コラーゲン生合成に関与する分子シャペロンHSP47

概要

論文の詳細を見る
HSP47 is an endoplasmic reticulum(ER)-resident glycoprotein with an ER-retention signal, Arg-Asp-Glu-Leu, at its C-terminus. This protein belongs to serine protease inhibitor(serpin)family, although the protease-inhibitory activity has not yet been detected. The expression of HSP47 under stress conditions is regulated by the heat shock transcription factor(HSF)system, and that under non-stress condition is well correlated with collagen expression in various cell lines and tissues. In the collagen producing cells, HSP47 tentatively interacts with procollagen during its translation, folding and / or modification steps, and releases procollagen at cis-Golgi. HSP47 shows the affinity to all types of collagen tested as well as simple collagen model peptides(Pro-Pro-Gly)n(n≥7)in vitro. Recent studies have suggested that chaperone proteins including HSP47 would facilitate or control the collagen biosynthesis in the ER.
日本結合組織学会の論文
1998-12-25