Faris B, Salcedo L L, Cook V, Johnson L, Foster J A, Franzblau C
Biochim Biophys Acta. 1976 Jan 5;418(1):93-103. doi: 10.1016/0005-2787(76)90330-0.
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.
通过氨基酸分析以及赖氨酸衍生交联键的存在，平滑肌细胞合成弹性蛋白得到了明确证实。所得数值与从兔主动脉组织分离出的无定形弹性蛋白中的数值相符。当这些细胞在[14C]脯氨酸存在的情况下生长时，通过[14C]羟脯氨酸的出现来监测相同细胞的胶原蛋白合成。当用[14C]赖氨酸脉冲处理细胞时，可以检测到[14C]羟赖氨酸和[14C]葡萄糖基半乳糖基羟赖氨酸。弹性蛋白和胶原蛋白合成的进一步证据是在用NaBH4还原[14C]赖氨酸脉冲处理的细胞后，发现了放射性标记的ε-羟基正亮氨酸以及两个烯赖氨酸残基的还原醛醇缩合物。
