule-1 (ICAM-1) mRNA, and increased ICAM-1 cell surface protein. Dermatan Sulfate 65-67 intercellular adhesion molecule 1 Homo sapiens 208-214 10225976-3 1999 Cultured human dermal microvascular endothelial cells exposed to DS responded with rapid nuclear translocation of nuclear factor-kappaB (NF-kappaB), increased expression of intercellular adhesion molecule-1 (ICAM-1) mRNA, and increased ICAM-1 cell surface protein. Dermatan Sulfate 65-67 intercellular adhesion molecule 1 Homo sapiens 236-242 10225976-7 1999 The ICAM-1-inductive activity of DS was confirmed in vivo. Dermatan Sulfate 33-35 intercellular adhesion molecule 1 Homo sapiens 4-10 10075664-5 1999 We report that heparan sulfate, dermatan sulfate, and to a lesser extent, chondroitin sulfate A, displaced HARP bound to the extracellular compartment. Dermatan Sulfate 32-48 pleiotrophin Mus musculus 107-111 10075664-6 1999 Binding analyses with a biosensor showed that HARP bound heparin with fast association and dissociation kinetics (kass = 1.6 x 10(6) M-1 s-1; kdiss = 0.02 s-1), yielding a Kd value of 13 nM; the interaction between HARP and dermatan sulfate was characterized by slower association kinetics (kass = 0.68 x 10(6) M-1 s-1) and a lower affinity (Kd = 51 nM). Dermatan Sulfate 224-240 pleiotrophin Mus musculus 46-50 10075664-7 1999 Exogenous heparin, heparan sulfate, and dermatan sulfate potentiated the growth-stimulatory activity of HARP, suggesting that corresponding proteoglycans could be involved in the regulation of the mitogenic activity of HARP. Dermatan Sulfate 40-56 pleiotrophin Mus musculus 104-108 10075664-7 1999 Exogenous heparin, heparan sulfate, and dermatan sulfate potentiated the growth-stimulatory activity of HARP, suggesting that corresponding proteoglycans could be involved in the regulation of the mitogenic activity of HARP. Dermatan Sulfate 40-56 pleiotrophin Mus musculus 219-223 10384999-5 1999 Dermatan sulphate was rich in iduronic acid (62% of total uronic acid) and composed of non-sulphated (44%), and mono-sulphated disaccharides bearing esterified sulphate groups at positions C-4 (53%) or C-6 (3%) of the N-acetyl galactosamine. Dermatan Sulfate 0-17 complement C4A (Rodgers blood group) Homo sapiens 189-192 10384999-5 1999 Dermatan sulphate was rich in iduronic acid (62% of total uronic acid) and composed of non-sulphated (44%), and mono-sulphated disaccharides bearing esterified sulphate groups at positions C-4 (53%) or C-6 (3%) of the N-acetyl galactosamine. Dermatan Sulfate 0-17 complement C6 Homo sapiens 202-205 10209287-1 1999 A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 61-78 serpin family D member 1 Homo sapiens 119-138 10209287-1 1999 A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate 61-78 serpin family D member 1 Homo sapiens 140-144 10209287-2 1999 Previous investigations indicated that the binding sites on HCII for heparin and dermatan sulphate overlap but are not identical. Dermatan Sulfate 81-98 serpin family D member 1 Homo sapiens 60-64 10447264-5 1999 The disease is caused by the inability to degrade dermatan sulphate and heparan sulphate due to mutations in the iduronate-2-sulphatase gene (IDS). Dermatan Sulfate 50-67 iduronate 2-sulfatase Homo sapiens 142-145 10349131-1 1999 Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate. Dermatan Sulfate 115-131 serpin family D member 1 Homo sapiens 0-19 10349131-1 1999 Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate. Dermatan Sulfate 115-131 serpin family D member 1 Homo sapiens 21-25 10349131-1 1999 Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate. Dermatan Sulfate 115-131 coagulation factor II, thrombin Homo sapiens 79-87 10349131-7 1999 HCII thrombin inhibition possibly takes place in extravascular sites where dermatan sulfate is present. Dermatan Sulfate 75-91 serpin family D member 1 Homo sapiens 0-4 10349131-7 1999 HCII thrombin inhibition possibly takes place in extravascular sites where dermatan sulfate is present. Dermatan Sulfate 75-91 coagulation factor II, thrombin Homo sapiens 5-13 9837939-0 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes. Dermatan Sulfate 61-77 heparin cofactor 2 Oryctolagus cuniculus 9-28 10093889-5 1999 For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively. Dermatan Sulfate 71-87 serpin family D member 1 Homo sapiens 33-52 9837939-0 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes. Dermatan Sulfate 61-77 heparin cofactor 2 Oryctolagus cuniculus 41-60 10093889-5 1999 For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively. Dermatan Sulfate 71-87 serpin family D member 1 Homo sapiens 54-58 10093889-5 1999 For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively. Dermatan Sulfate 71-87 coagulation factor II, thrombin Homo sapiens 125-133 9837939-2 1998 Heparin cofactor II is a naturally occurring anticoagulant that acts by specifically inhibiting thrombin and is facilitated by the binding of glycosaminoglycans such as heparin and dermatan sulfate. Dermatan Sulfate 181-197 heparin cofactor 2 Oryctolagus cuniculus 0-19 9837939-4 1998 We have produced permanently activated heparin cofactor II molecules by covalent linkage to either heparin or dermatan sulfate. Dermatan Sulfate 110-126 heparin cofactor 2 Oryctolagus cuniculus 39-58 9837939-5 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively). Dermatan