PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15265919-3 2004 Previous studies have shown that tryptase binds tightly to heparin, and that heparin is required in the assembly of the tryptase tetramer as well as for stabilization of the active tetramer. Heparin 77-84 tryptase alpha/beta 1 Mus musculus 120-128 23223449-5 2013 The activities of tryptase and carboxypeptidase-A were decreased in HS6ST-2(-/-)-FSMCs in which 6-O-sulfation of heparin was decreased at 50% of WT-FSMCs and almost lost in HS6ST-1(-/-)/HS6ST-2(-/-)-FSMCs, which lacked the 6-O-sulfation in heparin nearly completely. Heparin 113-120 tryptase alpha/beta 1 Mus musculus 18-26 23223449-5 2013 The activities of tryptase and carboxypeptidase-A were decreased in HS6ST-2(-/-)-FSMCs in which 6-O-sulfation of heparin was decreased at 50% of WT-FSMCs and almost lost in HS6ST-1(-/-)/HS6ST-2(-/-)-FSMCs, which lacked the 6-O-sulfation in heparin nearly completely. Heparin 240-247 tryptase alpha/beta 1 Mus musculus 18-26 17498058-5 2007 MC-like cells that contain tryptase-heparin complexes in their secretory granules have been identified in the Ciona intestinalis and Styela plicata urochordates that appeared approximately 500 million years ago. Heparin 36-43 tryptase alpha/beta 1 Mus musculus 27-35 15265919-0 2004 Histidines are critical for heparin-dependent activation of mast cell tryptase. Heparin 28-35 tryptase alpha/beta 1 Mus musculus 70-78 15265919-4 2004 Because the interaction of tryptase with heparin is optimal at acidic pH, we investigated in this study whether His residues are of importance for the heparin binding, tetramerization, and activation of the tryptase mouse mast cell protease 6. Heparin 41-48 tryptase alpha/beta 1 Mus musculus 27-35 15265919-3 2004 Previous studies have shown that tryptase binds tightly to heparin, and that heparin is required in the assembly of the tryptase tetramer as well as for stabilization of the active tetramer. Heparin 59-66 tryptase alpha/beta 1 Mus musculus 33-41 15265919-10 2004 Taken together, this study shows that surface-exposed histidines mediate the interaction of mast cell tryptase with heparin and are of critical importance in the formation of active tryptase tetramers. Heparin 116-123 tryptase alpha/beta 1 Mus musculus 102-110 7642636-8 1995 Site-directed mutagenesis confirmed the prediction that the conversion of His residues 8,68, and 70 in the positively charged region into Glu prevents the binding of pro-mMCP-7 to heparin. Heparin 180-187 tryptase alpha/beta 1 Mus musculus 170-176 11533057-0 2001 Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin. Heparin 42-49 tryptase alpha/beta 1 Mus musculus 102-110 11533057-0 2001 Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin. Heparin 42-49 tryptase alpha/beta 1 Mus musculus 160-168 11533057-0 2001 Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin. Heparin 218-225 tryptase alpha/beta 1 Mus musculus 102-110 11533057-1 2001 Mast cell tryptase is stored as an active tetramer in complex with heparin in mast cell secretory granules. Heparin 67-74 tryptase alpha/beta 1 Mus musculus 10-18 11533057-2 2001 Previously, we demonstrated the dependence on heparin for the activation/tetramer formation of a recombinant tryptase. Heparin 46-53 tryptase alpha/beta 1 Mus musculus 109-117 11533057-4 2001 The ability of heparin-related saccharides to activate a recombinant murine tryptase, mouse mast cell protease-6 (mMCP-6), was strongly dependent on anionic charge density and size. Heparin 15-22 tryptase alpha/beta 1 Mus musculus 76-84 11533057-5 2001 The dose-response curve for heparin-induced mMCP-6 activation displayed a bell-shaped appearance, indicating that heparin acts by binding to more than one tryptase monomer simultaneously. Heparin 28-35 tryptase alpha/beta 1 Mus musculus 155-163 11533057-5 2001 The dose-response curve for heparin-induced mMCP-6 activation displayed a bell-shaped appearance, indicating that heparin acts by binding to more than one tryptase monomer simultaneously. Heparin 114-121 tryptase alpha/beta 1 Mus musculus 155-163 11533057-10 2001 Our results suggest a model for tryptase tetramer formation that involves bridging of tryptase monomers by heparin or other highly sulfated polysaccharides of sufficient chain length. Heparin 107-114 tryptase alpha/beta 1 Mus musculus 32-40 10617625-2 2000 Mouse mast cell protease (mMCP) 6 and mMCP-7 are homologous tryptases stored in granules as macromolecular complexes with heparin and/or chondroitin sulfate E containing serglycin proteoglycans. Heparin 122-129 tryptase alpha/beta 1 Mus musculus 38-44 10536969-7 1999 Heparin affinity chromatography caused a high loss of tryptase and residual protein contamination. Heparin 0-7 tryptase alpha/beta 1 Mus musculus 54-62 7642636-4 1995 to understand the interaction of mMCP-7 with heparin inside and outside the mast cell, this trytase was first studied by comparative protein modeling. Heparin 45-52 tryptase alpha/beta 1 Mus musculus 33-39 