Abstract
Nitric oxide generation in brain cytosolic fractions markedly enhances ADP-ribosylation of a single 37-kDa protein. By utilizing a biotinylated NAD and avidin affinity chromatography, we purified this protein. Partial amino acid sequencing establishes its identity as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This is further confirmed by detection of GAPDH enzymatic activity in the purified 37-kDa protein. GAPDH is ADP-ribosylated in the absence of brain extract. This auto-ADP-ribosylation is enhanced by nitric oxide generation. ADP-ribosylation appears to involve the cysteine where NAD interacts with GAPDH so that ADP-ribosylation likely inhibits enzymatic activity. Such inhibition may play a role in nitric oxide-mediated neurotoxicity.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 8:10 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 1:31 p.m.) |
Indexed | 1 month, 3 weeks ago (July 7, 2025, 1:45 a.m.) |
Issued | 32 years, 10 months ago (Oct. 15, 1992) |
Published | 32 years, 10 months ago (Oct. 15, 1992) |
Published Online | 32 years, 10 months ago (Oct. 15, 1992) |
Published Print | 32 years, 10 months ago (Oct. 15, 1992) |
@article{Zhang_1992, title={Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase.}, volume={89}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.89.20.9382}, DOI={10.1073/pnas.89.20.9382}, number={20}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Zhang, J and Snyder, S H}, year={1992}, month=oct, pages={9382–9385} }