Sulfate 185-201 heparin cofactor 2 Oryctolagus cuniculus 41-60 9837939-5 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively). Dermatan Sulfate 61-77 heparin cofactor 2 Oryctolagus cuniculus 41-60 9837939-5 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively). Dermatan Sulfate 185-201 heparin cofactor 2 Oryctolagus cuniculus 9-28 9837939-5 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively). Dermatan Sulfate 185-201 heparin cofactor 2 Oryctolagus cuniculus 9-28 9837939-5 1998 Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively). Dermatan Sulfate 185-201 heparin cofactor 2 Oryctolagus cuniculus 41-60 9843172-1 1998 Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. Dermatan Sulfate 100-116 serpin family D member 1 Homo sapiens 0-19 9837939-6 1998 Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin. Dermatan Sulfate 57-73 heparin cofactor 2 Oryctolagus cuniculus 5-24 9837939-6 1998 Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin. Dermatan Sulfate 57-73 heparin cofactor 2 Oryctolagus cuniculus 37-56 9837939-6 1998 Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin. Dermatan Sulfate 57-73 prothrombin Oryctolagus cuniculus 190-198 9837939-7 1998 The intravenous half-life of the covalent complexes in rabbits was significantly longer than that of free heparin or dermatan sulfate (4.4, 3.4, 0.33, and 0.50 h for heparin cofactor II-heparin, heparin cofactor II-dermatan sulfate, heparin, and dermatan sulfate, respectively). Dermatan Sulfate 117-133 heparin cofactor 2 Oryctolagus cuniculus 166-185 9813026-10 1998 The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin. Dermatan Sulfate 90-106 coagulation factor II, thrombin Homo sapiens 26-34 9813026-10 1998 The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin. Dermatan Sulfate 90-106 serpin family D member 1 Homo sapiens 199-203 9774430-0 1998 Dermatan sulfate released after injury is a potent promoter of fibroblast growth factor-2 function. Dermatan Sulfate 0-16 fibroblast growth factor 2 Homo sapiens 63-89 9774430-6 1998 Dermatan sulfate, and not heparan sulfate, was the major contributor to this activity, and dermatan sulfate bound FGF-2 with Kd = 2.48 microM. Dermatan Sulfate 91-107 fibroblast growth factor 2 Homo sapiens 114-119 9774430-7 1998 These data demonstrate that proteoglycans released during wound repair are functionally active and provide the first evidence that dermatan sulfate is a potent mediator of fibroblast growth factor-2 responsiveness. Dermatan Sulfate 131-147 fibroblast growth factor 2 Homo sapiens 172-198 9774395-7 1998 In contrast dermatan sulfates from S. plicata and H. pyriformis are potent anticoagulants due to potentiation of thrombin inhibition by heparin cofactor II. Dermatan Sulfate 12-29 coagulation factor II, thrombin Homo sapiens 113-121 9727420-7 1998 The increases were associated with highly charged molecular forms of decorin and biglycan, indicating modification of the proteins with dermatan sulfate chains of increased sulfation. Dermatan Sulfate 136-152 decorin Homo sapiens 69-76 9727420-7 1998 The increases were associated with highly charged molecular forms of decorin and biglycan, indicating modification of the proteins with dermatan sulfate chains of increased sulfation. Dermatan Sulfate 136-152 biglycan Homo sapiens 81-89 9727420-9 1998 CONCLUSIONS: The increased dermatan sulfate associated with chronic corneal pathologic conditions results from stromal accumulation of decorin and particularly of biglycan in the affected corneas. Dermatan Sulfate 27-43 decorin Homo sapiens 135-142 9727420-9 1998 CONCLUSIONS: The increased dermatan sulfate associated with chronic corneal pathologic conditions results from stromal accumulation of decorin and particularly of biglycan in the affected corneas. Dermatan Sulfate 27-43 biglycan Homo sapiens 163-171 9843172-1 1998 Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. Dermatan Sulfate 100-116 serpin family D member 1 Homo sapiens 21-25 9843172-1 1998 Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. Dermatan Sulfate 100-116 coagulation factor II, thrombin Homo sapiens 53-61 9843172-3 1998 In this report, we show that both frog and chicken plasma contain a dermatan sulfate-dependent inhibitor that forms a 118-kDa complex with human 125I-thrombin. Dermatan Sulfate 68-84 coagulation factor II, thrombin Homo sapiens 150-158 9725536-3 1998 Scheie syndrome (MPS I S) is due to the deficient activity of alpha-L-iduronidase leading to the intralysosomal accumulation of dermatan sulfate and heparan sulfate. Dermatan Sulfate 128-144 alpha-L-iduronidase Homo sapiens 62-81 9153251-11 1997 The known inhibitors of the interaction of alpha-dystroglycan with laminin-1, including EDTA, sulfatide, fucoidan, dextran sulfate, heparin, and sialic acid, also perturbed the adhesion of RT4 cells to laminin-1, whereas the reagents which do not inhibit the interaction, including dextran, chondroitin sulfate, dermatan sulfate, and GlcNAc, did not. Dermatan Sulfate 312-328 dystroglycan 1 Homo sapiens 49-61 9682679-11 1998 An increase in the length of the dermatan sulphate chain on decorin, a previously reported characteristic of this glycosaminoglycan in hypertrophic scar, was seen in all but two of the strains treated with