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J Biol Chem, Vol. 273, Issue 19, 11563-11569, May 8, 1998
From the Division of Developmental and Newborn Biology, Department
of Pediatrics, Harvard Medical School, Boston,
Massachusetts 02115
An imbalance between proteases and antiproteases
is thought to play a role in the inflammatory injury that regulates
wound healing. The activities of some proteases and antiproteases found in inflammatory fluids can be modified in vitro by heparin,
a mast cell-derived glycosaminoglycan. Because syndecans, a family of
cell surface heparan sulfate proteoglycans, are the major cellular source of heparin-like glycosaminoglycan, we asked whether syndecans modify protease activities in vivo.
Syndecan-1 and syndecan-4 ectodomains are shed into acute human dermal
wound fluids (Subramanian, S. V., Fitzgerald, M. L., and
Bernfield, M. (1997) J. Biol. Chem. 272, 14713-14720). Moreover, purified syndecan-1 ectodomain binds cathepsin
G (Kd = 56 nM) and elastase
(Kd = 35 nM) tightly and reduces the
affinity of these proteases for their physiological inhibitors. Purified syndecan-1 ectodomain protects cathepsin G from inhibition by
1-antichymotrypsin and squamous cell carcinoma antigen 2 and elastase from inhibition by 1-proteinase inhibitor
by decreasing second order rate constants for protease-antiprotease
associations (kass) by 3700-, 32-, and 60-fold,
respectively. Both enzymatic degradation of heparan sulfate and
immunodepletion of the syndecan-1 and -4 in wound fluid reduce these
proteolytic activities in the fluid, indicating that the proteases in
the wound environment are regulated by interactions with syndecan
ectodomains. Thus, syndecans are shed into acute wound fluids, where
they can modify the proteolytic balance of the fluid. This suggests a
novel physiological role for these soluble heparan sulfate
proteoglycans.
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