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EVIDENCE FOR SEPARATE NETWORKS OF CLASSICAL AND NOVEL BASEMENT-MEMBRANE COLLAGEN - CHARACTERIZATION OF ALPHA-3(IV)-ALPORT ANTIGEN HETERODIMER
Author(s): KLEPPEL MM, FAN WW, CHEONG HI, MICHAEL AF
Source: JOURNAL OF BIOLOGICAL CHEMISTRY    Volume: 267    Issue: 6    Pages: 4137-4142    Published: FEB 25 1992  
Times Cited: 70     References: 35     
Abstract: The COOH-terminal non-collagenous domains (NC1) of type IV collagen from glomerular basement membranes (GBM), lens capsule basement membranes, and Descemet's membrane varied in the distribution of their NC1 subunits. All of these basement membranes (BMs) contained both classical (alpha-1(IV) and alpha-2(IV)) and novel collagen chains (alpha-3(IV), alpha-4(IV) and the Alport antigen). Whereas GBM had a predominance of disulfide-bonded subunits, the lens capsule and Descemet's membrane were primarily monomeric, differences that are likely related to the functional and structural diversity of collagen in various tissues. A heterodimer formed from monomeric subunits of alpha-3(IV) and the Alport antigen exists in human and bovine GBM. This dimer represents an important cross-link of the NC1 domain of novel collagen. Additionally, immunoaffinity methodology showed that the novel BM collagen hexamers segregate into populations containing only novel BM subunits without the participation of the classical subunits (alpha-1(IV) and alpha-2(IV)). These data provided evidence for the presence of two separate networks of BM collagen: one containing alpha-1(IV) and alpha-2(IV), and the other consisting of the novel collagen chains.
Document Type: Article
Language: English
Reprint Address: KLEPPEL, MM (reprint author), UNIV MINNESOTA, SCH MED, DEPT PEDIAT, BOX 491 UMHC, MINNEAPOLIS, MN 55455 USA
Addresses:
1. UNIV MINNESOTA, SCH MED, DEPT LAB MED & PATHOL, MINNEAPOLIS, MN 55455 USA
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814
Subject Category: Biochemistry & Molecular Biology
IDS Number: HE607
ISSN: 0021-9258
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