title: Proteins secreted by vascular smooth muscle cells as substrates of lysyl oxidase.
abstract: The mixture of proteins secreted by neonatal rat aorta smooth muscle cells cultured in the presence of beta-aminopropionitrile was readily oxidized and polymerized upon incubation with purified or crude preparations of lysyl oxidase. Western blot analysis indicated that these substrates included 30-60kDa protein bands reactive with anti-elastin, presumed to be fragments derived from tropoelastin. Thus, truncated, elastin-like as well as other proteins accumulate in the media of these cultures which, in toto, can serve as a conveniently prepared, highly efficient substrate for the routine assay of lysyl oxidase activity.
authors.affiliation: Department of Biochemistry, Boston University School of Medicine, MA 02118, USA.
authors.forename: K
authors.initials: K
authors.lastname: Nellaiappan
authors.forename: H M
authors.initials: HM
authors.lastname: Kagan
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D001011:Aorta; D015153:Blotting, Western; D002478:Cells, Cultured; D004549:Elastin / Q000378:metabolism*; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism*; D009131:Muscle, Smooth, Vascular / Q000166:cytology / Q000378:metabolism*; D010084:Oxidation-Reduction; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism*; D051381:Rats
chemical_list: D009124:Muscle Proteins; D004549:Elastin; D008249:Protein-Lysine 6-Oxidase