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Titolo:
Binding of the G domains of laminin alpha 1 and alpha 2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
Autore:
Talts, JF; Andac, Z; Gohring, W; Brancaccio, A; Timpl, R;
Indirizzi:
Max Planck Inst Biochem, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany Catholic Univ Sacred Heart, CNR, Ist Chim & Chim Clin, I-00168 Rome, ItalyCatholic Univ Sacred Heart Rome Italy I-00168 Clin, I-00168 Rome, Italy
Titolo Testata:
EMBO JOURNAL
fascicolo: 4, volume: 18, anno: 1999,
pagine: 863 - 870
SICI:
0261-4189(19990215)18:4<863:BOTGDO>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYSTROPHIN-ASSOCIATED GLYCOPROTEIN; CONGENITAL MUSCULAR-DYSTROPHY; COLLAGEN TYPE-IV; BASEMENT-MEMBRANES; CALCIUM-BINDING; CELL-ADHESION; A-CHAIN; AGRIN RECEPTOR; NIDOGEN; MEROSIN;
Keywords:
basement membranes; binding assays; cell-matrix interaction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Timpl, R Max Planck Inst Biochem, Klopferspitz 18A, D-82152 Martinsried, Germany Max Planck Inst Biochem Klopferspitz 18A Martinsried Germany D-82152
Citazione:
J.F. Talts et al., "Binding of the G domains of laminin alpha 1 and alpha 2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins", EMBO J, 18(4), 1999, pp. 863-870

Abstract

The C-terminal G domain of the mouse laminin alpha 2 chain consists of five lamin-type G domain (LG) modules (alpha 2LG1 to alpha 2LG5) and was obtained as several recombinant fragments, corresponding to either individual modules or the tandem arrays alpha 2LG1-3 and alpha 2LG4-5, These fragments were compared with similar modules from the laminin al chain and from the C-terminal region of perlecan (PGV) in several binding studies. Major heparin-binding sites were located on the two tandem fragments and the individual alpha 2LG1, alpha 2LG3 and alpha 2LG5 modules. The binding epitope on alpha2LG5 could be localized to a cluster of lysines by site-directed mutagenesis. In the alpha 1 chain, however, strong heparin binding was found on alpha 1LG4 and not on alpha 1LG5, Binding to sulfatides correlated to heparin binding in most but not all cases. Fragments alpha 2LG1-3 and alpha 2LG4-5 also bound to fibulin-1, fibulin-2 and nidogen-2 with K-d = 13-150 nM. Both tandem fragments, but not the individual modules, bound strongly to alpha-dystroglycan and this interaction was abolished by EDTA but not by high concentrations of heparin and NaCl. The binding of perlecan fragment PGV to alpha-dystroglycan was even stronger and was also not sensitive to heparin, This demonstrated similar binding repertoires for the LG modules of three basement membrane proteins involved in cell-matrix interactions and supramolecular assembly.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 00:44:46