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

Archives of biochemistry and biophysics (2012-09-25)
Yuki Ikeda, Ryoichi Yamaji, Kazuhiro Irie, Noriyuki Kioka, Akira Murakami
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Glyceraldehyde-3-phosphate Dehydrogenase from human erythrocytes, lyophilized powder, 50-150 units/mg protein
Sigma-Aldrich
Glyceraldehyde-3-phosphate Dehydrogenase from rabbit muscle, lyophilized powder, ≥75 units/mg protein
Supelco
GAPDH, standard for protein electrophoresis