transforming growth factor-beta 1. Dermatan Sulfate 33-50 transforming growth factor beta 1 Homo sapiens 206-239 9684733-0 1998 Pharmacokinetics of low molecular weight dermatan sulphate (desmin) in different cohorts of patients. Dermatan Sulfate 41-58 desmin Homo sapiens 60-66 9568695-7 1998 Other sulfated GAGs and related macromolecules were also effective in the enhancement of amylin fibril formation in the order of heparin > heparan sulfate > chondroitin-4-sulfate = dermatan sulfate = dextran sulfate > pentosan polysulfate, implicating the importance of the specific GAG/carbohydrate backbone. Dermatan Sulfate 187-203 islet amyloid polypeptide Homo sapiens 89-95 9488672-7 1998 The affinity of HPRG for various GAGs measured in a competition assay decreased in the following order: heparin > dermatan sulfate > heparan sulfate > chondroitin sulfate A. Dermatan Sulfate 117-133 histidine rich glycoprotein Homo sapiens 16-20 9488672-8 1998 Binding of HPRG to immobilized dermatan sulfate had a midpoint at pH 6.5, was less influenced by zinc, and exhibited cooperativity. Dermatan Sulfate 31-47 histidine rich glycoprotein Homo sapiens 11-15 9485475-1 1998 Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. Dermatan Sulfate 83-99 serpin family D member 1 Homo sapiens 0-19 9485475-1 1998 Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. Dermatan Sulfate 83-99 serpin family D member 1 Homo sapiens 21-25 9485475-1 1998 Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. Dermatan Sulfate 83-99 coagulation factor II, thrombin Homo sapiens 36-44 9417075-1 1998 We have demonstrated by affinity chromatography that hepatocyte growth factor/scatter factor (HGF/SF) binds strongly to dermatan sulfate (DS), with a similar ionic strength dependence to that previously seen with heparan sulfate (HS). Dermatan Sulfate 120-136 hepatocyte growth factor Homo sapiens 94-100 9417075-1 1998 We have demonstrated by affinity chromatography that hepatocyte growth factor/scatter factor (HGF/SF) binds strongly to dermatan sulfate (DS), with a similar ionic strength dependence to that previously seen with heparan sulfate (HS). Dermatan Sulfate 138-140 hepatocyte growth factor Homo sapiens 94-100 9353333-5 1997 Purified recombinant meizothrombin and meizothrombin(desF1) were inhibited by HCII in the presence of dermatan sulfate with maximal second-order rate constants of 8 x 10(6) M-1.min-1 and 1.8 x 10(7) M-1.min-1, respectively, but were inhibited less than one-tenth as fast by AT in the presence of heparin. Dermatan Sulfate 102-118 serpin family D member 1 Homo sapiens 78-82 9353333-7 1997 When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate. Dermatan Sulfate 14-30 serpin family D member 1 Homo sapiens 167-171 9353333-7 1997 When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate. Dermatan Sulfate 14-30 coagulation factor II, thrombin Homo sapiens 71-79 9305797-8 1997 The glycosaminoglycan chains on both decorin and biglycan were identified as dermatan sulphate by their susceptibility to chondroitinase-B. Dermatan Sulfate 77-94 decorin Bos taurus 37-44 9305797-8 1997 The glycosaminoglycan chains on both decorin and biglycan were identified as dermatan sulphate by their susceptibility to chondroitinase-B. Dermatan Sulfate 77-94 biglycan Bos taurus 49-57 9268591-7 1997 A significant decrease of dermatan sulfate levels with aging correlates well with the observed increase in the level of beta-glucuronidase activity. Dermatan Sulfate 26-42 glucuronidase beta Homo sapiens 120-138 9694594-1 1998 Collagen XIV is known to bind to the dermatan sulfate chain of decorin and to the heparan sulfate chain of perlecan. Dermatan Sulfate 37-53 collagen type XIV alpha 1 chain Gallus gallus 0-12 9692613-3 1998 The increase in thrombin-heparin cofactor II complexes suggests that the site of the additional thrombin generation is relatively rich in dermatan sulfate. Dermatan Sulfate 138-154 coagulation factor II, thrombin Homo sapiens 16-24 9692613-3 1998 The increase in thrombin-heparin cofactor II complexes suggests that the site of the additional thrombin generation is relatively rich in dermatan sulfate. Dermatan Sulfate 138-154 coagulation factor II, thrombin Homo sapiens 96-104 9692613-11 1998 The role of this placental dermatan sulfate in local regulation of thrombin in the placenta warrants further study. Dermatan Sulfate 27-43 coagulation factor II, thrombin Homo sapiens 67-75 9626917-0 1998 Desmin (a low molecular weight dermatan sulphate) versus heparin in the treatment of patients with deep venous thrombosis. Dermatan Sulfate 31-48 desmin Homo sapiens 0-6 9626917-1 1998 OBJECTIVE: There is theoretical and experimental evidence which indicates that Desmin, a low molecular weight dermatan sulphate, could be an attractive alternative to heparin in the treatment of deep venous thrombosis (DVT). Dermatan Sulfate 110-127 desmin Homo sapiens 79-85 9425437-1 1997 Hurler syndrome (mucopolysaccharidosis IH or MPS IH) is a congenital mucopolysaccharide storage disorder resulting from a genetic deficiency of alpha-L-iduronidase (IDUA), which is required for lysosomal degradation of glycosaminoglycans heparan sulfate and dermatan sulfate. Dermatan Sulfate 258-274 alpha-L-iduronidase Homo sapiens 144-163 9425437-1 1997 Hurler syndrome (mucopolysaccharidosis IH or