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Titolo:
REGULATED SHEDDING OF SYNDECAN-1 AND SYNDECAN-4 ECTODOMAINS BY THROMBIN AND GROWTH-FACTOR RECEPTOR ACTIVATION
Autore:
SUBRAMANIAN SV; FITZGERALD ML; BERNFIELD M;
Indirizzi:
HARVARD UNIV,SCH MED,JOINT PROGRAM NEONATOL,300 LONGWOOD AVE BOSTON MA 02115 HARVARD UNIV,SCH MED,JOINT PROGRAM NEONATOL BOSTON MA 02115
Titolo Testata:
The Journal of biological chemistry
fascicolo: 23, volume: 272, anno: 1997,
pagine: 14713 - 14720
SICI:
0021-9258(1997)272:23<14713:RSOSAS>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPARAN-SULFATE PROTEOGLYCANS; CELL-SURFACE PROTEOGLYCAN; MAMMARY EPITHELIAL-CELLS; FACTOR-ALPHA PRECURSOR; WOUND FLUID; MOLECULAR-CLONING; ENDOTHELIAL-CELLS; FINE-STRUCTURE; IL-6 RECEPTOR; CLEAVAGE SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
69
Recensione:
Indirizzi per estratti:
Citazione:
S.V. Subramanian et al., "REGULATED SHEDDING OF SYNDECAN-1 AND SYNDECAN-4 ECTODOMAINS BY THROMBIN AND GROWTH-FACTOR RECEPTOR ACTIVATION", The Journal of biological chemistry, 272(23), 1997, pp. 14713-14720

Abstract

The syndecan family of transmembrane heparan sulfate proteoglycans isabundant on the surface of all adherent mammalian cells. Syndecans bind and modify the action of various growth factors/cytokines, proteases/antiproteases, cell adhesion molecules, and extracellular matrix components. Syndecan expression is highly regulated during wound repair, a process orchestrated by many of these effecters. Each syndecan ectodomain is shed constitutively by cultured cells, but the mechanism and significance of this shedding are not understood. Therefore, we examined (i) whether physiological agents active during wound repair influence syndecan shedding, and (ii) whether wound fluids contain shed syndecan ectodomains. Using SVEC4-10 endothelial cells we find that certainproteases and growth factors accelerate shedding of the syndecan-1 and -4 ectodomains. Protease-accelerated shedding is completely inhibited by serum-containing media. Thrombin activity is duplicated by the 14-amino acid thrombin receptor agonist peptide that directly activates the thrombin receptor and is not inhibited by serum. Epidermal growth factor family members accelerate shedding but FGF-S, platelet-derived growth factor-AB, transforming growth factor-beta, tumor necrosis factor-cu, and vascular endothelial cell growth factor 165 do not. Shed ectodomains are soluble, stable in the conditioned medium, have the samesize core proteins regardless whether shed at a basal rate, or accelerated by thrombin or epidermal growth factor-family members and are found in acute human dermal wound fluids. Thus, shedding is accelerated by activation of at least two distinct receptor classes, Gr protein-coupled (thrombin) and protein tyrosine kinase (epidermal growth factor). Proteases and growth factors active during wound repair can accelerate syndecan shedding from cell surfaces. Regulated shedding of syndecans suggests physiological roles for the soluble proteoglycan ectodomains.

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Documento generato il 03/06/20 alle ore 20:16:02