Premium
Effects of fibroblasts and endothelial cells on inactivation of target proteases by protease nexin‐1, heparin cofactor II, and C1‐inhibitor
Author(s) -
Hiramoto Sheree A.,
Cunningham Dennis D.
Publication year - 1988
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240360302
Subject(s) - proteases , thrombin , extracellular matrix , protease , heparin , biochemistry , chemistry , glycosaminoglycan , heparan sulfate , heparin cofactor ii , fibroblast , microbiology and biotechnology , biology , enzyme , in vitro , platelet , antithrombin , immunology
Previous studies have shown that glycosaminoglycans in the extracellular matrix accelerate the inactivation of target proteases by certain protease inhibitors. It has been suggested that the ability of the matrix of certain cells to accelerate some inhibitors but not others might reflect the site of action of the inhibitors. Previous studies showed that fibroblasts accelerate the inactivation of thrombin by protease nexin‐1, an inhibitor that appears to function at the surface of cells in extravascular tissues. The present experiments showed that endothelial cells also accelerate this reaction. The accelerative activity was accounted for by the extracellular matrix and was mostly due to heparan sulfate. Fibroblasts but not endothelial cells accelerated the inactivation of thrombin by heparin cofactor II, an abundant inhibitor in plasma. This is consistent with previous suggestions that heparin cofactor II inactivates thrombin when plasma is exposed to fibroblasts and smooth muscle cells. Neither fibroblasts nor endothelial cells accelerated the inactivation of C1s by plasma C1‐inhibitor.