PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3218731-0 1988 Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin. Glycosaminoglycans 63-81 coagulation factor II, thrombin Homo sapiens 119-127 2713501-2 1989 An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed. Glycosaminoglycans 81-99 coagulation factor II, thrombin Homo sapiens 20-28 2851191-6 1988 This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma. Glycosaminoglycans 27-44 coagulation factor II, thrombin Homo sapiens 69-77 2851191-6 1988 This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma. Glycosaminoglycans 27-44 coagulation factor II, thrombin Homo sapiens 161-169 3218731-3 1988 This has been used to compare the binding of a range of glycosaminoglycans and other sulfated polymers to antithrombin III and thrombin, a major inhibitor of and a central protease in the coagulation system, respectively. Glycosaminoglycans 56-74 coagulation factor II, thrombin Homo sapiens 110-118 2931856-3 1985 Thrombin at more than one unit/ml accelerated the release of [35S] sulfate-labeled glycosaminoglycans from cultured porcine aortic endothelial cells. Glycosaminoglycans 83-101 coagulation factor II, thrombin Homo sapiens 0-8 2902851-7 1988 The findings suggest more stringent structural requirements for GAG stimulation of antithrombin-thrombin interaction than for antithrombin-Factor Xa or heparin cofactor-thrombin interaction, which may also be of significance in physiological control of haemostasis. Glycosaminoglycans 64-67 coagulation factor II, thrombin Homo sapiens 87-95 2902851-7 1988 The findings suggest more stringent structural requirements for GAG stimulation of antithrombin-thrombin interaction than for antithrombin-Factor Xa or heparin cofactor-thrombin interaction, which may also be of significance in physiological control of haemostasis. Glycosaminoglycans 64-67 coagulation factor II, thrombin Homo sapiens 96-104 3863104-2 1985 The rate of thrombin inhibition by heparin cofactor II is accelerated (greater than or equal to 1000-fold) in the presence of the glycosaminoglycans, heparin and dermatan sulfate. Glycosaminoglycans 130-148 coagulation factor II, thrombin Homo sapiens 12-20 6305407-4 1983 The 10 glutamic acid residues that are present in the amino-terminal region of prothrombin and are converted to gamma-carboxyglutamic acid in the mature protein are coded by only the GAG codon. Glycosaminoglycans 183-186 coagulation factor II, thrombin Homo sapiens 79-90 6486808-2 1984 This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease inhibitor for mucopolysaccharide. Glycosaminoglycans 214-232 coagulation factor II, thrombin Homo sapiens 85-93 6687888-1 1983 We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Glycosaminoglycans 38-56 coagulation factor II, thrombin Homo sapiens 95-103 6687802-3 1983 Heparin and dermatan sulfate which were eluted from the affinity column catalyzed the inhibition of thrombin by heparin cofactor II to a greater degree than did the respective unfractionated mucopolysaccharides. Glycosaminoglycans 191-210 coagulation factor II, thrombin Homo sapiens 100-108 6658719-4 1983 Thrombin was shown to bind to vascular endothelium and artificial surfaces containing GAG:s. The binding could be inhibited on both types of surfaces by pretreating them with protamine. Glycosaminoglycans 86-89 coagulation factor II, thrombin Homo sapiens 0-8 6658719-6 1983 It is concluded that thrombin binds to vessel wall GAG:s and is inactivated by the endothelium. Glycosaminoglycans 51-54 coagulation factor II, thrombin Homo sapiens 21-29 6448845-4 1980 Subsequently, we demonstrated that labeled heparin could be utilized in conjunction with fluorescence polarization spectroscopy to monitor the binding of mucopolysaccharide to thrombin, factor IXa, factor Xa, and plasmin. Glycosaminoglycans 154-172 coagulation factor II, thrombin Homo sapiens 176-207 6961402-15 1982 Given our method for generating the above data, these spectral alterations must be associated with the binding