MPS IH) is a congenital mucopolysaccharide storage disorder resulting from a genetic deficiency of alpha-L-iduronidase (IDUA), which is required for lysosomal degradation of glycosaminoglycans heparan sulfate and dermatan sulfate. Dermatan Sulfate 258-274 alpha-L-iduronidase Homo sapiens 165-169 9394322-1 1997 BACKGROUND: Dermatan sulphate (DS) is a selective thrombin inhibitor with antithrombotic properties and low bleeding potential. Dermatan Sulfate 12-29 coagulation factor II, thrombin Homo sapiens 50-58 9394322-1 1997 BACKGROUND: Dermatan sulphate (DS) is a selective thrombin inhibitor with antithrombotic properties and low bleeding potential. Dermatan Sulfate 31-33 coagulation factor II, thrombin Homo sapiens 50-58 9266027-6 1997 These results suggest that the increased amount of dermatan/chondroitin sulphate in SSc fibroblasts reflects an enhanced expression of decorin core protein. Dermatan Sulfate 51-60 decorin Homo sapiens 135-142 9255408-3 1997 The results of these studies on 12 sliced layers (average thickness of 250 microns) of skin show that the content of glucuronic acid in DS decreases when moving from the outer surface of the skin to the inside, while the degree of sulfation of the C-2 hydroxy group of iduronate and the C-4 and C-6 hydroxy groups of N-acetylgalactosamine increases with depth. Dermatan Sulfate 136-138 complement C4A (Rodgers blood group) Homo sapiens 287-298 9240182-6 1997 HPLC showed that CSBS contained a small amount of dermatan sulphate and abundant heparan sulphate, both of which inhibited crystal growth. Dermatan Sulfate 50-67 filamin A Homo sapiens 17-21 9240182-7 1997 CONCLUSION: Both heparan sulphate and dermatan sulphate may inhibit calcium oxalate crystallization, the former being the predominant GAG in CSBS. Dermatan Sulfate 38-55 filamin A Homo sapiens 141-145 9124611-4 1997 The diminished activity of oxidized SLPI could be almost completely restored when an iduronate-containing glycosaminoglycan, such as heparin, heparan sulfate, or dermatan sulfate, was added to the reaction medium. Dermatan Sulfate 162-178 secretory leukocyte peptidase inhibitor Homo sapiens 36-40 9165101-4 1997 Furthermore, a lower, but significant Ca2(+)-independent binding of SAP to heparan sulfate, dermatan sulfate, AA protein and the amyloid precursor protein beta2M was observed. Dermatan Sulfate 92-108 amyloid P component, serum Homo sapiens 68-71 8939995-0 1996 Distinct isoforms of chicken decorin contain either one or two dermatan sulfate chains. Dermatan Sulfate 63-79 decorin Gallus gallus 29-36 9068899-0 1997 Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative. Dermatan Sulfate 75-93 coagulation factor II, thrombin Homo sapiens 13-21 9068899-0 1997 Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative. Dermatan Sulfate 75-93 serpin family D member 1 Homo sapiens 36-55 9068899-1 1997 The kinetics of thrombin inhibition by heparin cofactor II (HC II) in the presence of dermatan sulphates, native (DS), or oversulphated (DSS 1 and DSS 2) and a biospecific dextran derivative substituted with carboxymethyl, carboxymethyl-benzylamide and carboxymethyl benzylamide-sulphonate functional groups (CMDBS), has been studied as a function of the sulphated polysaccharide concentration. Dermatan Sulfate 86-104 coagulation factor II, thrombin Homo sapiens 16-24 9013976-6 1997 Binding of C1q to CSPG was competitively inhibited by free glycosaminoglycans (GAG) in the order dextran sulfate > heparin > heparan sulfate > chondroitin-6-sulfate (CS-C) > dermatan sulfate (CS-B) > chondroitin-4-sulfate (CS-A). Dermatan Sulfate 186-202 complement C1q A chain Homo sapiens 11-14 8995662-8 1997 Our biosensor analyses showed that both heparan sulfate and dermatan sulfate inhibited gB2 binding (ED50 = 1 to 5 microg/ml), indicating that gB2 interacts with both heparin-like and dermatan sulfate glycosaminoglycans. Dermatan Sulfate 60-76 gamma-aminobutyric acid type B receptor subunit 2 Homo sapiens 87-90 8995662-8 1997 Our biosensor analyses showed that both heparan sulfate and dermatan sulfate inhibited gB2 binding (ED50 = 1 to 5 microg/ml), indicating that gB2 interacts with both heparin-like and dermatan sulfate glycosaminoglycans. Dermatan Sulfate 60-76 gamma-aminobutyric acid type B receptor subunit 2 Homo sapiens 142-145 8994426-0 1997 Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate. Dermatan Sulfate 141-157 serpin family C member 1 Homo sapiens 56-68 8994426-10 1997 In contrast, with UFH or DS, the rate of thrombin inhibition is twofold slower in plasma than in buffer. Dermatan Sulfate 25-27 coagulation factor II, thrombin Homo sapiens 41-49 9100165-2 1997 Ten patients affected by proximal deep venous thrombosis were treated in an open study with a low-molecular-weight dermatan sulphate (Desmin), administered at doses of 400 mg (intravenous bolus) followed by 1200 mg/day infused intravenously for 10 days, without activated partial thromboplastin adjustment. Dermatan Sulfate 115-132 desmin Homo sapiens 134-140 15622771-4 1997 CONCLUSION: Sjamp was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin. Dermatan Sulfate 33-49 serpin family C member 1 Homo sapiens 97-109 9352383-0 1997 Bioavailability of Desmin, a low molecular weight dermatan sulfate, after subcutaneous administration to healthy volunteers. Dermatan