Studies on the molecular mechanism of heat shock protein 47.

热休克蛋白47（HSP 47）可与胶原结合，在许多细胞系和组织中其表达与胶原的表达相关。我们认为HSP 47对前胶原的正确分泌具有重要作用。HSP47存在于ER中，并与新合成的前胶原瞬时结合。促进多肽折叠和组装的蛋白质被称为分子伴侣。我们认为HSP47是以底物特异性的方式作为分子伴侣的。本课题的主要目的是揭示HSP 47的分子结构，并确定其在胶原蛋白中的结合位点，主要介绍了本课题组近年来的研究进展：1）日本研究人员成功制备了HSP 47的表达载体，并将其发送给英国研究人员;他们建立了HSP 47的纯化方法，现在可以得到高纯度的HSP 47。通过CD光谱开始了HSP 47的结构分析。3）一些丝氨酸蛋白酶抑制剂家族成员的晶体结构是已知的。由于HSP47属于丝氨酸蛋白酶抑制剂家族，其结构可以通过计算机分析推测。

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.