ACTIVATION OF INTRACELLULAR CALCIUM-ACTIVATED NEUTRAL PROTEINASE IN ERYTHROCYTES AND ITS INHIBITION BY EXOGENOUSLY ADDED INHIBITORS

被引:33
作者
HAYASHI, M
INOMATA, M
SAITO, Y
ITO, H
KAWASHIMA, S
机构
[1] TOKYO METROPOLITAN GERIATR HOSP & INST GERONTOL, DEPT BIOCHEM, 35-2 SAKAE CHO, ITABASHI KU, TOKYO 173, JAPAN
[2] AOYAMA GAKUIN UNIV, DEPT CHEM, TOKYO 150, JAPAN
关键词
CALCIUM-ACTIVATED; PROTEINASE; AUTOLYTIC ACTIVATION; PROTEINASE INHIBITOR; ERYTHROCYTE;
D O I
10.1016/0167-4889(91)90083-A
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Intracellular calcium-activated neutral proteinase (CANP) in rabbit erythrocytes was activated by an influx of Ca2+ into the cells. The catalytic large subunit changed from the original 79 kDa form to the 77 kDa and 76 kDa forms on activation just in the same manner as occurs in the autolytic activation of purified CANP in vitro. The activation required both extracellular Ca2+ and A23187, and was accompanied by the degradation of some membrane proteins and morphological changes in erythrocyte shape from discocytes to echinodisks, echinocytes, and spherocytes. Exogenously added Cbz-Leu-Leu-Leu-aldehyde inhibited the activation of intracellular CANP as well as the degradation of membrane proteins and the morphological changes indicating that the latter two processes are due to the action of CANP. Leupeptin and E64d were without effect on intracellular CANP.
引用
收藏
页码:249 / 256
页数:8
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