Sulfate 50-66 desmin Homo sapiens 19-25 9352383-1 1997 The bioavailability of two different s.c. doses of Desmin (a new low molecular weight dermatan sulfate) was evaluated in 12 healthy volunteers (6 men, 6 women aged 22-45 years) who were injected, on 3 separate days and with a wash-out period of at least 21 days between each administration, with 200 and 300 mg of Desmin by the s.c. route and 200 mg by the i.v. Dermatan Sulfate 86-102 desmin Homo sapiens 51-57 9200333-1 1997 Dermatan sulfate (DS) is a component of connective tissue and catalyzes the heparin cofactor II-mediated inhibition of thrombin. Dermatan Sulfate 0-16 coagulation factor II, thrombin Homo sapiens 119-127 9200333-1 1997 Dermatan sulfate (DS) is a component of connective tissue and catalyzes the heparin cofactor II-mediated inhibition of thrombin. Dermatan Sulfate 18-20 coagulation factor II, thrombin Homo sapiens 119-127 8939995-2 1996 In mammals, decorin carries one chondroitin/dermatan sulfate chain as a distinction from its homologue, biglycan, which contains two glycosaminoglycan chains. Dermatan Sulfate 44-60 decorin Gallus gallus 12-19 8910299-2 1996 Mucopolysaccharidosis type VI (MPS VI) is an autosomal recessive disease caused by a deficiency of N-acetylgalactosamine 4-sulfatase (4S) leading to the lysosomal accumulation and urinary excretion of dermatan sulfate. Dermatan Sulfate 201-217 arylsulfatase B Felis catus 99-132 9067256-7 1996 Glycosaminoglycans such as chondroitin sulfate, dermatan sulfate and a chondroitin polysulfate, interacted with myeloblastin as non-essential activators in the presence of peptide substrates (activation up to a 6.7-fold factor) and as partial inhibitors (about 50% inhibition at saturation) in the presence of elastin. Dermatan Sulfate 48-64 proteinase 3 Homo sapiens 112-124 8810655-2 1996 Patients were randomly allocated to three treatment groups to receive a new low-molecular-weight dermatan sulfate (Desmin) at the dose, respectively, of 100 mg once daily by subcutaneous (SC) route, 100 mg twice a day SC, and 200 mg once daily by intramuscular (IM) route. Dermatan Sulfate 97-113 desmin Homo sapiens 115-121 8792767-1 1996 Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction. Dermatan Sulfate 89-105 serpin family D member 1 Homo sapiens 0-19 8792767-1 1996 Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction. Dermatan Sulfate 89-105 serpin family D member 1 Homo sapiens 21-25 8792767-1 1996 Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction. Dermatan Sulfate 89-105 coagulation factor II, thrombin Homo sapiens 39-47 8837309-0 1996 Pharmacology of a new low molecular weight dermatan sulphate (Desmin) in healthy volunteers: repeated daily intramuscular administration of 400 mg for a week. Dermatan Sulfate 43-60 desmin Homo sapiens 62-68 8710849-1 1996 Mucopolysaccharidosis VI (MPS VI) is a lysosomal storage disease with autosomal recessive inheritance caused by a deficiency of the enzyme arylsulfatase B (ASB), which is involved in degradation of dermatan sulfate and chondroitin 4-sulfate. Dermatan Sulfate 198-214 arylsulfatase B Mus musculus 156-159 8755662-2 1996 Mucopolysacchariodosis type VI (MPS VI) is the lysosomal storage disorder caused by the deficient activity of arylsulfatase B (ASB; N-acetylgalactosamine 4-sulfatase) and the subsequent accumulation of the glycosaminoglycan (GAG), dermatan sulfate. Dermatan Sulfate 231-247 arylsulfatase B Homo sapiens 110-125 8755662-2 1996 Mucopolysacchariodosis type VI (MPS VI) is the lysosomal storage disorder caused by the deficient activity of arylsulfatase B (ASB; N-acetylgalactosamine 4-sulfatase) and the subsequent accumulation of the glycosaminoglycan (GAG), dermatan sulfate. Dermatan Sulfate 231-247 arylsulfatase B Homo sapiens 127-130 8755662-2 1996 Mucopolysacchariodosis type VI (MPS VI) is the lysosomal storage disorder caused by the deficient activity of arylsulfatase B (ASB; N-acetylgalactosamine 4-sulfatase) and the subsequent accumulation of the glycosaminoglycan (GAG), dermatan sulfate. Dermatan Sulfate 231-247 arylsulfatase B Homo sapiens 132-165 8885144-0 1996 Active site for heparin cofactor II in low molecular mass dermatan sulfate. Dermatan Sulfate 58-74 serpin family D member 1 Homo sapiens 16-35 8885144-3 1996 Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII). Dermatan Sulfate 16-18 serpin family C member 1 Homo sapiens 58-63 8885144-3 1996 Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII). Dermatan Sulfate 16-18 serpin family D member 1 Homo sapiens 99-118 8885144-3 1996 Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII). Dermatan Sulfate 16-18 serpin family D member 1 Homo sapiens 120-124 8885144-10 1996 The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS. Dermatan Sulfate 135-137 serpin family D member 1 Homo sapiens 31-35 8885144-10 1996 The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS. Dermatan Sulfate 220-222 serpin family D member 1 Homo sapiens 31-35 8674529-2 1996 Considering 3H incorporation, we found that IFNgamma increased the production of glycosaminoglycan synthesis, including hyaluronic acid, heparan and chondroitin/dermatan sulfate. Dermatan Sulfate 161-177 interferon gamma Homo sapiens 44-52 8663298-8 1996 Examination of several well characterized glycosaminoglycans to