Studies on the molecular mechanism of heat shock protein 47.

热休克蛋白47 （Heat shock protein 47, HSP47）可以与胶原蛋白结合，在许多细胞系和组织中其表达与胶原蛋白表达相关。我们认为HSP47对前胶原蛋白的正常分泌有重要作用。HSP47存在于内质网中，并与新合成的前胶原短暂结合。促进多肽折叠和组装的蛋白质被称为分子伴侣蛋白。我们认为HSP47以一种底物特异性的方式作为分子伴侣。有趣的是，HSP47与胶原蛋白的结合受到生理ph变化的调节。在这个项目中，我们的目的是揭示HSP47的分子结构，并确定胶原蛋白中的结合位点。列出了今年的合作进展。1)日本的研究人员制作了HSP47的表达载体，寄给英国的研究人员，建立了HSP47的纯化方案，现在可以得到高纯度的HSP47。2)英国的研究人员开始了HSP47的CD谱结构分析。3)一些蛇形蛋白家族成员的晶体结构是已知的。由于HSP47属于serpin家族，可以通过计算机分析推测其结构。

Heat shock protein 47 (HSP47) can bind to collagen and its expression is correlated with that of collagen in many cell lines and tissues. We think that HSP47 has a significant role for procollagen to be secreted correctly. HSP47 exist in the ER and associates transciently with a newly synthesized procollagen. Proteins that facilitate the folding and assembly of polypeptides are called as molecular chaperone. We think HSP47 acts as a molecular chaperone by a substrate-specific manner. Interestingly, the binding of HSP47 with collagen is regulated by a physiological change of pH. In this project, our aims are to reveal the molecular structure of HSP47 and to identify the binding site in collagen.The progresses of collaboration in this year are listed.1) The researchers in Japan made the expression vector of HSP47 and sent it to researchers in U.K. They established the purification protocols of HSP47 and now they can get a highly purified HSP47.2) The researchers in U.K. started the structural analysis of HSP47 by CD spectrum.3) The crystal structures of some serpin family members are known. Because HSP47 belongs to the serpin family, its structure can be speculated by computer analysis.