Many faces of superoxide dismutase, originally known as erythrocuprein

Current Science

Volumn 92, Issue 2, 2007, Pages 184-191

  Ramasarma, T ^a,b  

^a CENTRE FOR DNA FINGERPRINTING AND DIAGNOSTICS   (India)

^b INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Calcineurin inactivation; Cholesterol biogenesis; Pyrogallol autoxidation; Superoxide dismutase

Indexed keywords

EID: 33847096515     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (52)

1. Ramasarma, T., One protein - many functions. Curr. Sci., 1994, 67, 24-29.
2. Mann, T. and Keilin, D., Hemocuprein and hepatocuprein, copper-protein compounds of blood and liver in mammals. Proc. R. Soc. London, Ser. B., 1938, 126, 303-315.
3. Carrico, R. J. and Deutsch, H. F., Isolation of human hepatocuprein and cerebrocuprein, Their identitiy with erythrocuprein. J. Biol. Chem., 1969, 244, 6087-6093.
4. Fridovich, I., The trail of superoxide dismutase. Protein Sci., 1998, 7, 2688-2690.
5. McCord, J. M. and Fridovich, I., Superoxide dismutase, an enzyme function for erythrocuprein (hemocuprein). J. Biol. Chem., 1969, 244, 6049-6055.
6. Misra, H. P. and Fridovich, I., The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J. Biol. Chem., 1972, 247, 3170-3175.
7. Ramasarma, T., Is it fair to describe a protein recruited for many cellular chores as 'moonlighting' and 'promiscuous'?. Curr. Sci., 1999, 77, 1401-1405.
8. Hekkila, R. E. and Cohen, G., 6-Hydroxydopamine: evidence for superoxide radical as an oxidative intermediate. Science, 1973, 181, 456-457.
9. Marklund, S. and Marklund, G., Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem., 1974, 47, 469-474.
10. Aparna Rao, V. S. and Ramasarma, T., Rate of catalytic activity of superoxide dismutase (SOD): A method based on a new interpretation of its inhibition of pyrogallol autoxidation. Curr. Sci., 2007, in press.
11. Ramasarma, T., Mackellar, W. and Crane, F. L., Nature of NADH: acceptor oxido-reductase in plasma membranes of mouse liver. Indian J. Biochem. Biophys., 1980, 17, 163-167.
12. Ramasarma, T., Mackellar, W. and Crane, F. L., Vanadate stimulated NADH oxidation in plasma membranes. Biochim. Biophys. Acta, 1981, 646, 88-98.
13. Dar, D. and Fridovich, I., Vanadate and molybdate stimulate the oxidation of NADH by superoxide radical. Arch. Biochem. Biophys., 1984, 232, 562-565.
14. Khandke, L., Sharada, G., Patole, M. S. and Ramasarma, T., Vanadate-stimulated NADH oxidation - an intrinsic property of xanthine oxidase. Arch. Biochem. Biophys., 1986, 244, 742-749.
15. Ramasarma, T., The emerging redox profile of vanadium. Proc. Indian Natl. Sci. Acad. Sect. B, 2003, B69, 649-672.
16. III-salen. Inorg. Chem., 2000, 39, 274-280.
17. Klee, C. B., Ren, H. and Wang, X., Regulation of the calmodulin- stimulated protein phosphatase, calcineurin. J. Biol. Chem., 1998, 273, 13367-13370.
18. King, M. M., Modification of the calmodulin-stimulated phosphatase, calcineurin, by sulphydryl reagents. J. Biol. Chem., 1986, 261, 4081-4086.
19. Volkel, H. et al., Superoxide dismutase mutations of familial amyotrophic lateral sclerosis and the oxidative inactivation of calcineurin. FEBS Lett., 2001, 503, 201-205.
20. Wang, X., Culotta, V. C. and Klee, C. B., Superoxide dismutase protects calcineurin from inactivation. Nature, 1996, 383, 434-437.
21. Carabello, M. et al., Characterization of calcineurin in human neutrophils. Inhibitory effect of hydrogen peroxide on its enzyme activity and on NF-B DNA binding. J. Biol. Chem., 1999, 274, 93-100.
22. Cabelli, D. E., Allen, D. and Bielski, B. H. J., The interaction between Cu(I) superoxide dismutase and hydrogen peroxide. J. Biol. Chem., 1989, 264, 9967-9971.
23. Yim, M. B., Chook, P. B. and Stadtman, E. R., Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J. Biol. Chem., 1992, 268, 4099-4105.
24. 2 in presence of abundant catalase. Biochim. Biophys. Acta, 1998, 1381, 249-255.
25. Murphy, M. E. and Sies, H., Reversible conversion of nitroxyl anion to nitric oxide by superoxide dismutase. Proc. Natl. Acad. Sci. USA, 1991, 88, 10860-10864.
26. Laranjinha and Cadenas, E., Oxidation of DOPAC by nitric oxide: effect of superoxide dismutase. J. Neurochem., 2002, 81, 893-900.
27. Downey, J. M., Free radicals and their involvement during myocardial ischemia and reperfusion. Annu. Rev. Physiol., 1990, 52, 487-504.
