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Titolo:
SEQUENCE OF EXTRACELLULAR MOUSE PROTEIN BM-90 FIBULIN AND ITS CALCIUM-DEPENDENT BINDING TO OTHER BASEMENT-MEMBRANE LIGANDS/
Autore:
PAN TC; KLUGE M; ZHANG RZ; MAYER U; TIMPL R; CHU ML;
Indirizzi:
MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY THOMAS JEFFERSON UNIV,JEFFERSON INST MOLEC MED,DEPT BIOCHEM & MOLEC BIOL PHILADELPHIA PA 19107 THOMAS JEFFERSON UNIV,JEFFERSON INST MOLEC MED,DEPT DERMATOL PHILADELPHIA PA 19107
Titolo Testata:
European journal of biochemistry
fascicolo: 3, volume: 215, anno: 1993,
pagine: 733 - 740
SICI:
0014-2956(1993)215:3<733:SOEMPB>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
LAMININ-NIDOGEN COMPLEX; COLLAGEN TYPE-IV; EGF-LIKE DOMAINS; HUMAN FACTOR-IX; MURINE COMPLEMENT; MARFAN-SYNDROME; COMPONENT C-3; FACTOR-X; FIBULIN; FIBRONECTIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
T.C. Pan et al., "SEQUENCE OF EXTRACELLULAR MOUSE PROTEIN BM-90 FIBULIN AND ITS CALCIUM-DEPENDENT BINDING TO OTHER BASEMENT-MEMBRANE LIGANDS/", European journal of biochemistry, 215(3), 1993, pp. 733-740

Abstract

Partial sequence comparisons have recently indicated that two extracellular components, fibulin from human placenta and BM-90 from a basement-membrane-producing mouse tumor, are either identical or closely related proteins. In this study, a complete sequence analysis of mouse BM-90 cDNA showed a 539-residue N-terminal core structure (domains I andII), which was 85% identical with the same core structure of human fibulin. A 137-residue C-terminal sequence (domain III) was unique for BM-90 and could also be identified by Edman degradation. This suggesteda novel splice product, variant D, which is characteristic for the mouse tumor. A second 117-residue C-terminal sequence (domain III) was identified in additional mouse cDNA clones and showed 91% identity withthe region specific for variant C of fibulin. Northern blots using mouse cells demonstrated two mRNA species, 2.7 kb and 2.3 kb, which encoded the variants D and C, respectively. The sequence of BM-90/fibulin indicates the presence of nine epidermal-growth-factor-like repeats inthe core domain-II structure, eight of which contain consensus motifsfor calcium binding. This binding is apparently important for the interaction of BM-90 with laminin and nidogen and for some weaker interactions with collagen IV Further binding of BM-90 was demonstrated to fibronectin and BM-90 itself, but did not depend on calcium. Major binding sites for BM-90 were identified at a C-terminal segment of laminin A chain and at the N-terminus of nidogen. The broad interaction repertoire of BM-90 is comparable to that of nidogen and both proteins may have similar roles as connecting elements in the extracellular matrix.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 20:16:23