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Titolo:
SYNDECANS, HEPARAN-SULFATE PROTEOGLYCANS, MAINTAIN THE PROTEOLYTIC BALANCE OF ACUTE WOUND FLUIDS
Autore:
KAINULAINEN V; WANG HM; SCHICK C; BERNFIELD M;
Indirizzi:
HARVARD UNIV,CHILDRENS HOSP,SCH MED,ENDERS 9,300 LONGWOOD AVE BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT PEDIAT,DIV DEV & NEWBORN BIOL BOSTON MA 02115
Titolo Testata:
The Journal of biological chemistry
fascicolo: 19, volume: 273, anno: 1998,
pagine: 11563 - 11569
SICI:
0021-9258(1998)273:19<11563:SHPMTP>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-SURFACE PROTEOGLYCAN; FIBROBLAST GROWTH-FACTOR; PROTEINASE-INHIBITORS; ALPHA-1-PROTEINASE INHIBITOR; EXTRACELLULAR-MATRIX; NEUTROPHIL ELASTASE; ENDOTHELIAL-CELLS; DEGRADATION; BINDING; FIBRONECTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
V. Kainulainen et al., "SYNDECANS, HEPARAN-SULFATE PROTEOGLYCANS, MAINTAIN THE PROTEOLYTIC BALANCE OF ACUTE WOUND FLUIDS", The Journal of biological chemistry, 273(19), 1998, pp. 11563-11569

Abstract

An imbalance between proteases and antiproteases is thought to play arole 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 (K-d = 56 nM) and elastase (K-d= 35 nM) tightly and reduces the affinity of these proteases for their physiological inhibitors. Purified syndecan-1 ectodomain protects cathepsin G from inhibition by alpha(1)-antichymotrypsin and squamous cell carcinoma antigen 2 and elastase from inhibition by alpha(1)-proteinase inhibitor by decreasing second order rate constants for protease-antiprotease associations (k(ass),,,) 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 proteolyticactivities 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/08/20 alle ore 13:24:26