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Titolo:
CELL-ADHESION AND INTEGRIN BINDING TO RECOMBINANT HUMAN FIBRILLIN-1
Autore:
PFAFF M; REINHARDT DP; SAKAI LY; TIMPL R;
Indirizzi:
SCRIPPS CLIN & RES FDN,10666 N TORREY PINES RD,VB2 LA JOLLA CA 92037 MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY SHRINERS HOSP CRIPPLED CHILDRENS,RES DEPT PORTLAND OR 97201
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 384, anno: 1996,
pagine: 247 - 250
SICI:
0014-5793(1996)384:3<247:CAIBTR>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARG-GLY-ASP; MARFAN-SYNDROME; MICROFIBRILS; COMPONENT; ORGANIZATION; PURIFICATION; VITRONECTIN; SEQUENCE; FIBERS; GENE;
Keywords:
FIBRILLIN-1; INTEGRIN; RGD; CELL ADHESION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
M. Pfaff et al., "CELL-ADHESION AND INTEGRIN BINDING TO RECOMBINANT HUMAN FIBRILLIN-1", FEBS letters, 384(3), 1996, pp. 247-250

Abstract

Fibrillin-1 is a major constituent of tissue microfibrils that occur in most connective tissues, either in close association with or independent of elastin. To test possible cell-adhesive functions of this protein, rye used recombinant human fibrillin-1 polypeptides produced in a mammalian expression system in cell attachment and solid-phase integrin binding assays. Fibrillin-1 polypeptides containing the single RGDsequence located in the fourth 8-cysteine domain, mediated distinct cell adhesion of a variety of cell lines and bound to purified integrinalpha V beta 3. Integrins alpha IIb beta 3, alpha 5 beta 1, alpha 2 beta 1 and alpha 1 beta 1 did not interact with any of the recombinant fibrillin-1 peptides. Our results indicate a novel role for fibrillin-1 in cellular interactions mediated via an RGD motif that is appropriately exposed for recognition by integrin alpha V beta 3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 07:15:41