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分离的大鼠肝细胞内胰岛素降解的溶酶体和非溶酶体途径

Lysosomal and non-lysosomal pathways of intracellular insulin degradation in isolated rat hepatocytes.

作者信息

Draznin B, Todd W W, Leitner J W, Toothaker D R

出版信息

Horm Res. 1981;15(4):252-62. doi: 10.1159/000179464.

DOI:10.1159/000179464
PMID:6765590
Abstract

The amount of 125I-insulin associated with freshly isolated hepatocytes was increased 50% in the presence of 0.2 mM chloroquine (CQ) after 2 h of incubation. The degradation of insulin by the hepatocytes incubated with CQ was significantly diminished as compared with control cells. Hepatocytes incubated with 125I-insulin in the presence of CQ showed a slower rate of ligand dissociation than control cells. More TCA-precipitable and less TCA-soluble material appeared in the dissociation buffer of CQ-treated cells. However, CQ inhibited only 25-35% of intracellular insulin degradation. Non-lysosomal intracellular insulin degradation appears to be responsible for the remaining portion of the ligand degradation by isolated hepatocytes.

摘要

在孵育2小时后,在0.2 mM氯喹(CQ)存在的情况下,与新鲜分离的肝细胞结合的125I胰岛素量增加了50%。与对照细胞相比,用CQ孵育的肝细胞对胰岛素的降解显著减少。在CQ存在下用125I胰岛素孵育的肝细胞显示出比对照细胞更慢的配体解离速率。在CQ处理细胞的解离缓冲液中出现更多的三氯乙酸沉淀物质和更少的三氯乙酸可溶物质。然而,CQ仅抑制25 - 35%的细胞内胰岛素降解。非溶酶体细胞内胰岛素降解似乎负责分离的肝细胞对配体降解的其余部分。

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