S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase decreases the enzyme affinity to the erythrocyte membrane

Nitric Oxide - Biology and Chemistry

Volumn 2, Issue 1, 1998, Pages 17-27

  Galli, Francesco ^a   Rovidati, Simona ^a   Ghibelli, Lina ^b   Canestrari, Franco ^a  

^a UNIVERSITY OF URBINO   (Italy)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MODIFICATION; ERYTHROCYTE MEMBRANE; HUMAN; HUMAN CELL; MEMBRANE BINDING; PRIORITY JOURNAL;

EID: 0032004726     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1006/niox.1997.0148     Document Type: Article

References (36)

1. Shmidt H. H. H. W., Walter U. NO at work. Cell. 78:1994;919-925.
2. Nathan C., Xie Q. Nitric oxide synthases: Roles, tolls, and controls. Cell. 78:1994;915-918.
3. Hibbs J. B., Vavrin Z., Taintor R. R. L-Arginine is required for expression of the activated macrophage effector mechanism causing selective metabolic inhibition in target cells. J. Immunol. 138:1987;550-565.
4. Corbett J. A., Sweetland M. A., Lancaster J. R., McDaniel M. L. A 1-hour pulse with IL-1b induces formation of nitric oxide and inhibits insulin secretion by rat islets of Langerhans: Evidence for a tyrosine kinase signaling mechanism. FASEB J. 7:1993;369-374.
5. Stamler J. S. Redox signaling: Nitrosylation and related target interactions of nitric oxide. Cell. 78:1994;931-936.
6. Mateo R. B., Reichner J. S., Mastrofrancesco B., Kraft-Stolar D., Albina J. E. Impact of nitric oxide on macrophage glucose metabolism and glyceraldehyde-3-phosphate dehydrogenase activity. Am. J. Physiol. 268:1995;C669-675.
7. Bereta J., Bereta M. Stimulation of glyceraldehyde-3-phosphate dehydrogenase mRNA levels by endogenous nitric oxide in cytokine-activated endothelium. Biochem. Biophys. Res. Commun. 217:1995;363-369.
8. Molina y Vedia L., McDonald B., Reep B., Brune B., Di Silvio M., Billiar T. R., Lapetina E. G. Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J. Biol. Chem. 267:1992;24929-24932.
9. McDonald L. J., Moss J. Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA. 90:1993;6238-6241.
10. Mohr S., Stamler J. S., Brune B. Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by nitric oxide, peroxynitrite and related nitrosating agents. FEBS Lett. 348:1994;223-227.
11. Mohr S., Stamler J. S., Brune B. Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment. J. Biol. Chem. 271:1996;4209-4214.
12. Kant J. A., Steck T. L. Specificity in the association of glyceraldehyde-3-phosphate dehydrogenase with isolated human erythrocyte membranes. J. Biol. Chem. 248:1973;8457-8464.
13. Rogalski A. A., Steck T. L., Waseem A. Association of glyceraldehyde-3-phosphate dehydrogenase with the plasma membrane of the intact human red blood cell. J. Biol. Chem. 264:1989;6438-6446.
14. Yu J., Steck T. L. Association of band 3, the predominant polypeptide of the human erythrocyte membrane. J. Biol. Chem. 250:1975;9176-9184.
15. Tsai I-H., Murthy S. N. P., Steck T. L. Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 257:1982;1438-1442.
16. Stocchi V., Magnani M., Canestrari F., Dach M., Fornaini G. Rabbit red blood cell hexokinase. J. Biol. Chem. 256:1981;7856-7862.
17. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
18. Meyer D. J., Kramer H., Vzer N., Coles B., Ketterer B. Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin. FEBS Lett. 345:1994;177-180.
19. De Vijlder J. J. M., Slater E. C. The reaction between NAD+ and rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta. 167:1968;23-34.
20. Stocchi V., Cucchiarini L., Canestrari F., Piacentini M. P., Fornaini G. A very fast ion-pair reversed-phase HPLC method for the separation of the most significant nucleotides and their degradation products in human red blood cells. Anal. Biochem. 167:1987;181-190.
21. Canestrari F., Galli F., Giorgini A., Galiotta P., Pascucci M., Albertini M. C., Bossy M. Erythrocyte redox state in uremic anemia: Effects on hemodialysis and relevance of glutathione metabolism. Acta Haematol. 91:1994;187-193.
22. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
23. Kots A. Y., Skurat A. V., Sergienko E. A., Bulargina T. V., Severin E. S. Nitroprusside stimulates the cysteine-specific mono (ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. FEBS Lett. 300:1992;9-12.
24. Durrieu C., Bernier-Valentin F., Rousset B. Microtubules bind glyceraldehyde-3-phosphate dehydrogenase and modulates its enzyme activity and quaternary structure. Arch. Biochem. Biophys. 252:1987;32-40.
25. Arnold H., Pette D. Binding of glycolytic enzymes to structure proteins of the muscle. Eur. J. Biochem. 6:1968;163-171.
26. Nagy E., Rigby W. F. Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold). J. Biol. Chem. 270:1995;2755-2763.
27. Baxi M. D., Vishwanatha J. K. Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4a binding protein. Biochemistry. 34:1995;9700-9707.
28. Kliman H. J., Steck T. L. Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane. J. Biol. Chem. 255:1980;6314-6321.
29. Malozzi C., Di Stasi A. M. M., Minetti M. Free radicals induce reversible membrane-cytoplasm translocation of glyceraldehyde-3-phosphate dehydrogenase in human erythrocytes. Arch. Biochem. Biophys. 321:1995;345-352.
30. Low P. S. Structure and function of the cytoplasmic domain of band 3: Center of erythrocyte membrane-peripheral protein interactions. Biochim. Biophys. Acta. 864:1986;145-167.
31. Stamler J. S., Jia L., Eu J. P., McMahon T. J., Demchenko I. T., Bonaventura J., Gernet K., Piantadosi C. A. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science. 276:1997;2034-2037.
32. Eby D., Kirtley M. E. Isolation and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranes. Arch. Biochem. Biophys. 198:1979;608-613.
33. Brune S. Dimmeler, Molina y Vedia L., Lapetina E. G. Nitric oxide: A signal for ADP-ribosylation of proteins. Life Sci. 54:1993;61-70.
34. Hyslop P. A., Hinshaw D. B., Halsey W. A., Schraufstdtter I. U., Sauerheber R. D., Spragg R. G., Jacson J. H., Cochrane C. G. Mechanisms of oxidant-mediated cell injury: The glycolytic and mithocondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J. Biol. Chem. 263:1988;1665-1675.
35. Schuppe-Koistinen I., Moldius P., Bergman T., Cotgreave I. A. S-Thiolation of human endothelian cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment. Eur. J. Biochem. 221:1994;1033-1037.
36. Galli, F. Basta, G. Ubaldi, S. Rovidati, S. Luca, G. Canestrari, F. Calafiore, R. Effects of s-nitrosoglutethione (GSNO) on thiol homeostasis of pancreatic islets, Diabetes Nutr. Metab.