of a second critical domain of the mucopolysaccharide to antithrombin that is required for rapid complex formation with thrombin or the activation of the protease inhibitor with respect to the neutralization of the latter enzyme. Glycosaminoglycans 146-164 coagulation factor II, thrombin Homo sapiens 172-180 6448845-5 1980 The interaction of this complex carbohydrate with thrombin exhibited a stoichiometry of 2:1 with KH1T DISS = KH2T DISS = 8 x 10(-7) M. The formation of mucopolysaccharide . Glycosaminoglycans 152-170 coagulation factor II, thrombin Homo sapiens 50-58 6448846-17 1980 Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor. Glycosaminoglycans 87-105 coagulation factor II, thrombin Homo sapiens 162-193 22618708-3 2012 Rather, PN1 is expressed by multiple cell types, including macrophages, smooth muscle cells, and platelets, and it is on the surface of these cells, bound to glycosaminoglycans, that PN1 inhibits the signaling functions of thrombin. Glycosaminoglycans 158-176 coagulation factor II, thrombin Homo sapiens 223-231 6768163-0 1980 Effect of glycosaminoglycans on thrombin-induced clotting of normal and antithrombin III-deficient plasmas. Glycosaminoglycans 10-28 coagulation factor II, thrombin Homo sapiens 32-40 570737-0 1978 Inhibition of thrombin by antithrombin III in the presence of certain glycosaminoglycans found in the mammalian aorta. Glycosaminoglycans 70-88 coagulation factor II, thrombin Homo sapiens 14-22 4261008-0 1972 The release of glycosaminoglycans during exposure of human platelets to thrombin and polystyrene latex particles. Glycosaminoglycans 15-33 coagulation factor II, thrombin Homo sapiens 72-80 30869126-1 2019 The glycosaminoglycan dermatan sulfate (DS) is a well-known activator of heparin cofactor II-dependent inactivation of thrombin. Glycosaminoglycans 4-21 coagulation factor II, thrombin Homo sapiens 119-127 29173042-1 2018 Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate. Glycosaminoglycans 104-122 coagulation factor II, thrombin Homo sapiens 4-12 26548632-4 2016 Here, we demonstrate that thrombin elicits dual transactivation-dependent signalling pathways to stimulate mRNA expression of glycosaminoglycan synthesizing enzymes chondroitin 4-O-sulfotransferase 1 and chondroitin sulfate synthase 1. Glycosaminoglycans 126-143 coagulation factor II, thrombin Homo sapiens 26-34 22618708-7 2012 The crystal structures suggest a unique 2-step mechanism of thrombin recognition involving rapid electrostatics-driven association to form an initial glycosaminoglycan-bridged complex, followed by a large conformational rearrangement to form the productive Michaelis complex. Glycosaminoglycans 150-167 coagulation factor II, thrombin Homo sapiens 60-68 22315264-3 2012 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes. Glycosaminoglycans 34-52 coagulation factor II, thrombin Homo sapiens 70-78 21256835-6 2011 RESULTS: Glycosaminoglycans extracted from aneurysms have a more potent anticoagulant activity than those from normal arteries of young adults, mostly due to a relative enrichment of dermatan sulfate, which potentiates heparin cofactor II inhibition of thrombin. Glycosaminoglycans 9-27 coagulation factor II, thrombin Homo sapiens 253-261 22506762-10 2012 The decorin protein was found in the tissue, the DS glycosaminoglycan chain was removed with thrombin digestion, and there was no change in the mechanical properties of the tissue due to the thrombin digestion relative to controls. Glycosaminoglycans 52-69 coagulation factor II, thrombin Homo sapiens 93-101 23152789-4 2012 The availability of multiple co-crystal structures facilitates a structural analysis that challenges the long-held belief that the GAG binding sites in antithrombin and thrombin are essentially similar with high solvent exposure and shallow surface characteristics. Glycosaminoglycans 131-134 coagulation factor II, thrombin Homo sapiens 156-164 20670608-7 2010 Second-order rate constants for thrombin inactivation by recombinant and deglycosylated