Bembenek M E, Liberti J P
Arch Biochem Biophys. 1984 Aug 15;233(1):203-11. doi: 10.1016/0003-9861(84)90618-0.
The anabolic effects of insulin on collagen production of freshly isolated Swarm rat chondrosarcoma chondrocytes were investigated. The specific radioactivity of newly synthesized collagen was not increased by insulin, indicating that the hormone has no effect on the specific radioactivity of the aminoacyl tRNA pool. Results of further studies obtained from collagen degradation experiments demonstrated that insulin did not alter the rate of [3H]collagen degradation. Together, these results clearly indicate that insulin stimulates collagen biosynthesis. Polyacrylamide gel analysis of the newly synthesized collagen of both control and insulin-stimulated cells revealed a large-molecular-weight component which migrated with authentic alpha 1(II) collagen and was collagenase-sensitive. Additional studies showed that, although insulin increased the processing and secretion of collagen, the hormone did not cause a shift in the distribution of the extracellular and intracellular collagen pools. Finally, results of studies conducted with the transcriptional inhibitor, actinomycin D, indicated that the anabolic effects of insulin on collagen and non-collagen proteins were mediated at a post-transcriptional site.
研究了胰岛素对新鲜分离的斯旺大鼠软骨肉瘤软骨细胞胶原蛋白生成的合成代谢作用。胰岛素并未增加新合成胶原蛋白的比放射性,表明该激素对氨酰基tRNA池的比放射性没有影响。从胶原蛋白降解实验获得的进一步研究结果表明,胰岛素并未改变[3H]胶原蛋白的降解速率。这些结果共同清楚地表明,胰岛素刺激胶原蛋白的生物合成。对对照细胞和胰岛素刺激细胞新合成的胶原蛋白进行聚丙烯酰胺凝胶分析,发现一种大分子成分,其迁移方式与纯α1(II)胶原蛋白相同,且对胶原酶敏感。额外的研究表明,虽然胰岛素增加了胶原蛋白的加工和分泌,但该激素并未导致细胞外和细胞内胶原蛋白池分布的改变。最后,用转录抑制剂放线菌素D进行的研究结果表明,胰岛素对胶原蛋白和非胶原蛋白的合成代谢作用是在转录后位点介导的。