INACTIVATION OF BCL-2 BY PHOSPHORYLATION

被引：729

作者：

HALDAR, S ^{[1
]}

JENA, N ^{[1
]}

CROCE, CM ^{[1
]}

机构：

[1] THOMAS JEFFERSON UNIV,JEFFERSON CANC CTR,PHILADELPHIA,PA 19107

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 10期

关键词：

APOPTOSIS; PROGRAMMED CELL DEATH; ONCOGENE; HUMAN CANCER; LIPID PEROXIDATION;

D O I：

10.1073/pnas.92.10.4507

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：

The antiapoptosis potential of Bcl-2 protein is well established, but the mechanism of Bcl-2 action is still poorly understood. Using the phosphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, we found that Bcl-2 was phosphorylated in lymphoid cells. Phospho amino acid analysis revealed that Bcl-2 was phosphorylated on serine. Under similar conditions, okadaic acid or taxol treatment led to the induction of apoptosis in these cells. Thus, phosphorylation of Bcl-2 seems to inhibit its ability to interfere with apoptosis. In addition, phosphorylated Bcl-2 can no longer prevent lipid peroxidation as required to protect cells from apoptosis.

引用

页码：4507 / 4511

页数：5

共 21 条

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