Apaf-1是一种与秀丽隐杆线虫CED-4同源的人类蛋白质，参与细胞色素c依赖性的半胱天冬酶-3激活过程。

Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3.

作者信息

Zou H, Henzel W J, Liu X, Lutschg A, Wang X

机构信息

Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 75235, USA.

出版信息

Cell. 1997 Aug 8;90(3):405-13. doi: 10.1016/s0092-8674(00)80501-2.

DOI:10.1016/s0092-8674(00)80501-2

PMID:9267021

Abstract

We report here the purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3. The NH2-terminal 85 amino acids of Apaf-1 show 21% identity and 53% similarity to the NH2-terminal prodomain of the Caenorhabditis elegans caspase, CED-3. This is followed by 320 amino acids that show 22% identity and 48% similarity to CED-4, a protein that is believed to initiate apoptosis in C. elegans. The COOH-terminal region of Apaf-1 comprises multiple WD repeats, which are proposed to mediate protein-protein interactions. Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis.

摘要

我们在此报告Apaf-1的纯化及cDNA克隆，Apaf-1是一种来自HeLa细胞胞质溶胶的新型130kd蛋白质，它参与细胞色素c依赖性的半胱天冬酶-3激活过程。Apaf-1的氨基末端85个氨基酸与秀丽隐杆线虫半胱天冬酶CED-3的氨基末端前结构域有21%的同一性和53%的相似性。接下来的320个氨基酸与CED-4有22%的同一性和48%的相似性，CED-4是一种据信在秀丽隐杆线虫中启动细胞凋亡的蛋白质。Apaf-1的羧基末端区域包含多个WD重复序列，这些序列被认为介导蛋白质-蛋白质相互作用。细胞色素c与Apaf-1结合，这一事件可能触发半胱天冬酶-3的激活，从而导致细胞凋亡。