Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.2.2.7 (heparinase)
 1,270 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To assess the contribution of mast cells to the maintenance of blood fluidity, the hindlimb vasculature of mast cell-deficient mice (W/Wv) and littermates containing normal levels of mast cells (+/+), were perfused with purified human thrombin and antithrombin. Enzyme-inhibitor complex generation within the vasculature was enhanced to a comparable extent for W/Wv and +/+ mice over the uncatalyzed rate, that level of complex produced within a similar time interval in the absence of heparin. Perfusion of purified Flavobacterium heparinase prior to infusion of the hemostatic components, or perfusion of antithrombin modified at the heparin-binding domain, reduced W/Wv and +/+ hindlimb thrombin-antithrombin complex formation to the uncatalyzed rate. To further define the cellular source of the vascular-associated heparin-like molecules, endothelial cells isolated from epididymal fat pads of W/Wv and +/+ mice were grown in vitro. The acceleration of thrombin-antithrombin interactions in the presence of endothelial cell-derived glycosaminoglycans was similar for W/Wv and +/+ mice, was abolished with purified bacterial heparinase, and was expressed to only a minor extent when utilizing modified antithrombin. The biologically active mucopolysaccharides appear to be present on the cell surface.
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PMID:Anticoagulantly active heparin-like molecules from mast cell-deficient mice. 370 60

Cultured microvascular endothelial cells isolated from rat epididymal fat pads produce glycosaminoglycans that accelerate thrombin-antithrombin complex formation. The heparinlike nature of these macromolecules was established by complete destruction of their anticoagulant activity employing purified Flavobacterium heparinase. Only 15% of the biologic activity of these complex carbohydrates was expressed when the heparin binding domain on the protease inhibitor was chemically modified at the Trp 49 residue. The anticoagulantly active species contains disaccharides which constitute the unique antithrombin binding region of the mucopolysaccharide. Removal of the biologically active heparinlike components from endothelial cells with 0.05% trypsin suggests that these molecular species are present on the cell surface.
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PMID:Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells. 397 Jun 99