Effects of aging on the various steps of protein synthesis: Fragmentation of elongation factor 2

Free Radical Biology and Medicine

Volumn 26, Issue 3-4, 1999, Pages 362-370

  Parrado, Juan ^a   Bougria, Mohammed ^a   Ayala, Antonio ^a   Castaño, Angelica ^a   Machado, Alberto ^a  

^a UNIVERSITY OF SEVILLE   (Spain)

Author keywords

Aging; Elongation factor 2; Free radical; Oxidative stress; Protein synthesis

Indexed keywords

ELONGATION FACTOR 2;

AGING; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CORRELATION FUNCTION; FEMALE; LIVER; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DETERMINATION; PROTEIN SYNTHESIS; RAT; RNA TRANSLATION;

AGING; AMINO ACID SEQUENCE; ANIMALS; FEMALE; FREE RADICALS; ISOELECTRIC FOCUSING; LIVER; MOLECULAR SEQUENCE DATA; OXIDATIVE STRESS; PEPTIDE CHAIN TERMINATION, TRANSLATIONAL; PEPTIDE ELONGATION FACTOR 2; PEPTIDE ELONGATION FACTORS; PHOSPHOPROTEINS; RATS; RATS, WISTAR;

ANIMALIA;

EID: 0032901078     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00202-0     Document Type: Article

References (47)

