Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin
Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin
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DOI：
10.1128/jvi.72.8.6574-6580.1998
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发表时间：
1998-08-01
影响因子：
5.4
通讯作者：
Koga, Y
中科院分区：
文献类型：
--
作者：
Ishikawa, H;Sasaki, M;Koga, Y
用单细胞杀伤法研究了钙调素（CaM）在人类免疫缺陷病毒1型gp 160诱导细胞凋亡中的作用。发现这些细胞在诱导型启动子的控制下表达缺乏各种长度羧基末端的野生型gp 160或突变型gp 160。伴随免疫印迹的免疫沉淀显示结合的钙调素的野生型gp 160，但不承担一个羧基端的缺失跨越超过5个氨基酸残基的突变体gp 160。一个显着的辅酶活性检测结合到gp 160的钙调素，即使在存在的钙离子螯合剂，EGTA。形成这种复合物的细胞表现出细胞内Ca ~（2+）水平升高，随后DNA断裂，这是凋亡的标志，最终细胞死亡，而不形成这种复合物的细胞没有表现出任何显著的Ca ~（2+）水平升高或DNA断裂。这些结果表明，CaM在gp 160诱导的凋亡中起关键作用。
The role of calmodulin (CaM) in apoptosis induced by gp160 of human immunodeficiency virus type 1 was investigated with cells undergoing single-cell killing. These cells were found to express, under the control of an inducible promoter, wild-type gp160 or mutant gp160 devoid of various lengths of the carboxyl terminus. Immunoprecipitation accompanied by immunoblotting revealed binding of CaM to wild-type gp160 but not to mutant gp160 bearing a carboxyl terminus with a deletion spanning more than five amino acid residues, A significant coenzyme activity was detected in the CaM bound to gp160 even in the presence of a Ca2+ chelater, EGTA. The cells forming this gp160-CaM complex exhibited an elevated intracellular Ca2+ level followed by DNA fragmentation, which is a hallmark of apoptosis, and finally cell killing, while the cells not forming this complex did not show any significant elevation in Ca2+ level or DNA fragmentation, These results thus indicated that CaM plays a key role in gp160-induced apoptosis.