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COLLAGEN FAMILY OF PROTEINS
Author(s): VANDERREST M, GARRONE R
Source: FASEB JOURNAL    Volume: 5    Issue: 13    Pages: 2814-2823    Published: OCT 1991  
Times Cited: 601     References: 61     
Abstract: Collagen molecules are structural macro-molecules of the extracellular matrix that include in their structure one or several domains that have a characteristic triple helical conformation. They have been classified by types that define distinct sets of polypeptide chains that can form homo- and heterotrimeric assemblies. All the collagen molecules participate in supramolecular aggregates that are stabilized in part by interactions between triple helical domains. Fourteen collagen types have been defined so far. They form a wide range of structures. Most notable are 1) fibrils that are found in most connective tissues and are made by alloys of fibrillar collagens (types I, II, III, V, and XI) and 2) sheets constituting basement membranes (type IV collagen), Descemet's membrane (type VIII collagen), worm cuticle, and organic exoskeleton of sponges. Other collagens, present in smaller quantities in tissues, play the role of connecting elements between these major structures and other tissue components. The fibril-associated collagens with interrupted triple helices (FACITs) (types IX, XII, and XIV) appear to connect fibrils to other matrix elements. Type VII collagen assemble into anchoring fibrils that bind epithelial basement membranes and entrap collagen fibrils from the underlying stroma to glue the two structures together. Type VI collagen forms thin-beaded filaments that may interact with fibrils and cells.
Document Type: Review
Language: English
Reprint Address: VANDERREST, M (reprint author), UNIV LYON 1, INST BIOL & CHEM PROT, CNRS, UPR 412, BATIMENT 403, F-69622 VILLEURBANNE, FRANCE
Addresses:
1. ECOLE NORMALE SUPER LYON, LYONS, FRANCE
Publisher: FEDERATION AMER SOC EXP BIOL, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998
Subject Category: Biochemistry & Molecular Biology; Biology; Cell Biology
IDS Number: GJ471
ISSN: 0892-6638
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