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Heparinase selectively sheds heparan sulphate from the endothelial glycocalyx
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Published/Copyright:
December 20, 2007
Abstract
A healthy vascular endothelium is coated by the endothelial glycocalyx. Its main constituents are transmembrane syndecans and bound heparan sulphates. This structure maintains the physiological endothelial permeability barrier and prevents leukocyte and platelet adhesion, thereby mitigating inflammation and tissue oedema. Heparinase, a bacterial analogue to heparanase, is known to attack the glycocalyx. However, the exact extent and specificity of degradation is unresolved. We show by electron microscopy, immunohistological staining and quantitative measurements of the constituent parts, that heparinase selectively sheds heparan sulphate from the glycocalyx, but not the syndecans.
Received: 2007-7-9
Accepted: 2007-9-20
Published Online: 2007-12-20
Published in Print: 2008-01-01
©2008 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity
- Reassessing the role of a 3′-UTR-binding translational inhibitor in regulation of circadian bioluminescence rhythm in the dinoflagellate Gonyaulax
- Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1
- A new subfamily of bacterial glutamate/aspartate receptors
- Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system
- Collagen IV regulates Caco-2 cell spreading and p130Cas phosphorylation by FAK-dependent and FAK-independent pathways
- Differential effects of novel tumour-derived p53 mutations on the transformation of NIH-3T3 cells
- Employing Rhodobacter sphaeroides to functionally express and purify human G protein-coupled receptors
- Heparinase selectively sheds heparan sulphate from the endothelial glycocalyx
- Inhibition of human μ-calpain by conformationally constrained calpastatin peptides
- Cloning, expression and characterization of insulin-degrading enzyme from tomato (Solanum lycopersicum)
