Biosynthesis of collagen.
Biosynthesis of collagen.
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胶原蛋白的生物合成。
DOI：
10.1002/jcb.240280106
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发表时间：
1985
影响因子：
4
通讯作者：
Fessler,LI
中科院分区：
文献类型：
--
作者：
Fessler,JH;Doege,KJ;Duncan,KG;Fessler,LI
在胶原蛋白结构的生物合成和组装过程中，二硫键可以发挥多种功能。在生物合成过程中，它们成功地稳定了肽内折叠以及将三条链连接成一个分子。对 I 型前胶原还原和变性羧基前肽的重折叠和重新结合的研究表明，折叠和组装的连续相互作用逐渐减弱。在正确重折叠的羧基前肽中重新建立了二硫键。在 V 型原胶原分子加工过程中，随着这些胶原蛋白融入细胞外基质，二硫键可能会发生重排。基底膜 IV 型原胶原分子的两端通过二硫键连接成网络，并且有迹象表明二硫键的进一步重排可能允许额外的调节。
During the biosynthesis and assembly of collagen structures, disulfide links can serve several functions. During biosynthesis they successively stabilize intra‐peptide folding and associations of three chains into one molecule. Studies on the refolding and reassociation of reduced and denatured carboxyl propeptides of procollagen I showed that successive interactions of folding and assembly are successively weaker. Disulfide bridges were reestablished within correctly refolded carboxyl propeptides. Rearrangements of disulfide bridges may occur during the processing of type V procollagen molecules as these collagens become incorporated into extracellular matrix. The basement membrane procollagen IV molecules become disulfide linked at each end into networks, and there are indications that further rearrangements of disulfide links may allow additional modulation.