HCII were comparable, at optimal GAG concentrations that were lower than those for plasma HCII, consistent with its weaker GAG binding. Glycosaminoglycans 121-124 coagulation factor II, thrombin Homo sapiens 32-40 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). Glycosaminoglycans 144-162 coagulation factor II, thrombin Homo sapiens 35-43 20670608-7 2010 Second-order rate constants for thrombin inactivation by recombinant and deglycosylated HCII were comparable, at optimal GAG concentrations that were lower than those for plasma HCII, consistent with its weaker GAG binding. Glycosaminoglycans 211-214 coagulation factor II, thrombin Homo sapiens 32-40 20002544-9 2010 Certain glycosaminoglycans, including heparin, only partially competed with polyphosphate for binding to thrombin, and polyphosphate did not reduce heparin-catalyzed inactivation of thrombin by antithrombin. Glycosaminoglycans 8-26 coagulation factor II, thrombin Homo sapiens 105-113 18574264-2 2008 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors. Glycosaminoglycans 34-52 coagulation factor II, thrombin Homo sapiens 70-78 20807657-5 2010 It is established that chemically oversulfated glycosaminoglycans (GAGs) induce thrombin generation through contact system activation in human plasma. Glycosaminoglycans 47-65 coagulation factor II, thrombin Homo sapiens 80-88 16556679-4 2006 This multifunctional glycosaminoglycan also inhibited apoptosis induced by other agents, including staurosporin, broad-spectrum kinase inhibitor and thrombin. Glycosaminoglycans 21-38 coagulation factor II, thrombin Homo sapiens 149-157 17222891-4 2007 All these glycosaminoglycans (GAGs) also inhibited thrombin-induced aggregation of washed platelets in the presence of antithrombin (AT) or heparin cofactor II (HCII) but not in their absence. Glycosaminoglycans 10-28 coagulation factor II, thrombin Homo sapiens 51-59 18571697-10 2008 Chemically cleaved glycosaminoglycan (GAG) chains analyzed by SDS-PAGE and size exclusion chromatography were larger for proteoglycans from thrombin treated cells. Glycosaminoglycans 19-36 coagulation factor II, thrombin Homo sapiens 140-148 18571697-10 2008 Chemically cleaved glycosaminoglycan (GAG) chains analyzed by SDS-PAGE and size exclusion chromatography were larger for proteoglycans from thrombin treated cells. Glycosaminoglycans 38-41 coagulation factor II, thrombin Homo sapiens 140-148 18571697-17 2008 Thus, thrombin has actions on VSMCs which increase the length and modify the sulfation pattern of GAG chains on proteoglycans in a manner that would enhance the binding of LDL. Glycosaminoglycans 98-101 coagulation factor II, thrombin Homo sapiens 6-14 17658885-0 2007 Glycosaminoglycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers. Glycosaminoglycans 0-18 coagulation factor II, thrombin Homo sapiens 142-150 15383472-2 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors. Glycosaminoglycans 34-52 coagulation factor II, thrombin Homo sapiens 70-78 15292227-8 2004 Collectively, our results support a "double bridge" mechanism for HCII inhibition of thrombin in the presence of glycosaminoglycans, which relies in part on ternary complex formation but is primarily dominated by an allosteric process involving contact of the "hirudin-like" domain of HCII with thrombin exosite-1. Glycosaminoglycans 113-131 coagulation factor II, thrombin Homo sapiens 85-93 15292227-8 2004 Collectively, our results support a "double bridge" mechanism for HCII inhibition of thrombin in the presence of glycosaminoglycans, which relies in part on ternary complex formation but is primarily dominated by an allosteric process involving contact of the "hirudin-like" domain of HCII with thrombin exosite-1. Glycosaminoglycans 113-131 coagulation factor II, thrombin Homo sapiens 295-303 15196911-3 2004 In the presence of glycosaminoglycans, AT and PCI had significantly reduced thrombin inhibition with Toggle-25, but it was only reduced 3-fold for HCII. Glycosaminoglycans 19-37 coagulation factor