一种新型的 hPirh2 剪接变异体，缺乏泛素蛋白连接酶活性，与 p53 相互作用，并在肝癌中下调。

A novel hPirh2 splicing variant without ubiquitin protein ligase activity interacts with p53 and is down-regulated in hepatocellular carcinoma.

机构信息

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, China.

出版信息

FEBS Lett. 2010 Jul 2;584(13):2772-8. doi: 10.1016/j.febslet.2010.04.075. Epub 2010 May 7.

DOI:10.1016/j.febslet.2010.04.075

PMID:20452352

Abstract

A novel splice variant of hPirh2, named hPirh2b, was isolated from human fetal liver cDNA library. hPirh2b has a 38-nucleotide deletion and encodes a 188-amino acid protein with a truncated RING-H2 domain. It shows no ubiquitin protein ligase activity. A low level of expression of hPirh2 was found both at transcriptional and translational level in human hepatocellular carcinoma (HCC) when compared to non-cancerous tissue. Statistical analysis showed that the low expression is associated with lack of differentiation of HCC. In direct binding studies hPirh2b bound p53 indicating that RING-H2 domain is not needed for this interaction.

摘要

从人胎肝 cDNA 文库中分离到 hPirh2 的一种新剪接变体，命名为 hPirh2b。hPirh2b 缺失 38 个核苷酸，编码一个含 188 个氨基酸的蛋白质，其 RING-H2 结构域被截断。它没有泛素蛋白连接酶活性。与非癌组织相比，在人肝癌 (HCC) 的转录和翻译水平上均发现 hPirh2 的表达水平较低。统计分析表明，低表达与 HCC 的分化缺失有关。在直接结合研究中，hPirh2b 与 p53 结合表明 RING-H2 结构域不是这种相互作用所必需的。