The synthesis of connective tissue protein in smooth muscle cells.
The synthesis of elastin by smooth muscle cells was clearly demonstrated by amino acid analyses and the presence of lysine-derived crosslinks. The values obtained were compatible with those found in amorphous elastin isolated from rabbit aortic tissue. Collagen synthesis by these same cells was monitored by the appearance of [14C] hydroxyproline when the cells were grown in the presence of [14C] proline. When the cells were pulsed with [14C] lysine, one could detect [14C] hydroxylysine and [14C] glucosylgalactosylhydroxylysine. Further evidence for the synthesis of elastin and collagen was the finding of radiolabelled epsilon-hydroxynorleucine and the reduced aldol condensate of two residues of allysine after reduction of [14C] lysine pulsed cells with NaBH4.
D000818:Animals; D001011:Aorta / Q000378:metabolism; D003094:Collagen / Q000096:biosynthesis; D003238:Connective Tissue / Q000378:metabolism*; D004549:Elastin / Q000096:biosynthesis; D006901:Hydroxylysine / Q000378:metabolism; D006909:Hydroxyproline / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D009124:Muscle Proteins / Q000096:biosynthesis*; D009130:Muscle, Smooth / Q000378:metabolism*; D011392:Proline / Q000378:metabolism; D014176:Protein Biosynthesis; D011817:Rabbits
D009124:Muscle Proteins; D006901:Hydroxylysine; D003094:Collagen; D004549:Elastin; D011392:Proline; D008239:Lysine; D006909:Hydroxyproline