II, thrombin Homo sapiens 76-84 15320789-0 2004 Novel human plasma proteins, IHRP (acute phase protein) and PHBP (serine protease), which bind to glycosaminoglycans. Glycosaminoglycans 98-116 coagulation factor II, thrombin Homo sapiens 66-81 15311269-2 2004 Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans. Glycosaminoglycans 146-164 coagulation factor II, thrombin Homo sapiens 4-12 12818259-0 2003 Additive thrombin inhibition by fast moving heparin and dermatan sulfate explains the anticoagulant effect of sulodexide, a natural mixture of glycosaminoglycans. Glycosaminoglycans 143-161 coagulation factor II, thrombin Homo sapiens 9-17 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). Glycosaminoglycans 43-61 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). Glycosaminoglycans 43-61 coagulation factor II, thrombin Homo sapiens 270-278 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). Glycosaminoglycans 63-66 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). Glycosaminoglycans 63-66 coagulation factor II, thrombin Homo sapiens 270-278 14962227-5 2004 Nucleotide sequencing of amplified DNA revealed a novel mutation, Glu (GAG) to Gly (GGG) at residue 29, which normally undergoes gamma-carboxylation within the Gla domain of prothrombin. Glycosaminoglycans 71-74 coagulation factor II, thrombin Homo sapiens 174-185 15013278-0 2003 Prolonged bleeding time induced by anticoagulant glycosaminoglycans in dogs is associated with the inhibition of thrombin-induced platelet aggregation. Glycosaminoglycans 49-67 coagulation factor II, thrombin Homo sapiens 113-121 12413592-1 2002 Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans. Glycosaminoglycans 235-253 coagulation factor II, thrombin Homo sapiens 4-12 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. Glycosaminoglycans 28-45 coagulation factor II, thrombin Homo sapiens 94-102 12169660-5 2002 HCII inhibits thrombin, the final protease of the coagulation cascade, in a glycosaminoglycan-dependent manner that involves the release of a sequestered hirudin-like N-terminal tail for interaction with thrombin. Glycosaminoglycans 76-93 coagulation factor II, thrombin Homo sapiens 14-22 12169660-5 2002 HCII inhibits thrombin, the final protease of the coagulation cascade, in a glycosaminoglycan-dependent manner that involves the release of a sequestered hirudin-like N-terminal tail for interaction with thrombin. Glycosaminoglycans 76-93 coagulation factor II, thrombin Homo sapiens 204-212 11460008-7 2001 The low second-order rate constant and the lack of a significant interaction in plasma suggest that the inhibition of thrombin by C1-INH has a minor role in circulating blood; however, its role might be important at the endothelial surface, where high concentrations of glycosaminoglycans occur. Glycosaminoglycans 270-288 coagulation factor II, thrombin Homo sapiens 118-126 11856753-8 2002 D72N/Y73F/D75N rHCII and D75K rHCII were significantly more active than wt-rHCII in a plasma-based thrombin inhibition assay with glycosaminoglycans. Glycosaminoglycans 130-148 coagulation factor II, thrombin Homo sapiens 99-107 11856753-9 2002 These results indicate that improved thrombin inhibition in the AR2 HCII mutants is mediated by enhanced interactions between the acidic domain and anion-binding exosite-1 of thrombin and that AR2 may be a "molecular rheostat" to promote thrombin inhibition in the presence of glycosaminoglycans. Glycosaminoglycans 277-295 coagulation factor II, thrombin Homo sapiens 37-45 11856753-9 2002 These results indicate that improved thrombin inhibition in the AR2 HCII mutants is mediated by enhanced interactions between the acidic domain and anion-binding exosite-1 of thrombin and that AR2 may be a "molecular rheostat" to promote thrombin inhibition in the presence of glycosaminoglycans. Glycosaminoglycans 277-295 coagulation factor II, thrombin Homo sapiens 175-183 11856753-9 2002 These results indicate that improved thrombin inhibition in the AR2 HCII mutants is mediated by