inhibit the binding of heparin to both heparin-binding IGFBP-3 peptides revealed that the most potent inhibitors were heparin, heparan sulfate, and dermatan sulfate; chondroitin sulfate A and hyaluronic acid were intermediate in their inhibitory activities; and chondroitin sulfate C caused no inhibition. Dermatan Sulfate 212-228 insulin like growth factor binding protein 3 Homo sapiens 119-126 8791281-6 1996 H suppressed the stimulation of the synthesis of HA, CS and DS by TGF-beta. Dermatan Sulfate 60-62 transforming growth factor, beta 1 Rattus norvegicus 66-74 8651289-1 1996 Maroteaux-Lamy syndrome, or mucopolysaccharidosis type VI (MPS-VI), is a lysosomal storage disorder characterized by the defective degradation of dermatan sulfate due to the deficiency of N-acetylgalactosamine-4-sulfatase (4S). Dermatan Sulfate 146-162 arylsulfatase B Homo sapiens 188-221 8603018-4 1996 Using recently developed sensitive assays for FXIa-inhibitor complexes we found thrombin-mediated and FXII-dependent activation of endogenous FXI in plasma in the presence of heparan sulphate, heparin, dermatan sulphate or dextran sulphate. Dermatan Sulfate 202-219 coagulation factor II, thrombin Homo sapiens 80-88 8701414-3 1996 DS extracted and purified from pig mucosa has a relative molecular mass (Mr) of about 23,100 and is composed of about 10% nonsulfated disaccharide, 80% monosulfated disaccharides and about 10% disulfated disaccharides, with a sulfate to carboxyl ratio of 1.00 and a heparin cofactor II (HCII) activity of about 160 units/mg. Dermatan Sulfate 0-2 serpin family D member 1 Sus scrofa 266-285 8701414-3 1996 DS extracted and purified from pig mucosa has a relative molecular mass (Mr) of about 23,100 and is composed of about 10% nonsulfated disaccharide, 80% monosulfated disaccharides and about 10% disulfated disaccharides, with a sulfate to carboxyl ratio of 1.00 and a heparin cofactor II (HCII) activity of about 160 units/mg. Dermatan Sulfate 0-2 serpin family D member 1 Sus scrofa 287-291 8562924-1 1996 Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin. Dermatan Sulfate 126-142 serpin family D member 1 Homo sapiens 0-19 8562924-1 1996 Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin. Dermatan Sulfate 126-142 serpin family D member 1 Homo sapiens 21-25 8562924-1 1996 Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin. Dermatan Sulfate 126-142 coagulation factor II, thrombin Homo sapiens 98-106 8725717-0 1996 The effects of dermatan sulfate at submicrogram/ml concentrations on in vitro thrombin generation. Dermatan Sulfate 15-31 coagulation factor II, thrombin Homo sapiens 78-86 8725717-3 1996 We investigated the ability of dermatan sulfate added to plasma at 0.2, 0.5 and 1.0 microgram/ml to inhibit thrombin generation initiated by low concentrations of recombinant human tissue factor in defibrinated plasma. Dermatan Sulfate 31-47 coagulation factor II, thrombin Homo sapiens 108-116 8725717-4 1996 A dose dependent decrease in thrombin potential was demonstrated at therapeutically relevant concentrations of dermatan sulfate (0.5 and 1.0 microgram/ml) but there was no induction of a lag phase in thrombin generation. Dermatan Sulfate 111-127 coagulation factor II, thrombin Homo sapiens 29-37 8725717-7 1996 The effect on the thrombin potential was somewhat greater at the lowest concentration of tissue factor and amounted to a maximum inhibition of approximately 50% at 1 microgram/ml dermatan sulfate. Dermatan Sulfate 179-195 coagulation factor II, thrombin Homo sapiens 18-26 8725717-8 1996 A dose dependent increase in formation of thrombin-heparin cofactor II complexes and a decrease in thrombin-antithrombin complex formation with increasing dermatan sulfate concentration were observed at all dermatan sulfate concentrations. Dermatan Sulfate 155-171 coagulation factor II, thrombin Homo sapiens 99-107 8725717-10 1996 We conclude that dermatan sulfate, at the concentrations tested, catalyses inhibition of free thrombin by heparin cofactor II but not efficiently enough to inhibit prothrombinase formation. Dermatan Sulfate 17-33 coagulation factor II, thrombin Homo sapiens 94-102 8668693-2 1996 Mucin is a gelatinous substance composed of glycosaminoglycanes, especially hyaluronic acid and dermatan sulfate bound to small quantities of chondoitin sulfate and heparin sulfate. Dermatan Sulfate 96-112 LOC100508689 Homo sapiens 0-5 8656041-3 1996 We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Dermatan Sulfate 108-124 platelet factor 4 Homo sapiens 44-47 8603018-4 1996 Using recently developed sensitive assays for FXIa-inhibitor complexes we found thrombin-mediated and FXII-dependent activation of endogenous FXI in plasma in the presence of heparan sulphate, heparin, dermatan sulphate or dextran sulphate. Dermatan Sulfate 202-219 coagulation factor XI Homo sapiens 46-49 8603018-6 1996 We conclude that endogenous FXI in plasma can be activated by thrombin in the presence of various glycosaminoglycans, including the physiological compounds heparan sulphate and dermatan sulphate, but only at very high concentrations of thrombin, corresponding to 100% prothrombin activation in undiluted plasma. Dermatan Sulfate 177-194 coagulation factor XI Homo sapiens 28-31 8603018-6 1996 We conclude that endogenous FXI in plasma can be activated