Proteasomal insensitivity of apoptin in tumor cells

被引：10

作者：

Lanz, Henriette L. ^{[1
]}

Suijker, Johnny ^{[1
]}

Noteborn, Mathieu H. M. ^{[1
]}

Backendorf, Claude ^{[1
]}

机构：

[1] Leiden Univ, Leiden Inst Chem, Dept Mol Genet, NL-2333 CC Leiden, Netherlands

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2012年 / 422卷 / 01期

关键词：

Protein degradation; Proteasome; Apoptin; Bortezomib; Ada-Ahx(3)L(3)VS; Tumor-selective apoptosis; CHICKEN ANEMIA VIRUS; PROTEIN APOPTIN; APOPTOSIS; INHIBITOR; SUBSTRATE; COMPLEX; CYCLE; P53;

D O I：

10.1016/j.bbrc.2012.04.132

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：

The small viral protein apoptin is capable of inducing apoptosis selectively in human tumor cells. In normal cells apoptin localizes in the cytoplasm where it forms aggregates, becomes epitope-shielded and eventually degraded. By inhibiting the proteasome activity with the chemical inhibitors bortezomib and Ada-Ahx(3)L(3)VS apoptin levels can be stabilized in normal cells similar to the tumor suppressor p53 protein. In contrast, proteasome inhibition in tumor cells did not affect the apoptin stability while it still stabilized p53 levels. Apparently, apoptin is degraded by proteasomal activity in normal human cells, a process that no longer takes place in tumor cells. This loss of proteasomal susceptibility appears to be specific for apoptin. (C) 2012 Elsevier Inc. All rights reserved.

引用

页码：169 / 173

页数：5

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