Acyl phosphatase activity of NO-inhibited glyceraldehyde-3-phosphate dehydrogenase (GAPDH): A potential mechanism for uncoupling glycolysis from ATP generation in NO-producing cells

Biochemical Journal

Volumn 341, Issue 1, 1999, Pages 5-9

  Albina, Jorge E ^a,b   Mastrofrancesco, Balduino ^a   Reichner, Jonathan S ^a,b  

^a RHODE ISLAND HOSPITAL   (United States)

^b BROWN UNIVERSITY   (United States)

Author keywords

Glucose; Macrophage; Metabolism

Indexed keywords

ACYLPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DIETHYLAMINE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LINSIDOMINE; NITRIC OXIDE; S NITROSOGLUTATHIONE;

ANIMAL CELL; ARTICLE; CELL CULTURE; CONTROLLED STUDY; DOSE RESPONSE; ENERGY METABOLISM; ENZYME ACTIVITY; ENZYME INHIBITION; GLUCOSE METABOLISM; GLYCOLYSIS; MACROPHAGE; NONHUMAN; PERITONEUM MACROPHAGE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION;

ADENOSINE TRIPHOSPHATE; ANIMALS; ENERGY METABOLISM; GLUCOSE; GLUTATHIONE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; GLYCOLYSIS; MACROPHAGES, PERITONEAL; MUSCLES; NITRIC OXIDE; NITROSO COMPOUNDS; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; RABBITS; RATS; RATS, INBRED F344; S-NITROSOGLUTATHIONE; UNCOUPLING AGENTS;

ANIMALIA;

EID: 0033165935     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3410005     Document Type: Article

References (28)

1. Zhang, J. and Snyder, S. H. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 9382-9385
2. Vedia, L. M. Y., McDonald, B., Reep, B., Brüne, B., Di Silvio, M., Billiar, T. R. and Lapetina, E. G. (1992) J. Biol. Chem. 267, 24929-24932
3. Dimmeler, S., Lottspeich, F. and Brüne, B. (1992) J. Biol. Chem. 267, 16771-16774
4. Dimmeler, S., Ankarcrona, M., Nicotera, P. and Brüne, B. (1993) J. Immunol. 150, 2964-2971
5. Padgett, C. M. and Whorton, A. R. (1995) Am. J. Physiol. 269, C739-C749
6. Messmer, U.K. and Brüne, B. (1996) Eur. J. Pharmacol. 302, 171-182
7. Mohr, S., Stamler, J. S. and Brüne, B. (1996) J. Biol. Chem. 271, 4209-4214
8. Albina, J. E. and Mastrofrancesco, B. (1993) Am. J. Physiol. 264, C1594-C1599
9. Mateo, R. B., Reichner, J. S., Mastrofrancesco, B., Kraft-Stolar, D. and Albina, J. E. (1995) Am. J. Physiol. 268, C669-C675
10. Harary, I. (1957) Biochim. Biophys. Acta 26, 434-436
11. Park, J. H. and Koshland, Jr., D. E. (1958) J. Biol. Chem. 233, 986-990
12. Allison, W. S. and Connors, M. J. (1970) Arch. Biochem. Biophys. 136, 383-391
13. Becker, K., Savvides, S. N., Keese, M., Schirmer, H. and Karplus, P. A. (1998) Nat. Struct. Biol. 5, 267-271
14. Ehring, R. and Colowick, S. P. (1969) J. Biol. Chem. 17, 4589-4599
15. Micheli, V., Simmonds, H. A., Bari, M. and Pompucci, G. (1993) Clin. Chim. Acta 220, 1-17
16. Lipmann, F. and Tuttle, L. C. (1945) J. Biol. Chem. 159, 21-28
17. Albina, J. E., Mills, C. D., Henry, Jr., W. L. and Caldwell, M. D. (1989) J. Immunol. 143, 3641-3646
18. Atkinson, D. E. and Walton, G. M. (1967) J. Biol. Chem. 242, 3239-3241
19. Rafter, G. W. (1957) Arch. Biochem. Biophys. 67, 267-271
20. Parker, D. J. and Allison, W. S. (1969) J. Biol. Chem. 244, 180-189
21. Stamler, J. S. and Hausladen, A. (1998) Nat. Struct. Biol. 5, 247-249
22. Drapier, J.-C. and Hibbs, Jr., J. B. (1988) J. Immunol. 140, 2829-2838
23. Albina, J. E., Caldwell, M. D., Henry, Jr., W. L. and Mills, C. D. (1989) J. Exp. Med. 169, 1021-1029
24. Sato, T., Kamata, Y., Irifune, M. and Nishikawa, T. (1995) Brain Res. 704, 117-120
25. Swallow, C. J., Grinstein, S., Sudsbury, R. A. and Rotstein, O. D. (1991) J. Exp. Med. 174, 1009-1021
26. Clancy, R. M., Levartovsky, D., Leszczynska-Piziak, J., Yegudin, J. and Abramson, S. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 3680-3684
27. Gaston, B., Reilly, J., Drazen, J. M., Fackler, J., Ramdev, P., Arnelle, D., Mullins, M. E., Sugarbaker, D. J., Chee, C., Singel, D. J. et al. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 10957-10961
28. Stamler, J. S., Singel, D. J. and Loscalzo, J. (1992) Science 258, 1898-1902