Fessler L I, Kumamoto C A, Meis M E, Fessler J H
J Biol Chem. 1981 Sep 25;256(18):9640-5.
The biosynthesis and processing of type V procollagens was investigated in chick embryo blood vessels labeled with radioactive amino acids. Monomeric, pepsin-sensitive pro alpha 1 V and pro alpha 2 V chains are slowly assembled into triple helically folded molecules. A small proportion of these procollagen V molecules contain interchain disulfide bridges, and the disulfide-linked heterodimer and heterotrimer (pro alpha 1 V)2pro alpha 2 V were found. A relatively fast conversion of procollagen V to p-collagen V is followed by slow change to collagen V. This time course is similar to the processing of procollagen III and is much slower than the rate of appearance of type I collagen in blood vessels. A combination of sedimentation and electrophoretic analyses was used to measure the relative size of the type V chains and to demonstrate attachment of noncollagenous peptides (Mr = 33,000) to p alpha 2 V by disulfide linkage. Similar quantitative pulse-chase studies were made with calvaria and crop. As the same unusual features of assembly and processing of type V chains were seen in muscle, bone, and blood vessels, we conclude that these are characteristic of type V collagen biosynthesis.
利用放射性氨基酸标记鸡胚血管，对Ⅴ型前胶原的生物合成及加工过程进行了研究。单体的、对胃蛋白酶敏感的前α1（Ⅴ）链和前α2（Ⅴ）链缓慢组装成三螺旋折叠分子。这些前胶原Ⅴ分子中有一小部分含有链间二硫键，并且发现了二硫键连接的异二聚体和异三聚体（前α1（Ⅴ））2前α2（Ⅴ）。前胶原Ⅴ向ｐ-胶原Ⅴ的转化相对较快，随后向胶原Ⅴ的转变则较慢。这个时间进程与前胶原Ⅲ的加工过程相似，且比血管中Ⅰ型胶原的出现速度慢得多。采用沉降和电泳分析相结合的方法来测定Ⅴ型链的相对大小，并证明非胶原肽（分子量 = 33,000）通过二硫键与ｐα2（Ⅴ）相连。对颅骨和嗉囊进行了类似的定量脉冲追踪研究。由于在肌肉、骨骼和血管中都观察到了Ⅴ型链组装和加工的相同异常特征，我们得出结论，这些是Ⅴ型胶原生物合成的特征。