28. Wawryn, J., Swiecilo, A., Bartosz, G. and Bilinski, T., Effect of superoxide dismutase deficiency on the lifespan of the yeast Saccharomyces cerevisiae. An oxygen-independent role of Cu, Zn-superoxide dismutase. Biochim. Biophys. Acta, 2002, 1570, 199-202.
29. Fee, J. A., Superoxide, superoxide dismutases and oxygen toxicity. In Metal Ion Activation of Dioxygen (ed. Spiro, T. G.), John Wiley, 1980, pp. 209-237.
30. Mondola, P. et al., Effect of Cu, Zn superoxide dismutase on cholesterol metabolism in human hepatocarcinoma (HepG2) cells. Biochem. Biophys. Res. Commun., 2002, 295, 603-609.
31. Mondola, P., Bifulco, M., Seru, R., Annella, T. and Ciriola, M. R., Presence of superoxide dismutase in human serum lipoproteins. FEBS Lett., 2000, 467, 57-60.
32. Ramasarma, T., Control of biogenesis of isoprenoid compounds in animals. In Current Topics in Cellular Regulation (eds Horecker, B. L. and Stadtman, E. R.), Academic Press, 1972, vol. 6, pp. 169-207.
33. Ramasarma, T., Endogenous inhibitors of cholesterol biogenesis. Indian J. Physiol. Allied Sci., 1997, 38-47.
34. Rosen, D. R. et al., Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature, 1993, 362, 59-62.
35. Anderson, P. M., Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase. Curr. Neurol. Neurosci. Rep., 2006, 6, 37-46.
36. Ogasawara, M., Matsubara, Y., Narisawa, K., Aoki, M., Nakamura, S., Itoyama, Y. and Abe, K., Mild ALS in Japan associated with novel SOD mutation. Nature Genet., 1993, 5, 323-324.
37. Rabizedeh, S. et al., Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA, 1995, 92, 3024-3028.
38. Gurney, M. E. et al., Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science, 1994, 264, 1772-1774.
39. Wiedau-Pazos, M. et al., Altered reactivity of superoxide dismutase in amyotrophic lateral sclerosis. Science, 1996, 271, 515-518.
40. Kang, J. H. and Eum, W. S., Enhanced oxidative damage by the familial amyotrophic lateral sclerosis-associated Cu-Zn-superoxide dismutase. Biochim. Biophys. Acta, 2000, 1524, 162-170.
41. Johnston, J. A., Dalton, M. J., Gurney, M. E. and Kopoto, R. R., Formation of high molecular weight complexes of mutant Cu, Znsuperoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA, 2000, 97, 12571-12576.
42. Hough, M. A. et al., Dimer stabilization in superoxide dismutase may result in disease-causing properties: structure of motor neuron disease mutants. Proc. Natl. Acad. Sci. USA, 2004, 101, 5976-5982.
43. Ray, S. S., Nowak, R. J., Brown Jr. R. H. and Lansbury Jr. P. T., Small molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proc. Natl. Acad. Sci. USA, 2005, 102, 3639-3644.
44. Tiwari, A., Xu, Z. and Hayward, L. J., Abberantly increased hydrophobicity shared mutants of Cu, Zn-superoxide dismutase in familial amyotrophic lateral sclerosis. J. Biol. Chem., 2005, 280, 29771-29779.
45. Ferri, A., Gabbianelli, R., Casciati, A., Paolucci, E., Rptillo, G. and Carri, M. T., Calcineurin activity is regulated both by redox compounds and by mutant familial amyotrophic lateral sclerosissuperoxide dismutase. J. Neurochem., 2000, 75, 606-613.
46. Turner, B. J. et al., Impaired extracellular secretion of mutant superoxide dismutase 1 associated with neurotoxicity in familial amyotrophic lateral sclerosis. J. Neurosci., 2005, 25, 108-117.
47. Banci, L., Berini, I., Cantini, F., D'Amello, N. and Gaggelli, E., Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. J. Biol. Chem., 2006, 281, 2333-2337.
48. Brown, D. R., Wong, B.-S., Hafiz, F., Clive, C., Haswell, S. J. and Jones, I. M., Normal prion protein has an activity like that of superoxide dismutase. Biochem. J., 1999, 344, 1-5.
49. Woo, E.-J., Dunwell, J. M., Goodenough, P. W., Marvier, A. C. and Pickersgill, R. W., Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nature Struct. Biol., 2000, 11, 1036-1040.
50. Singh, A., Sowjanya, P. and Ramakrishnan, G., The wild-type Ras: road ahead. FASEB J., 2005, 19, 161-169.
51. Anderson, P. M., Amyotrophic lateral sclerosis associated with mutations in the Cu, Zn superoxide dismutase gene. Curr. Neurol. Neurosci. Rep., 2006, 6, 37-46.
52. Chance, B., Sies, H. and Boveris, A., Hydroperoxide metabolism in mammalian tissues. Physiol. Rev., 1979, 59, 527-605.