Sodium butyrate modifies the stabilizing complexes of tyrosine hydroxylase mRNA

被引：20

作者：

Aranyi, T. ^{[1
]}

Sarkis, C. ^{[1
]}

Berrard, S. ^{[1
]}

Sardin, K. ^{[1
]}

Siron, V. ^{[1
]}

Khalfallah, O. ^{[1
]}

Mallet, J. ^{[1
]}

机构：

[1] Univ Paris 06, CNRS, UMR 7091, Hop La Pitie Salpetriere, F-75013 Paris, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 359卷 / 01期

关键词：

tyrosine hydroxylase; PC12; RNA stability; HDAC; sodium butyrate; TSA; histone acetylation; run-on assay; UV crosslinking;

D O I：

10.1016/j.bbrc.2007.05.025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Multiple mechanisms regulate the expression of the tyrosine hydroxylase (Th) gene, which encodes the rate-limiting enzyme in the biosynthesis of catecholamines. Sodium butyrate (SOB), a physiological histone deacetylase (HDAC) inhibitor, was reported to stimulate the Th gene promoter activity in reporter gene assays. However, the expression of the endogenous Th gene in PC12 cells was reported to be either stimulated or inhibited by SOB. Here, we report that SOB and other HDAC inhibitors drastically (up to 90%) and reversibly decrease the level of TH rnRNA in PC12 cells. We also show that SOB does not influence the transcription initiation rate of the Th gene but perturbs the formation of protein-RNA complexes at the 3'UTR of the gene. Our results,suggest that SOB inhibits the expression of the Th gene by destabilizing TH mRNAs. (C) 2007 Elsevier Inc. All rights reserved.

引用

页码：15 / 19

页数：5

共 23 条

[1]

Multiple complexes involved in tyrosine hydroxylase mRNA stability in rat adrenal medulla, after reserpine stimulation [J].