enhanced interactions between the acidic domain and anion-binding exosite-1 of thrombin and that AR2 may be a "molecular rheostat" to promote thrombin inhibition in the presence of glycosaminoglycans. Glycosaminoglycans 277-295 coagulation factor II, thrombin Homo sapiens 175-183 10574918-1 1999 Heparin cofactor II (HCII) is a serpin whose thrombin inhibition activity is accelerated by glycosaminoglycans. Glycosaminoglycans 92-110 coagulation factor II, thrombin Homo sapiens 45-53 11323006-1 2001 In the presence of glycosaminoglycans, thrombin is rapidly inactivated by two natural inhibitors secreted from liver: antithrombin (AT) is presumed to be the principal thrombin inhibitor in circulating blood, while for heparin cofactor II (HCII), a role outside circulation has been proposed. Glycosaminoglycans 19-37 coagulation factor II, thrombin Homo sapiens 39-47 11323006-1 2001 In the presence of glycosaminoglycans, thrombin is rapidly inactivated by two natural inhibitors secreted from liver: antithrombin (AT) is presumed to be the principal thrombin inhibitor in circulating blood, while for heparin cofactor II (HCII), a role outside circulation has been proposed. Glycosaminoglycans 19-37 coagulation factor II, thrombin Homo sapiens 122-130 11068038-3 2000 Thrombin inhibition by HCII without glycosaminoglycan was decreased approximately two-fold by the aptamer. Glycosaminoglycans 36-53 coagulation factor II, thrombin Homo sapiens 0-8 11776053-3 2000 The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system. Glycosaminoglycans 30-33 coagulation factor II, thrombin Homo sapiens 8-16 11776053-10 2000 GAG inhibited thrombin activity in the presence of HCII with a second order rate constant of 1.14 x 10(7) m-1.min-1, which was 4.6 times higher than that of ATIII. Glycosaminoglycans 0-3 coagulation factor II, thrombin Homo sapiens 14-22 10574918-12 1999 In a plasma-based assay, the glycosaminoglycan-dependent inhibition of thrombin by rHCII-CHis(6) was significantly greater compared with wt-rHCII. Glycosaminoglycans 29-46 coagulation factor II, thrombin Homo sapiens 71-79 9813026-1 1998 Site-directed mutagenesis was used to investigate the role of basic residues in the thrombin anion-binding exosite-I during formation of thrombin-antithrombin III (ATIII), thrombin-protease nexin 1 (PN1), and thrombin-heparin cofactor II (HCII) inhibitor complexes, in the absence and presence of glycosaminoglycans. Glycosaminoglycans 297-315 coagulation factor II, thrombin Homo sapiens 84-92 10447213-3 1999 By inhibiting thrombin we have previously shown that heparin, a highly negatively-charged glycosaminoglycan (GAG), suppresses the production of ET-1 by cultured human umbilical vein endothelial cells (HUVEC). Glycosaminoglycans 90-107 coagulation factor II, thrombin Homo sapiens 14-22 9692391-8 1998 GAG anti-thrombin activity was completely abolished by heparin lyase III. Glycosaminoglycans 0-3 coagulation factor II, thrombin Homo sapiens 9-17 9597755-1 1998 Thrombomodulin (TM) is an anticoagulant glycoprotein on the surface of endothelial cell that directly inhibits the procoagulant activities of thrombin, and the TM-thrombin complex accelerates thrombin-catalyzed activation of protein C. Soluble TM in urine has no glycosaminoglycan (GAG) chain which accelerates the anticoagulant activities. Glycosaminoglycans 263-280 coagulation factor II, thrombin Homo sapiens 163-171 9586576-4 1998 In vitro, the activity of cleavage of fibrinogen by thrombin or prothrombinase activity was more potently depressed by GAG-UTM than by r-UTM, and the generation of activated protein C by TM-thrombin complex was accelerated by GAG modification. Glycosaminoglycans 119-122 coagulation factor II, thrombin Homo sapiens 67-75 9597755-1 1998 Thrombomodulin (TM) is an anticoagulant glycoprotein on the surface of endothelial cell that directly inhibits the procoagulant activities of thrombin, and the TM-thrombin complex accelerates thrombin-catalyzed activation of protein C. Soluble TM in urine has no