重组生产胶原蛋白的研究进展

近几年来对人源胶原蛋白的重组表达系统的研究有很大进展.哺乳动物细胞和昆虫细胞是最开始被应用的,但其生产成本昂贵.酵母已经可以较高水平的表达Ⅰ型、Ⅱ型和Ⅲ型胶原蛋白,共表达胶原蛋白基因和脯氨酰羟化酶亚基cDNAs的酵母已经能够产生完全羟基化和热稳定的胶原蛋白.人源Ⅰ型和Ⅲ型胶原蛋白同型三聚体可以在转基因烟草中得到表达.转基因小鼠可以表达全长的Ⅰ型原胶原同型三聚体.最近,转基因蚕用来表达包含胶原蛋白序列的融合蛋白.每一个重组系统都有可能应用于大规模的商业化生产.

Advance in the Studies of the Production of Rrecombinant Human Collagens

The tools of recombinant protein expression are now being used to provide recombinant sources of collagen. Several recombinant systems have been developed for production of human sequence collagens. Mammalian and insect cells were initiallyused, but were thought to be too costly for commercial production. Yeast have been engineered to express high levels of typeI homotrimer and heterotrimer and type II and type III collagen. Co-expression of collagen genes and cDNAs encoding the subunits of prolyl hydroxylase has lead to the synthesis of completely hydroxylated thermostable collagens.Human types I and III collagen homotrimers have been expressed in transgenic tobacco plants, while transgenic mice have been engineered to produce full-length type I procollagen homotrimer . Most recently, a transgenic silkworm system was used to produce a fusion protein containing a collagenous sequence. Each of these transgenic systems holds great promise for the cost-effective large-scale production of recombinant human collagens.