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Titolo:
An angiogenic laminin site and its antagonist bind through the alpha v beta 3 and alpha 5 beta 1 integrins
Autore:
Ponce, ML; Nomizu, M; Kleinman, HK;
Indirizzi:
NIDCR, CDBRB, NIH, Bethesda, MD 20892 USA NIDCR Bethesda MD USA 20892NIDCR, CDBRB, NIH, Bethesda, MD 20892 USA Hokkaido Univ, Grad Sch Environm Earth Sci, Sapporo, Hokkaido 060, Japan Hokkaido Univ Sapporo Hokkaido Japan 060 ci, Sapporo, Hokkaido 060, Japan
Titolo Testata:
FASEB JOURNAL
fascicolo: 8, volume: 15, anno: 2001,
pagine: 1389 - 1397
SICI:
0892-6638(200106)15:8<1389:AALSAI>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-ENDOTHELIAL CELLS; TUMOR-GROWTH; SYNTHETIC PEPTIDES; ADHESION MOLECULE; ALPHA-1 CHAIN; GAMMA-1 CHAIN; IDENTIFICATION; ALPHA(V)BETA(3); RECEPTORS; PROTEIN;
Keywords:
angiogenesis; laminin-1; bFGF; endothelium; peptides;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Kleinman, HK NIDCR, CDBRB, NIH, Bldg 30,Room 433,30 Convent Dr, Bethesda, MD 20892 USA NIDCR Bldg 30,Room 433,30 Convent Dr Bethesda MD USA 20892 SA
Citazione:
M.L. Ponce et al., "An angiogenic laminin site and its antagonist bind through the alpha v beta 3 and alpha 5 beta 1 integrins", FASEB J, 15(8), 2001, pp. 1389-1397

Abstract

Angiogenesis is important for wound healing, tumor growth, and metastasis. Endothelial cells differentiate into capillary-like structures on a laminin-1-rich matrix (Matrigel). We previously identified 20 angiogenic sites onlaminin-1 (alpha1 beta1 gamma1) by screening 559 overlapping synthetic peptides. C16, the most potent gamma1 chain peptide, blocked laminin-1-mediated adhesion and was the only gamma1 chain peptide to block attachment to both collagen I and fibronectin. This suggested that C16 was acting via a receptor common to these substrates. We demonstrated that C16 is angiogenic in vivo. Affinity chromatography identified the integrins alpha5 beta1 and alphav beta3 as surface receptors. Blocking antibodies confirmed the role of these receptors in C16 adhesion. C16 does not contain an RGD sequence and, as expected, an RGD-containing peptide did not block C16 adhesion nor did C16 act via MAP kinase phosphorylation. Furthermore, we identified a C16 scrambled sequence, C16S, which antagonizes the angiogenic activity of bFGF andof C16 by binding to the same receptors. Because the laminin gamma1 chain is ubiquitous in most tissues, C16 is likely an important functional site. Since the biological activity of C16 is blocked by a scrambled peptide, C16S may serve as an anti-angiogenic therapeutic agent.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 07:58:37