PROTEASES AND PROTEOLYSIS IN THE LYSOSOME

被引:207
作者
BOHLEY, P [1 ]
SEGLEN, PO [1 ]
机构
[1] NORWEGIAN RADIUM HOSP,INST CANC RES,DEPT TISSUE CULTURE,N-0310 OSLO 3,NORWAY
来源
EXPERIENTIA | 1992年 / 48卷 / 02期
关键词
LYSOSOME; PROTEIN DEGRADATION; PROTEINASE; CATHEPSIN;
D O I
10.1007/BF01923508
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Proteins sequestered by a non-selective bulk process within the lysosomes turn over with an apparent half-life of about 8 minutes and this rapid lysosomal proteolysis is initiated by endopeptidases, in particular by the cathepsins D and L. We describe also the cathepsins B and H which show mainly exopeptidase and only low endopeptidase activity. Especially cathepsin H is most probably the only lysosomal aminopeptidase in many cell types. Additionally, the properties of other mammalian lysosomal endo- and exopeptidases are compared. Finally, we discuss some of the conditions for the action of lysosomal proteases as the low intralysosomal pH, the high part of lysosomal thiol groups and the absence of intralysosomal proteinase inhibitors.
引用
收藏
页码:151 / 157
页数:7
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