glycosaminoglycan (GAG) chain which accelerates the anticoagulant activities. Glycosaminoglycans 263-280 coagulation factor II, thrombin Homo sapiens 163-171 9597755-1 1998 Thrombomodulin (TM) is an anticoagulant glycoprotein on the surface of endothelial cell that directly inhibits the procoagulant activities of thrombin, and the TM-thrombin complex accelerates thrombin-catalyzed activation of protein C. Soluble TM in urine has no glycosaminoglycan (GAG) chain which accelerates the anticoagulant activities. Glycosaminoglycans 282-285 coagulation factor II, thrombin Homo sapiens 163-171 9597755-1 1998 Thrombomodulin (TM) is an anticoagulant glycoprotein on the surface of endothelial cell that directly inhibits the procoagulant activities of thrombin, and the TM-thrombin complex accelerates thrombin-catalyzed activation of protein C. Soluble TM in urine has no glycosaminoglycan (GAG) chain which accelerates the anticoagulant activities. Glycosaminoglycans 282-285 coagulation factor II, thrombin Homo sapiens 163-171 8384442-0 1993 Role of the glycosaminoglycan component of thrombomodulin in its acceleration of the inactivation of single-chain urokinase-type plasminogen activator by thrombin. Glycosaminoglycans 12-29 coagulation factor II, thrombin Homo sapiens 154-162 7806495-3 1994 Thrombin is inhibited by the serpins antithrombin and heparin cofactor II (HCiI) in reactions that are accelerated markedly by specific glycosaminoglycans. Glycosaminoglycans 136-154 coagulation factor II, thrombin Homo sapiens 0-8 7806495-5 1994 The present study examines the role of anion-binding exosite II of thrombin in the interaction with glycosaminoglycans and HCII. Glycosaminoglycans 100-118 coagulation factor II, thrombin Homo sapiens 67-75 7806495-6 1994 Acceleration of thrombin inhibition by serpins in the presence of glycosaminoglycans is proposed to occur by a template mechanism, in which inhibitor and protease bind simultaneously to the same glycosaminoglycan chain, facilitating their interaction. Glycosaminoglycans 66-84 coagulation factor II, thrombin Homo sapiens 16-24 7806495-6 1994 Acceleration of thrombin inhibition by serpins in the presence of glycosaminoglycans is proposed to occur by a template mechanism, in which inhibitor and protease bind simultaneously to the same glycosaminoglycan chain, facilitating their interaction. Glycosaminoglycans 66-83 coagulation factor II, thrombin Homo sapiens 16-24 7806495-8 1994 Specific mutations in exosite II (R89E, R245E, K248E, and K252E) disrupted thrombin binding to both dermatan sulfate and heparin, indicating that both glycosaminoglycans bind to a common site in exosite II. Glycosaminoglycans 151-169 coagulation factor II, thrombin Homo sapiens 75-83 8186357-2 1994 In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans. Glycosaminoglycans 111-129 coagulation factor II, thrombin Homo sapiens 28-36 8603018-0 1996 Thrombin-mediated activation of endogenous factor XI in plasma in the presence of physiological glycosaminoglycans occurs only with high concentrations of thrombin. Glycosaminoglycans 96-114 coagulation factor II, thrombin Homo sapiens 0-8 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. Glycosaminoglycans 98-116 coagulation factor II, thrombin Homo sapiens 62-70 8807725-4 1996 The generation of thrombin seems to be a pivotal event in thrombogenesis, and inactivation of this enzyme has been attempted for many years with heparin, low-molecular-weight heparin, and other glycosaminoglycans. Glycosaminoglycans 194-212 coagulation factor II, thrombin Homo sapiens 18-26 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. Glycosaminoglycans 19-37 coagulation factor II, thrombin Homo sapiens 51-59 21244893-3 1994 Both heparin cofactor II and thrombin interact with highly negatively charged glycosaminoglycans like heparin and dermatan sulfate, and they both are leukocyte chemoattractants. Glycosaminoglycans 78-96 coagulation factor II, thrombin Homo sapiens 29-37 8339853-7 1993 This study shows an altered fibrinolytic