7642636-6 1995 Although mMCP-7 lacks known linear sequences of amino acis that interact with heparin, the three-dimensional model of mMCP-7 revealed an area on the surface of the folded protein away from the substrate-binding site that exhibits a strong positive electrostatic potential at the acidic pH of the granule. Heparin 78-85 tryptase alpha/beta 1 Mus musculus 9-15 7642636-7 1995 In agreement with this calculation, recombinant pro-mMCP-7 bound to a heparin-affinity column at pH 5.5 and readily dissociated from the column at pH > 6.5. Heparin 70-77 tryptase alpha/beta 1 Mus musculus 52-58 11533057-10 2001 Our results suggest a model for tryptase tetramer formation that involves bridging of tryptase monomers by heparin or other highly sulfated polysaccharides of sufficient chain length. Heparin 107-114 tryptase alpha/beta 1 Mus musculus 86-94 11401583-0 2001 Heparin antagonists are potent inhibitors of mast cell tryptase. Heparin 0-7 tryptase alpha/beta 1 Mus musculus 55-63 11401583-3 2001 Tryptase is present in a macromolecular complex with heparin proteoglycan where the interaction with heparin is known to be essential for maintaining enzymatic activity. Heparin 53-60 tryptase alpha/beta 1 Mus musculus 0-8 11401583-7 2001 We show that the heparin antagonists Polybrene and protamine are potent inhibitors of both human lung tryptase and of recombinant mouse tryptase (mouse mast cell protease 6). Heparin 17-24 tryptase alpha/beta 1 Mus musculus 102-110 11401583-7 2001 We show that the heparin antagonists Polybrene and protamine are potent inhibitors of both human lung tryptase and of recombinant mouse tryptase (mouse mast cell protease 6). Heparin 17-24 tryptase alpha/beta 1 Mus musculus 136-144 11041873-0 2000 Mechanism for activation of mouse mast cell tryptase: dependence on heparin and acidic pH for formation of active tetramers of mouse mast cell protease 6. Heparin 68-75 tryptase alpha/beta 1 Mus musculus 44-52 11041873-10 2000 When heparin was added at pH 6.0, enzymatically active higher molecular weight complexes were formed, e.g., a dominant approximately 200 kDa complex that may correspond to tryptase tetramers. Heparin 5-12 tryptase alpha/beta 1 Mus musculus 172-180 11041873-13 2000 The present paper thus indicates a crucial role for heparin in the formation of active mast cell tryptase. Heparin 52-59 tryptase alpha/beta 1 Mus musculus 97-105 7642636-11 1995 The heparin/mMCP-7 interaction, which depends on the tertiary structure of the tryptase, may be representative of a general control mechanism by which hematopoietic cells maximize storage of properly folded, enzymatically active proteins in their granules. Heparin 4-11 tryptase alpha/beta 1 Mus musculus 12-18 7642636-11 1995 The heparin/mMCP-7 interaction, which depends on the tertiary structure of the tryptase, may be representative of a general control mechanism by which hematopoietic cells maximize storage of properly folded, enzymatically active proteins in their granules. Heparin 4-11 tryptase alpha/beta 1 Mus musculus 79-87 32709152-2 2020 In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase. Heparin 81-88 tryptase alpha/beta 1 Mus musculus 27-35 2179409-5 1990 Dextran sulfate, like heparin, stabilizes the catalytic activity and quaternary structure of tryptase and also maintains the native secondary structure of the enzyme at and beyond a temperature of 40 degrees C. Dextran sulfate-stabilized tryptase therefore was used as an immunogen to which were produced three murine mAb (B2, C11, and G4) recognizing the catalytically active form of the enzyme. Heparin 22-29 tryptase alpha/beta 1 Mus musculus 93-101 2179409-9 1990 A pragmatic result of these newly generated antibodies is the affinity purification to homogeneity of active tryptase by sequential chromatography with B2 coupled to CH-Sepharose and heparin-agarose. Heparin 183-190 tryptase alpha/beta 1 Mus musculus 109-117 32709152-2 2020 In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase. Heparin 124-131 tryptase alpha/beta 1 Mus musculus 27-35 32709152-2 2020 In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase. Heparin 124-131 tryptase alpha/beta 1 Mus musculus 187-195 32709152-4 2020 Here we hypothesized that tryptase, as well as being stabilized by heparin, can be stabilized by DNA, the rationale being that the anionic charge of DNA could potentially substitute for that of heparin to execute this function. Heparin 67-74 tryptase alpha/beta 1 Mus musculus 26-34 32709152-4 2020 Here we hypothesized that tryptase, as well as being stabilized by heparin, can be stabilized by DNA, the rationale being that the anionic charge of DNA could potentially substitute for that of heparin to execute this function. Heparin 194-201 tryptase alpha/beta 1 Mus musculus 26-34 32709152-8 2020 Further, we showed that DNA-stabilized tryptase was more efficient in degrading nuclear core histones than heparin-stabilized enzyme. Heparin 107-114 tryptase alpha/beta 1 Mus musculus 39-47