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Titolo:
THE C-TERMINAL DOMAIN-V OF PERLECAN PROMOTES BETA-1 INTEGRIN-MEDIATEDCELL-ADHESION, BINDS HEPARIN, NIDOGEN AND FIBULIN-2 AND CAN BE MODIFIED BY GLYCOSAMINOGLYCANS
Autore:
BROWN JC; SASAKI T; GOHRING W; YAMADA Y; TIMPL R;
Indirizzi:
MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY NIDR,NIH BETHESDA MD 20892
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 250, anno: 1997,
pagine: 39 - 46
SICI:
0014-2956(1997)250:1<39:TCDOPP>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
DENSITY-LIPOPROTEIN-RECEPTOR; EPIDERMAL-GROWTH-FACTOR; COLLAGEN TYPE-IV; EXTRACELLULAR-MATRIX PROTEIN; SULFATE PROTEOGLYCAN; BASEMENT-MEMBRANE; CORE PROTEIN; GLOBULAR DOMAIN; CALCIUM-BINDING; LAMININ;
Keywords:
BASEMENT MEMBRANES; CELL-MATRIX INTERACTION; PROTEIN BINDING; PROTEOGLYCAN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
J.C. Brown et al., "THE C-TERMINAL DOMAIN-V OF PERLECAN PROMOTES BETA-1 INTEGRIN-MEDIATEDCELL-ADHESION, BINDS HEPARIN, NIDOGEN AND FIBULIN-2 AND CAN BE MODIFIED BY GLYCOSAMINOGLYCANS", European journal of biochemistry, 250(1), 1997, pp. 39-46

Abstract

Domain V of the major basement-membrane proteoglycan perlecan, a domain which consists of three laminin type G (LG) and four epidermal-growth-factor-like (EG) modules, was obtained in recombinant form by transfecting embryonic kidney cells with an episomal expression vector. A major 90-kDa fragment V was obtained together with fragments Va (74 kDa) and Vb (26 kDa) which were generated by endogenous proteolysis in front of the most C-terminal LG module. All three fragments bound to a heparin affinity column and could be displaced at a moderate (0.2 M) NaCl concentration. Rotary-shadowing electron microscopy demonstrated a three-globule structure for fragment V. Fragment V also showed a strong immunological cross-reaction with tissue-derived perlecan, indicating that it was folded into a native structure. A further, larger fragment, Vc, was apparently substituted with heparan sulphate and/or chondroitin sulphate chains and failed to bind to heparin. Fragment V but not fragment Vc promoted a distinct adhesion of several cell lines and this could be blocked by antibodies against the integrin beta 1 chain. This domain may, however, represent only one of several cell-adhesive sites of perlecan. The recombinant perlecan fragment V bound in surface plasmon resonance assays to fibulin-2, laminin-nidogen complex, nidogen and two nidogen fragments. This indicated two different nidogen-binding epitopes on perlecan domain V with about a 10-fold difference intheir affinities (K-d = 0.05-0.2 mu M and about 2 mu M) Perlecan domain V therefore seems to participate in the supramolecular assembly andcell connections of basement membranes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 02:51:21