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J. Biol. Chem., Vol. 268, Issue 6, 3920-3924, Feb, 1993
HC Whinna, HU Choi, LC Rosenberg and FC Church
Two small interstitial dermatan sulfate-containing proteoglycans, biglycan
and decorin, are present in extracellular matrices of skin, tendon,
ligament, and cartilage. We investigated the effects of biglycan and
decorin on the inhibition of alpha-thrombin by the serine proteinase
inhibitor heparin cofactor II. 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. L-Iduronic acid-rich skin decorin and GAG chains had a greater
accelerating effect than proteoglycan and GAG chains from cartilage that
had lower L-iduronic acid content. 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. Both biglycan and decorin
bound to type V collagen in a saturable and specific manner. Biglycan,
decorin, and core protein from biglycan competed for decorin binding to the
type V collagen, while only the intact proteoglycans competed for biglycan
binding. When bound to type V collagen, both biglycan and decorin
accelerated the heparin cofactor II/thrombin inhibition reaction as
efficiently as the proteoglycans in solution. Our results demonstrate that
heparin cofactor II in the presence of biglycan or decorin bound to type V
collagen provides a "thromboresistant surface," further suggesting a
physiological function for these proteins in regulating the extravascular
activities of thrombin.
Interaction of heparin cofactor II with biglycan and decorin
Department of Pathology, University of North Carolina School of Medicine, Chapel Hill 27599.
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