Immunocytochemical localization of cathepsins B, H, and their endogenous inhibitor, cystatin beta, in islet endocrine cells of rat pancreas.
Immunocytochemical localization of cathepsins B, H, and their endogenous inhibitor, cystatin beta, in islet endocrine cells of rat pancreas.
复制标题
组织蛋白酶 B、H 及其内源性抑制剂半胱氨酸蛋白酶抑制剂 β 在大鼠胰腺胰岛内分泌细胞中的免疫细胞化学定位。
DOI：
--
复制
发表时间：
1988
影响因子：
3.2
通讯作者：
Y. Uchiyama
中科院分区：
文献类型：
--
作者：
M. Watanabe;Tsuyoshi Watanabe;Y. Ishii;H. Matsuba;S. Kimura;T. Fujita;E. Kominami;N. Katunuma;Y. Uchiyama
为了确定大鼠胰岛内分泌细胞中溶酶体的特征，我们使用免疫细胞化学技术研究了组织蛋白酶B、H和L及其特异性抑制剂半胱氨酸蛋白酶抑制剂α和β的精确定位。通过使用连续半薄切片，我们检测组织蛋白酶B在胰岛素，胰高血糖素，生长抑素和胰腺多肽阳性（PP）细胞的免疫反应。组织蛋白酶H在A细胞中呈强阳性反应，在PP细胞中呈弱阳性反应，而在其他细胞中无阳性反应。在B细胞中证实了胱抑素β的免疫沉积物。在免疫细胞化学反应之前，将薄切片在1%甲醇钠中短暂浸渍，增强了免疫金颗粒在靶细胞器上的特异性沉积。双重免疫染色技术的使用表明，在许多分泌颗粒中胰岛素与胱抑素β共定位。这表明胱抑素β可能调节参与胰岛素成熟过程的转化酶。通过使用免疫金技术，在溶酶体中的组织蛋白酶B和H的异质性定位也被发现在胰岛细胞在光镜水平。这可能是由于细胞之间溶酶体中降解的肽的差异。
To determine the characteristics of lysosomes in rat islet endocrine cells, we examined the precise localization of cathepsins B, H, and L and their specific inhibitors, cystatins alpha and beta, using immunocytochemical techniques. By use of serial semi-thin sections, we detected immunoreactivity for cathepsin B in insulin-, glucagon-, somatostatin-, and pancreatic polypeptide-positive (PP) cells. Strong immunoreactivity for cathepsin H was seen in A-cells and weak immunoreactivity in PP cells, but none in others. Immunodeposits for cystatin beta were demonstrated in B-cells. Brief dipping of thin sections in 1% sodium methoxide before the following immunocytochemical reaction enhanced specific deposits of immunogold particles on the target organelles. Use of a double-immunostaining technique showed co-localization of insulin with cystatin beta in many secretory granules. This suggests that cystatin beta may regulate converting enzymes participating in the maturation process of insulin. By use of an immunogold technique, heterogeneous localization of cathepsins B and H in lysosomes was also found among islet cells at the light microscopic level. This may be due to the difference in peptides degraded in lysosomes among the cells.