Glyceraldehyde-3-phosphate dehydrogenase regulates cyclooxygenase-2 expression by targeting mRNA stability

被引：25

作者：

Ikeda, Yuki ^{[1
]}

Yamaji, Ryoichi ^{[2
]}

Irie, Kazuhiro ^{[1
]}

Kioka, Noriyuki ^{[3
]}

Murakami, Akira ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Agr, Div Food Sci & Biotechnol, Kyoto, Japan

[2] Osaka Prefecture Univ, Grad Sch Life & Environm Sci, Div Appl Biol Chem, Osaka, Japan

[3] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto, Japan

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2012年 / 528卷 / 02期

基金：

日本学术振兴会;

关键词：

GAPDH; Cyclooxygenase-2; Post-transcriptional regulation; mRNA stability; Glutathione; Aggregation; POSTTRANSCRIPTIONAL REGULATION; FUNCTIONAL DIVERSITY; CANCER CELLS; PROTEIN; HUR; RECEPTOR; BINDING; GLUTATHIONE; MECHANISM; REGION;

D O I：

10.1016/j.abb.2012.09.004

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：

Cyclooxygenase (COX)-2 is an inducible inflammatory protein whose expression is partially regulated at the post-transcriptional level. We investigated whether glyceraldehyde-3-phosphate dehydrogenase (GAPDH) binds to the AU-rich element (ARE) of COX-2 mRNA for its degradation. Knockdown of GAPDH in hepa1c1c7 cells significantly enhanced COX-2 expressions. Recombinant GAPDH bound to the COX-2 ARE within the first 60 nucleotides of the 3'-UTR via the NAD(+) binding domain. Interestingly, a C151S GAPDH mutant retained binding activity. Confocal microscopy observation revealed that LPS exposure reduced the localization of GAPDH in nuclei. Our results indicate that GAPDH negatively regulates COX-2 by binding to its ARE. (C) 2012 Elsevier Inc. All rights reserved.

引用

页码：141 / 147

页数：7

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