Miyaishi O, Sakata K, Matsuyama M, Saga S
Second Department of Pathology, Nagoya University School of Medicine, Japan.
J Histochem Cytochem. 1992 Jul;40(7):1021-9. doi: 10.1177/40.7.1607635.
We examined the tissue distribution of heat-shock protein MW 47,000 D, hsp47, which binds to native and denatured collagen including Types I, III, and IV, in various chicken tissues by Western blotting and immunohistochemical methods. hsp47 was located on fibrocytes or fibroblasts in the connective tissue in various organs, chondrocytes in the cartilage, smooth muscle cells in the gastrointestinal tract and blood vessels, vitamin A storage cells in sinusoidal area of liver, endothelial cells in blood vessels, and epithelial cells of renal glomeruli, tubules, and basal layer of epidermis. These cells also co-expressed a certain type of collagen molecule. Furthermore, in developing embryos, fibroblasts and chondrocytes expressed hsp47 before the deposition of collagen Type I or Type II in the surrounding tissue. These results indicate that the binding of hsp47 to collagen molecules has important biological significance.
我们通过蛋白质免疫印迹法和免疫组织化学方法,检测了分子量为47,000道尔顿的热休克蛋白(hsp47)在各种鸡组织中的组织分布情况,hsp47可与包括I型、III型和IV型在内的天然及变性胶原蛋白结合。hsp47位于各器官结缔组织中的纤维细胞或成纤维细胞、软骨中的软骨细胞、胃肠道和血管中的平滑肌细胞、肝脏血窦区域的维生素A储存细胞、血管内皮细胞以及肾小球、肾小管和表皮基底层的上皮细胞中。这些细胞还共同表达某种类型的胶原蛋白分子。此外,在发育中的胚胎中,成纤维细胞和软骨细胞在周围组织中沉积I型或II型胶原蛋白之前就表达了hsp47。这些结果表明,hsp47与胶原蛋白分子的结合具有重要的生物学意义。