by thrombin in the presence of various glycosaminoglycans, including the physiological compounds heparan sulphate and dermatan sulphate, but only at very high concentrations of thrombin, corresponding to 100% prothrombin activation in undiluted plasma. Dermatan Sulfate 177-194 coagulation factor II, thrombin Homo sapiens 62-70 8838671-9 1996 Fibroblasts responded to the addition of dermatan sulfate, heparan sulfate and heparin with a decrease in fibronectin, collagenase and interleukin-6 mRNA. Dermatan Sulfate 41-57 fibronectin 1 Homo sapiens 106-117 8838671-9 1996 Fibroblasts responded to the addition of dermatan sulfate, heparan sulfate and heparin with a decrease in fibronectin, collagenase and interleukin-6 mRNA. Dermatan Sulfate 41-57 interleukin 6 Homo sapiens 135-148 8836009-9 1996 In addition it was found that dermatan sulfate levels, expressed as antithrombin activity by heparin cofactor II, were significantly increased over control values. Dermatan Sulfate 30-46 serpin family D member 1 Rattus norvegicus 93-112 8815578-2 1996 However, the low molecular weight (LMW) dermatan sulphate Desmin 370 has been shown to generate circulating anti-Xa activity following administration to humans. Dermatan Sulfate 40-57 desmin Homo sapiens 58-64 8815580-3 1996 In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate. Dermatan Sulfate 144-160 MIR7-3 host gene Homo sapiens 23-28 8815580-3 1996 In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate. Dermatan Sulfate 144-160 serpin family D member 1 Homo sapiens 55-60 8815580-3 1996 In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate. Dermatan Sulfate 144-160 coagulation factor II, thrombin Homo sapiens 116-124 8845462-1 1996 Low-molecular-weight (LMW)-dermatan sulfate (Desmin) with the mean molecular weight of 5600 Da has been obtained by limited depolymerization of natural dermatan sulfate. Dermatan Sulfate 27-43 desmin Homo sapiens 45-51 8845462-1 1996 Low-molecular-weight (LMW)-dermatan sulfate (Desmin) with the mean molecular weight of 5600 Da has been obtained by limited depolymerization of natural dermatan sulfate. Dermatan Sulfate 152-168 desmin Homo sapiens 45-51 8665399-0 1996 Release of interleukin-1 beta by dermatan sulfate suppresses hepatocyte growth. Dermatan Sulfate 33-49 interleukin 1 beta Rattus norvegicus 11-29 8665399-6 1996 Similarly, more than 10 hr was required after the addition of DS before IL-1 beta mRNA was detected. Dermatan Sulfate 62-64 interleukin 1 beta Rattus norvegicus 72-81 8665399-7 1996 These findings suggest that DS in the medium induced the production of IL-1 beta which, in turn, reduced DNA synthesis in hepatocytes. Dermatan Sulfate 28-30 interleukin 1 beta Rattus norvegicus 71-80 8944417-7 1996 They induced a dermatan sulfate-like activity in the plasma of treated rats, as measured by heparin cofactor II-mediated thrombin inhibition assay. Dermatan Sulfate 15-31 serpin family D member 1 Rattus norvegicus 92-111 8944417-7 1996 They induced a dermatan sulfate-like activity in the plasma of treated rats, as measured by heparin cofactor II-mediated thrombin inhibition assay. Dermatan Sulfate 15-31 coagulation factor II Rattus norvegicus 121-129 8747085-4 1995 TGF beta 1 induced a more marked increase in collagen and fibronectin release and greater production of sulphated GAGs as DS and heparan sulphate (HS) in the otosclerotic cells. Dermatan Sulfate 122-124 transforming growth factor beta 1 Homo sapiens 0-10 7779094-0 1995 Formation of heparan sulfate or chondroitin/dermatan sulfate on recombinant domain I of mouse perlecan expressed in Chinese hamster ovary cells. Dermatan Sulfate 44-60 LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein Cricetulus griseus 94-102 8746633-9 1995 In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII. Dermatan Sulfate 195-211 coagulation factor II, thrombin Homo sapiens 51-59 8746633-9 1995 In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII. Dermatan Sulfate 195-211 CD59 molecule (CD59 blood group) Homo sapiens 93-98 8746633-9 1995 In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII. Dermatan Sulfate 195-211 serpin family D member 1 Rattus norvegicus 104-109 8746633-9 1995 In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII. Dermatan Sulfate 304-320 coagulation factor II, thrombin Homo sapiens 51-59 8746633-9 1995 In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII. Dermatan Sulfate 304-320 CD59 molecule (CD59 blood group) Homo sapiens 93-98 8746633-9 1995 In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII. Dermatan Sulfate 304-320 serpin family D member 1 Rattus norvegicus 104-109 8530090-1 1995 Iduronate-2-sulfatase (IDS) is involved in the degradation of heparan sulfate and dermatan sulfate in the lysosomes, and a deficiency in this enzyme results in Hunter syndrome. Dermatan Sulfate 82-98 iduronate 2-sulfatase Homo sapiens 0-21 7487873-5 1995 Although bFGF and/or TGF-beta 1 induced a similar stimulation in cell-surface chondroitin sulphate/dermatan sulphate and heparan sulphate (HS) proteoglycan synthesis, only the turnover of HS proteoglycans was increased. Dermatan Sulfate 99-116 transforming growth factor beta 1 Sus scrofa 21-31 8530090-1 1995 Iduronate-2-sulfatase (IDS) is involved in the degradation of heparan sulfate and dermatan sulfate in the