title: Characterisation of the major collagen species present in porcine aortae and the synthesis of their precursors by smooth muscle cells in culture.
abstract: Porcine aortae were digested with pepsin and the solubilised collagen molecules separated by differential salt precipitation at pH7.5. The fraction precipitated at 1.71 M NaCl was shown to comprise collagen type III as judged by its elution characteristics from CM-cellulose, its alpha-chain composition on sodium dodeclysulphate polyacrylamide gel electrophoresis, and amino acid analyses. Pepsin-derived type I collagen was recovered by precipitation at 2.56 M NaCl and similarly characterised. cultures of porcine arterial smooth muscle cells have been established and radiolabelling studies with [14Clproline have demonstrated that these cells synthesis and secrete the precursors of collagen types I and III into the culture medium. Ion-exchange chromatography of these secreted collagen molecules and gel filtration of their pepsin-derived alpha-chains have demonstrated that type III is the major collagen species present in the medium.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis* / Q000166:cytology; D002478:Cells, Cultured; D003094:Collagen / Q000032:analysis* / Q000096:biosynthesis; D004591:Electrophoresis, Polyacrylamide Gel; D009130:Muscle, Smooth / Q000166:cytology / Q000378:metabolism; D011498:Protein Precursors / Q000096:biosynthesis; D013552:Swine
chemical_list: D000596:Amino Acids; D011498:Protein Precursors; D003094:Collagen