Murawaki Y, Yamada S, Koda M, Hirayama C
Second Department of Internal Medicine, Tottori University School of Medicine.
J Biochem. 1990 Aug;108(2):241-4. doi: 10.1093/oxfordjournals.jbchem.a123187.
Collagenase and collagenolytic cathepsin activities in normal and carbon tetrachloride-induced fibrotic livers of rats were simultaneously determined at 35 and 25 degrees C for 18 h, using the same 14C-labeled neutral soluble collagen as a substrate. Collagenolytic cathepsin had higher activity under the assay conditions at both 35 and 25 degrees C than collagenase in normal and fibrotic livers. On sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis, the collagen was visibly degraded by collagenolytic cathepsin, but not by collagenase. These results indicate that, unlike collagenase, collagenolytic cathepsins exist as active forms in the rat liver, and can participate in the degradation of collagens, especially of soluble collagens including procollagens.
使用相同的14C标记的中性可溶性胶原蛋白作为底物，在35℃和25℃下同时测定正常大鼠和四氯化碳诱导的纤维化大鼠肝脏中胶原酶和胶原分解组织蛋白酶的活性，作用18小时。在35℃和25℃的测定条件下，正常肝脏和纤维化肝脏中的胶原分解组织蛋白酶活性均高于胶原酶。在十二烷基硫酸钠-聚丙烯酰胺平板凝胶电泳中，胶原分解组织蛋白酶可使胶原蛋白明显降解，而胶原酶则不能。这些结果表明，与胶原酶不同，胶原分解组织蛋白酶在大鼠肝脏中以活性形式存在，并且可以参与胶原蛋白的降解，尤其是包括前胶原在内的可溶性胶原蛋白的降解。
