凋亡特异性蛋白（45 kDa的ASP）不同于人类Apg5，后者是酵母自噬基因apg5的同源物。

Apoptosis-specific protein (ASP 45 kDa) is distinct from human Apg5, the homologue of the yeast autophagic gene apg5.

作者信息

Yung Hong Wa, Xue Luzheng, Tolkovsky Aviva M

机构信息

Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK.

出版信息

FEBS Lett. 2002 Nov 6;531(2):168-72. doi: 10.1016/s0014-5793(02)03497-x.

DOI:10.1016/s0014-5793(02)03497-x

PMID:12417306

Abstract

We have examined whether the apoptosis-specific protein p45ASP and human Apg5 are identical proteins. Like p45ASP, myc-hApg5 cross-reacted with a c-Jun antibody and approximately 50% of myc-hApg5 was bound to a Triton X-100-insoluble fraction in HeLa cells. However, soluble myc-hApg5 was degraded during apoptosis induced by staurosporine or TNFalpha/cycloheximide whilst expression of soluble p45ASP was stabilised. Furthermore, myc-hApg5 degradation was blocked by the caspase inhibitor Boc-Asp(OMe)FMK whilst p45ASP expression was eliminated. Moreover, myc-hApg5 ( approximately 32 kDa) never assumed the size of p45ASP (45 kDa). It is therefore likely that p45ASP and human Apg5 are distinct proteins although they do share some common characteristics.

摘要

我们已经研究了凋亡特异性蛋白p45ASP与人类Apg5是否为同一蛋白。与p45ASP一样，myc-hApg5能与c-Jun抗体发生交叉反应，并且在HeLa细胞中约50%的myc-hApg5与Triton X-100不溶性组分结合。然而，可溶性myc-hApg5在星形孢菌素或TNFα/环己酰亚胺诱导的凋亡过程中被降解，而可溶性p45ASP的表达则保持稳定。此外，半胱天冬酶抑制剂Boc-Asp(OMe)FMK可阻断myc-hApg5的降解，而p45ASP的表达则被消除。而且，myc-hApg5（约32 kDa）的大小从未与p45ASP（45 kDa）一致。因此，尽管p45ASP和人类Apg5确实有一些共同特征，但它们很可能是不同的蛋白。