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Titolo:
SPARC, a matricellular protein: at the crossroads of cell-matrix
Autore:
Brekken, RA; Sage, EH;
Indirizzi:
Hope Heart Inst, Dept Vasc Biol, Seattle, WA 98122 USA Hope Heart Inst Seattle WA USA 98122 ept Vasc Biol, Seattle, WA 98122 USA
Titolo Testata:
MATRIX BIOLOGY
fascicolo: 7, volume: 19, anno: 2000,
pagine: 569 - 580
SICI:
0945-053X(200012)19:7<569:SAMPAT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLLAGEN-BINDING EPITOPE; FIBROBLAST GROWTH-FACTOR; RAT EMBRYO FIBROBLASTS; HUMAN PULP CELLS; EXTRACELLULAR-MATRIX; CALCIUM-BINDING; ENDOTHELIAL-CELLS; EF-HAND; CAENORHABDITIS-ELEGANS; INSITU HYBRIDIZATION;
Keywords:
SPARC/osteonectin/BM-40; matricellular; cell-matrix interaction;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
85
Recensione:
Indirizzi per estratti:
Indirizzo: Sage, EH Hope Heart Inst, Dept Vasc Biol, 528 18th Ave, Seattle, WA 98122 USA Hope Heart Inst 528 18th Ave Seattle WA USA 98122 e, WA 98122 USA
Citazione:
R.A. Brekken e E.H. Sage, "SPARC, a matricellular protein: at the crossroads of cell-matrix", MATRIX BIOL, 19(7), 2000, pp. 569-580

Abstract

SPARC is a multifunctional glycoprotein that belongs to the matricellular group of proteins. It modulates cellular interaction with the extracellularmatrix (ECM) by its binding to structural matrix proteins, such as collagen and vitronectin, and by its abrogation of focal adhesions, features contributing to a counteradhesive effect on cells. SPARC inhibits cellular proliferation by an arrest of cells in the G1 phase of the cell cycle. It also regulates the activity of growth factors, such as platelet-derived growth factor (PDGF), fibroblast growth factor (FGF)-2, and vascular endothelial growth factor (VEGF). The expression of SPARC in adult animals is limited largely to remodeling tissue, such as bone, gut mucosa, and healing wounds, andit is prominent in tumors and in disorders associated with fibrosis. The crystal structure of two of the three domains of the protein has revealed a novel follistatin-like module and an extracellular calcium-binding (EC) module containing two EF-hand motifs. The follistatin-like module and the EC module are shared by at least four other proteins that comprise a family of SPARC-related genes. Targeted disruption of the SPARC locus in mice has shown that SPARC is important for lens transparency, as SPARC-null mice develop cataracts shortly after birth. SPARC is a prototypical matricellular protein that functions to regulate cell-matrix interactions and thereby influences many important physiological and pathological processes. (C) Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/08/20 alle ore 23:04:07