Inhibition of Bax channel-forming activity by Bcl-2

被引：919

作者：

Antonsson, B ^{[1
]}

Conti, F ^{[1
]}

Ciavatta, A ^{[1
]}

Montessuit, S ^{[1
]}

Lewis, S ^{[1
]}

Martinou, I ^{[1
]}

Bernasconi, L ^{[1
]}

Bernard, A ^{[1
]}

Mermod, JJ ^{[1
]}

Mazzei, G ^{[1
]}

Maundrell, K ^{[1
]}

Gambale, F ^{[1
]}

Sadoul, R ^{[1
]}

Martinou, JC ^{[1
]}

机构：

[1] IST CIBERNET & BIOFIS, I-16149 GENOA, ITALY

来源：

SCIENCE | 1997年 / 277卷 / 5324期

关键词：

D O I：

10.1126/science.277.5324.370

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 of the Bcl-2 family are intracellular membrane-associated proteins that regulate programmed cell death (apoptosis) either positively or negatively by as yet unknown mechanisms. Bax, a pro-apoptotic member of the Bcl-2 family, was shown to form channels in lipid membranes. Bax triggered the release of liposome-encapsulated carboxyfluorescein at both neutral and acidic pH. AS physiological pH, release could be blocked by Bcl-2, Bcl-2, in contrast, triggered carboxyfluorescein release at acidic pH only. In planar lipid bilayers, Bax formed pH- and voltage-dependent ion-conducting channels. Thus, the pro-apoptotic effects of Bax may be elicited through an intrinsic pore-forming activity that can be antagonized by Bcl-2.

引用

页码：370 / 372

页数：3

共 16 条

[1] THE PROTEIN BCL-2-ALPHA DOES NOT REQUIRE MEMBRANE ATTACHMENT, BUT 2 CONSERVED DOMAINS TO SUPPRESS APOPTOSIS [J].