response to increased thrombin activation in Type 1 diabetic patients and suggests that the administration of the glycosaminoglycan, Sulodexide, may help to reduce this phenomenon. Glycosaminoglycans 155-172 coagulation factor II, thrombin Homo sapiens 63-71 8440685-3 1993 In solution, heparin cofactor II inhibition of thrombin is accelerated by intact biglycan or decorin and by the dermatan sulfate-containing glycosaminoglycan (GAG) chains prepared from the proteoglycans, while core protein from cartilage biglycan had no effect. Glycosaminoglycans 140-157 coagulation factor II, thrombin Homo sapiens 47-55 8440685-3 1993 In solution, heparin cofactor II inhibition of thrombin is accelerated by intact biglycan or decorin and by the dermatan sulfate-containing glycosaminoglycan (GAG) chains prepared from the proteoglycans, while core protein from cartilage biglycan had no effect. Glycosaminoglycans 159-162 coagulation factor II, thrombin Homo sapiens 47-55 8440685-5 1993 Treatment of skin decorin and GAG chains with chondroitinase ABC totally eliminated the ability of these compounds to accelerate thrombin inhibition by heparin cofactor II suggesting that dermatan sulfate was responsible for this action. Glycosaminoglycans 30-33 coagulation factor II, thrombin Homo sapiens 129-137 8429040-3 1993 Thrombin is inhibited by the serpins antithrombin III and heparin cofactor II in a reaction that is dramatically accelerated by glycosaminoglycans. Glycosaminoglycans 128-146 coagulation factor II, thrombin Homo sapiens 0-8 8429008-1 1993 Heparin cofactor II and antithrombin are plasma serine proteinase inhibitors whose ability to inhibit alpha-thrombin is accelerated by glycosaminoglycans. Glycosaminoglycans 135-153 coagulation factor II, thrombin Homo sapiens 28-36 8429040-8 1993 In contrast, the rate constant for inhibition by heparin cofactor II without glycosaminoglycan was 4.3 x 10(4) M-1 min-1 for wild-type thrombin; rates were 10-fold slower for thrombin K52E and 2- to 3-fold slower for thrombins R68E and R70E. Glycosaminoglycans 77-94 coagulation factor II, thrombin Homo sapiens 135-143 8429008-7 1993 We also found that heparin cofactor II formed a SDS-resistant bimolecular complex with Quick II and alpha-thrombin at similar rates and the rate of complex formation was accelerated in the presence of glycosaminoglycans. Glycosaminoglycans 201-219 coagulation factor II, thrombin Homo sapiens 106-114 8429008-9 1993 The importance of heparin cofactor II as a thrombin regulator will depend upon its ability to interact with glycosaminoglycans and the functional availability of thrombin exosites. Glycosaminoglycans 108-126 coagulation factor II, thrombin Homo sapiens 43-51 8431448-5 1993 In addition, a qualitative analysis was performed by determining the formation of SDS-stable, equimolar complexes between thrombin and PAI-1 in the presence of various glycosaminoglycans. Glycosaminoglycans 168-186 coagulation factor II, thrombin Homo sapiens 122-130 8429040-10 1993 Compared to wild-type thrombin, the rate of inhibition by HCII with glycosaminoglycan was 5- to 15-fold slower for thrombins K52E and R70E and 50- to over 100-fold slower for thrombin R68E. Glycosaminoglycans 68-85 coagulation factor II, thrombin Homo sapiens 22-30 8429040-10 1993 Compared to wild-type thrombin, the rate of inhibition by HCII with glycosaminoglycan was 5- to 15-fold slower for thrombins K52E and R70E and 50- to over 100-fold slower for thrombin R68E. Glycosaminoglycans 68-85 coagulation factor II, thrombin Homo sapiens 115-123 1740413-4 1992 Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin. Glycosaminoglycans 34-52 coagulation factor II, thrombin Homo sapiens 203-211 1740413-4 1992 Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin. Glycosaminoglycans 34-52 coagulation factor II, thrombin Homo sapiens 255-263 1740413-4 1992 Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin. Glycosaminoglycans 34-52 coagulation factor II, thrombin Homo sapiens 255-263 1740413-9 1992 Our