Nonhelical, fibronectin-binding basement-membrane collagen from endodermal cell culture.
A novel method of affinity chromatography on insolubilized collagen-binding fragments of fibronectin was utilized to isolate a random-coil collagenous protein from culture media of mouse teratocarcinoma-derived endodermal cells. These cells also produced another collagenous protein, which did not bind to fibronectin but could be isolated by differential salt precipitation. The affinity-purified collagen differs from its conventionally isolated counterpart in that it is not triple-helical in structure, its polypeptides are not disulfide-crosslinked and it has affinity for fibronectin in its native state. Both collagens resemble previously characterized type IV basement-membrane collagens with respect to their amino acid composition, cyanogen bromide peptides, chain size, immunological reactivity and tissue localization. The random-coil collagen is directly active in promoting the attachment of some lines of cells, but for attachment of the endodermal cells addition of fibronectin is required. This suggests that the presence of nonhelical, fibronectin-binding collagen may have biological significance in the interaction of cells with the extracellular matrix.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001485:Basement Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D003094:Collagen / Q000276:immunology / Q000378:metabolism*; D004707:Endoderm; D005353:Fibronectins / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006023:Glycoproteins / Q000378:metabolism; D007797:Laminin; D051379:Mice; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D013724:Teratoma
D000596:Amino Acids; D005353:Fibronectins; D006023:Glycoproteins; D007797:Laminin; D010446:Peptide Fragments; D003094:Collagen