TEMPERATURE-DEPENDENCE OF PROTEIN-DEGRADATION, AUTOPHAGIC SEQUESTRATION AND MITOCHONDRIAL SUGAR UPTAKE IN RAT HEPATOCYTES
TEMPERATURE-DEPENDENCE OF PROTEIN-DEGRADATION, AUTOPHAGIC SEQUESTRATION AND MITOCHONDRIAL SUGAR UPTAKE IN RAT HEPATOCYTES
复制标题
大鼠肝细胞中蛋白质降解、自噬封存和线粒体糖摄取的温度依赖性
DOI:
10.1016/0167-4889(87)90167-4
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发表时间:
1987-07-06
期刊:
影响因子:
--
通讯作者:
SEGLEN, PO
中科院分区:
文献类型:
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作者:
GORDON, PB;KOVACS, AL;SEGLEN, PO
Lysosomal (propylamine-sensitive) protein degradation as well as the energy-dependent (chymostatin-sensitive) part of the non-lysosomal protein degradation was found to be strongly affected by temperature in isolated rat hepatocytes, the activation energy (Ea) being about 25 kcal/mol for both processes. In contrast, the energy-independent (chymostatin-resistant) part of the non-lysosomal degradation had an Ea of approx. 10 kcal/mol only. Sequestration of electroinjected [14C]sucrose into sedimentable organelles showed a pronounced temperature dependence. By means of digitonin extraction it was possible to distinguish between a moderately temperature-sensitive mitochondrial sugar uptake (Ea approx. 12 kcal/mol) and a strongly temperature-dependent autophagic sequestration (Ea approx. 22 kcal/mol). There was no significant autophagic sequestration below 20.degree. C. The sequestration process is more temperature-sensitive than, for example, the early steps of endocytosis, and is likely to represent the major controlling step in the overall autophagic-lysosomal pathway.