results suggest that the beta-loop region of anion-binding exosite-I in alpha-thrombin, which is not present in gamma T-thrombin, is essential for the rapid inhibition reaction by HC in the presence of a glycosaminoglycan. Glycosaminoglycans 208-225 coagulation factor II, thrombin Homo sapiens 82-90 1939083-0 1991 The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans. Glycosaminoglycans 113-131 coagulation factor II, thrombin Homo sapiens 85-93 1939083-11 1991 The stimulatory effect of glycosaminoglycans on native rHCII was decreased by a C-terminal hirudin peptide which binds to anion-binding exosite I of alpha-thrombin. Glycosaminoglycans 26-44 coagulation factor II, thrombin Homo sapiens 155-163 1939083-12 1991 Furthermore, the ability of native rHCII to inhibit gamma-thrombin, which lacks the binding site for hirudin, was stimulated weakly by glycosaminoglycans. Glycosaminoglycans 135-153 coagulation factor II, thrombin Homo sapiens 58-66 2164263-6 1990 These findings could be due to the different, additional anti-thrombin activities of these glycosaminoglycans and/or to their different anti-prothrombinase activities. Glycosaminoglycans 91-109 coagulation factor II, thrombin Homo sapiens 62-70 1902471-1 1991 Heparin cofactor II (HC) is a plasma serine proteinase inhibitor (serpin) that inhibits alpha-thrombin in a reaction that is dramatically enhanced by heparin and other glycosaminoglycans/polyanions. Glycosaminoglycans 168-186 coagulation factor II, thrombin Homo sapiens 94-102 1780805-3 1991 A radioimmunoassay for recombinant (r.) hirudin was used to study the effect of heparin and other glycosaminoglycans (GAG"s) on interactions between hirudin and thrombin. Glycosaminoglycans 118-123 coagulation factor II, thrombin Homo sapiens 161-169 1646210-1 1991 Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII). Glycosaminoglycans 28-45 coagulation factor II, thrombin Homo sapiens 75-83 2226466-1 1990 There is evidence that by catalyzing thrombin inhibition, several glycosaminoglycans can inhibit the thrombin-mediated amplification reactions of coagulation and thereby delay prothrombin activation. Glycosaminoglycans 66-84 coagulation factor II, thrombin Homo sapiens 37-45 2226466-1 1990 There is evidence that by catalyzing thrombin inhibition, several glycosaminoglycans can inhibit the thrombin-mediated amplification reactions of coagulation and thereby delay prothrombin activation. Glycosaminoglycans 66-84 coagulation factor II, thrombin Homo sapiens 101-109 2318889-0 1990 On the activation of human leuserpin-2, a thrombin inhibitor, by glycosaminoglycans. Glycosaminoglycans 65-83 coagulation factor II, thrombin Homo sapiens 42-50 2318889-3 1990 One of these regions, which encompasses a dimeric structure enriched in basic amino acids, is required for both glycosaminoglycan binding and glycosaminoglycan-mediated acceleration of thrombin inhibition. Glycosaminoglycans 112-129 coagulation factor II, thrombin Homo sapiens 185-193 2318889-3 1990 One of these regions, which encompasses a dimeric structure enriched in basic amino acids, is required for both glycosaminoglycan binding and glycosaminoglycan-mediated acceleration of thrombin inhibition. Glycosaminoglycans 142-159 coagulation factor II, thrombin Homo sapiens 185-193 2318889-7 1990 The key feature of this model is the suggestion that the glycosaminoglycan-enhanced reaction between hLS2 and thrombin is mediated by at least two regions of contact, involving both the reactive center region and the acidic domain of hLS2. Glycosaminoglycans 57-74 coagulation factor II, thrombin Homo sapiens 110-118 2083865-8 1990 The activities of thrombin and other serine proteases are modulated by the serine protease inhibitors (serpins), including antithrombin III and heparin cofactor II which are important in regulating the physiological anticoagulant action of glycosaminoglycans at the endothelium and the pharmacological action of heparin. Glycosaminoglycans 240-258 coagulation factor II, thrombin Homo sapiens 18-26