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Titolo:
MICROFIBRIL-ASSOCIATED GLYCOPROTEIN-1 (MAGP-1) BINDS TO THE PEPSIN-RESISTANT DOMAIN OF THE ALPHA-3(VI) CHAIN OF TYPE-VI COLLAGEN
Autore:
FINNIS ML; GIBSON MA;
Indirizzi:
UNIV ADELAIDE,DEPT PATHOL ADELAIDE SA 5006 AUSTRALIA UNIV ADELAIDE,DEPT PATHOL ADELAIDE SA 5006 AUSTRALIA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 36, volume: 272, anno: 1997,
pagine: 22817 - 22823
SICI:
0021-9258(1997)272:36<22817:MG(BTT>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIN-ASSOCIATED MICROFIBRILS; GROWTH-FACTOR-BETA; EXTRACELLULAR-MATRIX; VONWILLEBRAND-FACTOR; SULFATE PROTEOGLYCANS; MOLECULAR-CLONING; SEQUENCE-ANALYSIS; CL GLYCOPROTEIN; TERMINAL DOMAIN; FIBRILLIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
M.L. Finnis e M.A. Gibson, "MICROFIBRIL-ASSOCIATED GLYCOPROTEIN-1 (MAGP-1) BINDS TO THE PEPSIN-RESISTANT DOMAIN OF THE ALPHA-3(VI) CHAIN OF TYPE-VI COLLAGEN", The Journal of biological chemistry, 272(36), 1997, pp. 22817-22823

Abstract

The interactions of type VI collagen have been investigated, using solid phase binding assays, with two components of the fibrillin-containing microfibrils, the elastin-binding protein, MAGP-1 and its structural relative MAGP-2. Both native and pepsin-treated forms of type VI collagen specifically bound to MAGP-1 but not to MAGP-2, Pepsin type VI collagen was shown to block the binding of MAGP-1 to native type VI collagen indicating that the major MAGP-1-binding site was in the triple-helical region of the molecule. MAGP-1 was found not to bind to collagens I, III, and V. Affinity blotting of pepsin-treated type VI collagen showed that MAGP-1 binding was specific for the collagenous domain of the alpha 3(VI) chain. Decorin and biglycan were found not to inhibit the interaction of pepsin-treated type VI collagen with MAGP-1, indicating that its binding site on the collagen is not close to that forthe proteoglycans. Reduction and alkylation of disulfide bonds in MAGP-1 did not destroy its type VI collagen-binding properties, indicating. that the binding site was likely to be in the cysteine-free, N-terminal domain of MAGP-1. Interestingly, the interaction of MAGP-1 with type VI collagen was inhibit ed by tropoelastin, suggesting that the binding sites for tropoelastin and type VI collagen may be in the same domain of MAGP-1. A peptide, corresponding to amino acids 29-38 of MAGP-1, was found to inhibit the interactions of MAGP-1 with type VI collagen and tropoelastin. The results suggest that the peptide may containthe binding sequences for both type VI collagen and tropoelastin, andthus that these two proteins may share the same binding site on MAGP-1. The interactions of MAGP-1 with type VI collagen and tropoelastin were both determined to be of moderately high affinity, with K-d valuesof 5.6 x 10(-7) M and 2.6 x 10(-7) M, respectively. The findings indicate that MAGP-1 may mediate a molecular interaction between type M collagen microfibrils and fibrillin-containing microfibrils, structures which are often found in close proximity to each other in a wide rangeof extracellular matrices.

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Documento generato il 05/07/20 alle ore 10:27:28