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Titolo:
COMPLETE PRIMARY STRUCTURE OF THE 6TH CHAIN OF HUMAN BASEMENT-MEMBRANE COLLAGEN, ALPHA-6(IV) - ISOLATION OF THE CDNAS FOR ALPHA-6(IV) AND COMPARISON WITH 5 OTHER TYPE-IV COLLAGEN CHAINS
Autore:
ZHOU J; DING M; ZHAO ZH; REEDERS ST;
Indirizzi:
HARVARD UNIV,BRIGHAM & WOMENS HOSP,SCH MED,DEPT NEPHROL BOSTON MA 02115
Titolo Testata:
The Journal of biological chemistry
fascicolo: 18, volume: 269, anno: 1994,
pagine: 13193 - 13199
SICI:
0021-9258(1994)269:18<13193:CPSOT6>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPORT SYNDROME; BIDIRECTIONAL PROMOTER; ALPHA-2(IV) COLLAGEN; GOODPASTURE ANTIGEN; EXTENSIVE HOMOLOGY; CELL-ADHESION; IDENTIFICATION; DOMAIN; ALPHA-1(IV); REGION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
J. Zhou et al., "COMPLETE PRIMARY STRUCTURE OF THE 6TH CHAIN OF HUMAN BASEMENT-MEMBRANE COLLAGEN, ALPHA-6(IV) - ISOLATION OF THE CDNAS FOR ALPHA-6(IV) AND COMPARISON WITH 5 OTHER TYPE-IV COLLAGEN CHAINS", The Journal of biological chemistry, 269(18), 1994, pp. 13193-13199

Abstract

Basement membranes were previously believed to contain five distinct type IV collagen subunits. We have recently isolated part of the cDNA for a novel type IV collagen, alpha 6(IV), and shown that COL4A6, the gene encoding this new chain, is deleted in Alport syndrome-associatedleiomyomatosis (Zhou, J., Mochizuki, T., Smeets, H., Antignac, C., Laurila, P., de Paepe, A., Tryg- gvason, K., and Reeders, S. T. (1993) Science 261, 1167-1169). Here, we describe the entire human (alpha 6(IV) cDNA and show that the gene encodes a classical type IV collagen with homology throughout its length to all the other five chains. There is a 21-residue signal peptide, a 1417-residue collagenous domain interrupted at 25 points, and a 228-residue carboxyl-terminal non-collagenous domain. When the complete primary structure of this new chain was compared with all the other known chains, it became clear that (alpha 6(IV) has the most resemblance to alpha 2(IV) and alpha 4(IV). The evolution of the six chains was deduced, allowing a new classification of the type IV collagen family. The alpha 6(IV) chain is a candidate genefor X-linked Alport syndrome; knowledge of the complete structure of the chain will permit us to screen systematically for mutations in patients and to generate recombinant proteins and synthetic peptides for further study of cell-matrix interactions involving the alpha 6(IV) chain.

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Documento generato il 01/12/20 alle ore 19:35:01