lysosomes, and a deficiency in this enzyme results in Hunter syndrome. Dermatan Sulfate 82-98 iduronate 2-sulfatase Homo sapiens 23-26 8533121-0 1995 Pharmacology of desmin (low molecular weight dermatan sulphate) in healthy volunteers following intravenous bolus administration of different dosages (200, 400, 800 mg). Dermatan Sulfate 45-62 desmin Homo sapiens 16-22 8533121-1 1995 Eight healthy volunteers (6 males, 2 females, mean age 31.6 yrs), were administered--on three separate days--200, 400 and 800 mg of a new low molecular weight Dermatan sulphate (Desmin), given as a single i.v. Dermatan Sulfate 159-176 desmin Homo sapiens 178-184 7626005-1 1995 Iduronate 2-sulphatase (IDS) is a lysosomal enzyme involved in degradation of dermatan sulphate and heparan sulphate. Dermatan Sulfate 78-95 iduronate 2-sulfatase Homo sapiens 0-22 7626005-1 1995 Iduronate 2-sulphatase (IDS) is a lysosomal enzyme involved in degradation of dermatan sulphate and heparan sulphate. Dermatan Sulfate 78-95 iduronate 2-sulfatase Homo sapiens 24-27 7676405-0 1995 Structural heterogeneity of dermatan sulfate chains: correlation with heparin cofactor II activating properties. Dermatan Sulfate 28-44 serpin family D member 1 Bos taurus 70-89 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 15-17 serpin family D member 1 Bos taurus 52-71 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 15-17 serpin family D member 1 Bos taurus 73-77 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 15-17 coagulation factor II, thrombin Bos taurus 102-110 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 159-161 serpin family D member 1 Bos taurus 52-71 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 159-161 serpin family D member 1 Bos taurus 73-77 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 159-161 coagulation factor II, thrombin Bos taurus 102-110 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 159-161 serpin family D member 1 Bos taurus 52-71 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 159-161 serpin family D member 1 Bos taurus 73-77 7676405-5 1995 The ability of DS crude preparation to activate the heparin cofactor II (HCII) mediated inhibition of thrombin depends on the relative amount of highly active DS chains; this activity is related to the overall charge of DS chains and particularly with the content of IdoUA-2-SO4-->GalNAc-4-SO4 and UA-->GalNAc-4,6-di-SO4 disaccharides. Dermatan Sulfate 159-161 coagulation factor II, thrombin Bos taurus 102-110 7647222-3 1995 A low-molecular-weight dermatan sulphate releases only very small amounts of TFPI after intravenous injection without a clear dose-dependent effect. Dermatan Sulfate 23-40 tissue factor pathway inhibitor Homo sapiens 77-81 7663435-1 1995 The iduronate-2-sulfatase (IDS) is a lysosomal enzyme that acts on sulphate groups on C-2 positions of the iduronic acid residues of the mucopolysaccharides heparan sulphate and dermatan sulphate. Dermatan Sulfate 178-195 iduronate 2-sulfatase Homo sapiens 4-25 7781777-3 1995 HCII inhibits thrombin in both a progressive reaction, and in an accelerated reaction catalyzed by a glycosaminoglycan, dermatan sulphate (DS). Dermatan Sulfate 139-141 heparin cofactor 2 Oryctolagus cuniculus 0-4 7781777-3 1995 HCII inhibits thrombin in both a progressive reaction, and in an accelerated reaction catalyzed by a glycosaminoglycan, dermatan sulphate (DS). Dermatan Sulfate 139-141 prothrombin Oryctolagus cuniculus 14-22 8589262-2 1995 IL-7 binds to heparin and heparan sulfate, to a lesser extent to dermatan sulfate and does not bind to chondroitin sulfate. Dermatan Sulfate 65-81 interleukin 7 Mus musculus 0-4 7721830-8 1995 The novel aspect of this molecule is the presence of a terminal alpha-Gal-NAc residue at a position that is normally occupied by beta-GalNAc in chondroitin/dermatan sulfate or by alpha-Glc-NAc in heparin or heparan sulfate chains. Dermatan Sulfate 156-172 synuclein alpha Homo sapiens 74-77 7721830-8 1995 The novel aspect of this molecule is the presence of a terminal alpha-Gal-NAc residue at a position that is normally occupied by beta-GalNAc in chondroitin/dermatan sulfate or by alpha-Glc-NAc in heparin or heparan sulfate chains. Dermatan Sulfate 156-172 synuclein alpha Homo sapiens 137-140 7592529-3 1995 Two predominant proteoglycans were identified in the stromal fraction: keratan sulfate proteoglycan and chondroitin sulfate/dermatan sulfate proteoglycan. Dermatan Sulfate 124-140 versican Gallus gallus 16-28 7592530-14 1995 Analysis of proteoglycans of the culture medium has shown that most of the medium proteoglycans were keratan sulfate proteoglycan and free keratan sulfate chain (or keratan sulfate chain with a short peptide) during all ages after Day 7, although the major proteoglycan of Day 5 medium was chondroitin sulfate/dermatan sulfate proteoglycan. Dermatan Sulfate 310-326 versican Gallus gallus 82-94 7592530-14 1995 Analysis of proteoglycans of the culture medium has shown that most of the medium proteoglycans were keratan sulfate proteoglycan and free keratan sulfate chain (or keratan sulfate chain with a short peptide) during all ages after Day 7, although the major proteoglycan of Day 5 medium was chondroitin sulfate/dermatan sulfate proteoglycan. Dermatan Sulfate 310-326 versican Gallus gallus 82-94