Ii K, Hizawa K, Kominami E, Bando Y, Katunuma N
J Histochem Cytochem. 1985 Nov;33(11):1173-5. doi: 10.1177/33.11.4056381.
Different localizations of cathepsin B, H, and L in normal rat liver were revealed immunohistochemically with anticathepsin Fab'-horseradish peroxidase conjugates. Staining of cathepsin B was strong in the periportal sinusoids, possibly in Kupffer cells; and weaker in panlobular hepatocytes. Staining of cathepsin H was strong in panlobular hepatocytes, especially in the periphery of the cytoplasm, possibly representing the peribiliary dense bodies; and weaker in periportal sinusoidal cells, possibly Kupffer cells. Staining of cathepsin L was strongest in centrilobular hepatocytes and weaker in periportal sinusoidal cells, possibly Kupffer cells. These findings, revealed for the first time in the present study, show that the histologic and intracellular localizations of the three cathepsins are different, suggesting that they have different roles in degradation of exogenous and endogenous proteins.
用抗组织蛋白酶Fab'-辣根过氧化物酶偶联物免疫组织化学方法揭示了组织蛋白酶B、H和L在正常大鼠肝脏中的不同定位。组织蛋白酶B在汇管区窦状隙中染色强烈，可能位于库普弗细胞中；而在全小叶肝细胞中染色较弱。组织蛋白酶H在全小叶肝细胞中染色强烈，尤其是在细胞质周边，可能代表胆小管致密体；而在汇管区窦状隙细胞中染色较弱，可能是库普弗细胞。组织蛋白酶L在中央小叶肝细胞中染色最强，在汇管区窦状隙细胞中染色较弱，可能是库普弗细胞。本研究首次揭示的这些发现表明，这三种组织蛋白酶的组织学和细胞内定位不同，提示它们在外源性和内源性蛋白质降解中具有不同作用。
