Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 528, Issue 2, Pages 141-147Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.09.004
Keywords
GAPDH; Cyclooxygenase-2; Post-transcriptional regulation; mRNA stability; Glutathione; Aggregation
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Funding
- Japan Society for the Promotion of Science [23580164]
- Grants-in-Aid for Scientific Research [23580164] Funding Source: KAKEN
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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.
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