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Titolo:
ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alpha v beta 3 integrin through an RGD-independent mechanism
Autore:
Cal, S; Freije, JMP; Lopez, JM; Takada, Y; Lopez-Otin, C;
Indirizzi:
Univ Oviedo, Fac Med, Inst Oncol, Dept Bioquim & Biol Mol, E-33006 Oviedo,Spain Univ Oviedo Oviedo Spain E-33006 ioquim & Biol Mol, E-33006 Oviedo,Spain Univ Oviedo, Fac Med, Inst Oncol, Dept Morfol & Biol Celular, E-33006 Oviedo, Spain Univ Oviedo Oviedo Spain E-33006 l & Biol Celular, E-33006 Oviedo, Spain Scripps Clin & Res Inst, Dept Vasc Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 4, volume: 11, anno: 2000,
pagine: 1457 - 1469
SICI:
1059-1524(200004)11:4<1457:A2AHDT>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NECROSIS-FACTOR-ALPHA; MOLECULAR-CLONING; ENDOTHELIAL-CELLS; METALLOPROTEINASE-DISINTEGRIN; DIVALENT-CATIONS; BETA-SUBUNIT; IN-VIVO; PROTEIN; EXPRESSION; SPERM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
69
Recensione:
Indirizzi per estratti:
Indirizzo: Lopez-Otin, C Univ Oviedo, Fac Med, Inst Oncol, Dept Bioquim & Biol Mol, E-33006 Oviedo,Spain Univ Oviedo Oviedo Spain E-33006 Mol, E-33006 Oviedo,Spain
Citazione:
S. Cal et al., "ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alpha v beta 3 integrin through an RGD-independent mechanism", MOL BIOL CE, 11(4), 2000, pp. 1457-1469

Abstract

ADAM 23 (a disintegrin and metalloproteinase domain)/MDC3 (metalloprotease, disintegrin, and cysteine-rich domain) is a member of the disintegrin family of proteins expressed in fetal and adult brain. Ln this work we show that the disintegrin-like domain of ADAM 23 produced in Escherichia coli and immobilized on culture dishes promotes attachment of different human cells of neural origin, such as neuroblastoma cells (NB100 and SH-S(y)5(y)) or astrocytoma cells (U373 and U87 MG). Analysis ur ADAM 23 binding to integrinsrevealed a specific interaction with alpha v beta 3, mediated by a short amino acid sequence present in its putative disintegrin loop. This sequence lacks any RGD motif, which is a common structural determinant supporting alpha v beta 3-mediated interactions of diverse proteins, including other disintegrins. alpha v beta 3 also supported adhesion of HeLa cells transfectedwith a full-length cDNA for ADAM 23, extending the results obtained with the recombinant protein containing the disintegrin domain of ADAM 23. On thebasis of these results, we propose that ADAM 23, through its disintegrin-like domain, may function as an adhesion molecule involved in alpha v beta 3-mediated cell interactions occurring in normal and pathological processes,including progression of malignant tumors from neural origin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 06:16:14