1. Richardson A., Birchenall-Sparks M.C. Age-related changes in protein synthesis. Review of Biological researching in aging. Vol. 1:1983;255-273 Alan R. Liss, Inc, New York.
2. Makrides S.C. Protein synthesis and degradation during aging and senescence. Biol. Rev. 58:1983;343-422.
3. Webster G.C. Protein synthesis in aging organisms. Sohal R.S., Birnbaum L.S., Cutler R.G. Molecular biology of aging: Gene stability and gene expression. 1985;263-289 Raven, New York.
4. Stadtman E.R. Protein oxidation and aging. Science. 257:1992;1220-1224.
5. Rattan S.I.S. Synthesis, modifications and turnover of proteins during aging. Exp. Gerontol. 31:1996;33-37.
6. Rattan S.I.S. Protein synthesis and the components of protein synthetic machinery during cellular ageing. Mutation Res. 256:1991;115-125.
7. Kimball S.R., Vary T.C., Jefferson L.S. Age-dependent decrease in the amount of eukaryotic initiation factor 2 in various rat tissues. Biochem. J. 286:1992;263-268.
8. Shikama N., Ackermann R., Brack C. Protein synthesis elongation factor EF-1 alpha expression and longevity in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA. 91:1994;4199-4203.
9. Ayala A., Parrado J., Bougria M., Machado A. Effect of oxidative stress, produced by cumene hydroperoxide, on the various steps of protein synthesis. J. Biol. Chem. 271:1996;23105-23110.
10. Tamarit J., Cabiscol E., Ros J. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273:1997;3027-3032.
11. Harman D. The aging process. Proc. Natl. Acad. Sci. USA. 78:1981;7124-7128.
12. Pacifici R.E., Davies K.J.A. Protein degradation as and index of oxidative stress. Methods Enzymol. 186:1990;485-502.
13. Stadtman E.R. Oxidation of free amino acids and amino acids residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62:1993;797-821.
14. Sahakian J.A., Szweda L.I., Friguet B., Kitani K., Levine R.L. Aging of the liver proteolysis of oxidatively modified glutamine synthetase . Arch. Biochem. Biophys. 318:1995;411-417.
15. Ayuso-Parrilla M.S., Martin-Requero A., Perez-Diaz J., Parrilla R. Role of glucagon on the control of hepatic protein synthesis and degradation in the rat in vivo. J. Biol. Chem. 251:1976;7785-7790.
16. Scornik O.A. In vivo rate of translation by ribosomes of normal and regenerating liver. J. Biol. Chem. 249:1974;3876-3883.
17. Esterbauer H., Cheeseman K.H. Determination of aldehydic lipid peroxidation products malonaldehyde and 4-hydroxynonenal . Methods Enzymol. 186:1990;407421.
18. Lenz A.G., Costabel U., Shaltiel S., Levine R.L. Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride. Anal. Biochem. 177:1989;419-425.
19. Riis B., Rattan S.I.S., Clark B.F.C. Estimating the amounts of ADP-ribosylatable active elongation factor-2 in mammalian cell-free extracts. J. Biochem. Biophys. Methods. 19:1989;319-326.
20. Redpath N.T. High-resolution one-dimensional polyacrylamide gel isoelectric focusing of various forms of elongation factor-2. Anal. Biochem. 202:1992;340-343.
21. Parrado J., Ayala A., Machado A. Direct quantitative determination of peptides and proteins in PVDF transfer membranes using a computing densitometer. Peptide Res. 6:1993;13-16.
22. Ku Z., Thomason D.B. Soleus muscle nascent polypeptide chain elongation slows protein synthesis rate during non-weight-bearing activity. Am. J. Physiol. 267:1994;115-126.
23. Omura F., Kohno K., Uchida T. The histidine residue of codon 715 is essential for function of elongation factor 2. Eur. J. Biochem. 180:1989;1-8.
24. Cook J.R., Buetow D.E. Decreased protein synthesis by polysomes, tRNA and aminoacyl-tRNA synthetases from senescent rat liver. Mech. Ageing Dev. 17:1981;41-52.
25. Moudgil P.G., Cook J.R., Buetow D.E. The proportion of ribosomes active in protein synthesis and the content of polyribosomal poly(A)-containing RNA in adult and senescent rat livers. Gerontology. 25:1979;322-326.
26. Riis B., Ward W.F., Clark B.F.C., Nygård O. Polysome profile and in vitro protein synthesis capacity in liver cell extracts from young and old Fischer 344 rats. Top Aging Res. Europe. 16:1991;115-124.
27. Claes-Reckinger N., Vandenhaute J., Van Benzooijen C.F., Delcour J. Functional properties of rat liver protein synthesizing machinery in relation to aging. Exp. Gerontol. 17:1982;281-286.
28. Layman D.K., Ricca G.A., Richardson A. The effect of age on protein synthesis and ribosome aggregation to messenger RNA in rat liver. Arch. Biochem. Biophys. 173:1976;246-254.
29. Vandenhaute J., Claes-Reckinger N., Delcour J. Age-related functional alteration of mouse liver ribosomes. Exp. Gerontol. 18:1983;355-363.
30. Makrides S.C., Goldthwaite J. The content and size distribution of membrane-bound and free polyribosomes in mouse liver during aging. Mech. Ageing Dev. 27:1984;111-134.
31. Richardson A. The relationship between aging and protein synthesis. Florini J.R. Handbook of Biochemistry in Aging. 1981;79-101 CRC Press, Inc, Florida.
32. Nygard O., Nilsson L. Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis. Eur. J. Biochem. 191:1990;1-17.
33. Hershey J.W.B. Translational control in mammalian cells. Annu. Rev. Biochem. 60:1991;717-755.
34. Van Ness B.G., Howard J.B., Bodley J.W. ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products. J. Biol. Chem. 255:1980;10710-10716.
35. Fendrick J.L., Igleswki W.J. Endogenous ADP-ribosylation of elongation factor 2 in polyoma virus-transformed baby hamster kidney cells. Proc. Natl. Acad. Sci. USA. 86:1989;554-557.
36. Perentesis J.P., Miller S.P., Bodley J.W. Protein toxin inhibitors of protein synthesis. Biofactors. 3:1992;173-184.
37. Riis B., Rattan S.I.S., Derventzi A., Clark B.F.C. Reduced levels of ADP-ribosylatable elongation factor-2 in aged and SV40-transformed human cell cultures. FEBS Lett. 266:1990;45-47.
38. Rattan S.I.S., Ward W.F., Glenting M., Svendsen L., Riis B., Clark B.D.F. Dietary calorie restriction does not affect the levels of protein elongation factors in rat livers during ageing. Mech. Ageing Dev. 6:1991;379-382.
39. Stadtman E.R. Oxidation of proteins by mixed-function oxidation systems implication in protein turnover, ageing and neutrophil function . Trends Biochem. Sci. 11:1986;11-12.
40. Cabiscol E., Levine R.L. Carbonic anhydrase III. Oxidative modification in vivo and loss of phosphatase activity during aging. J. Biol. Chem. 270:1995;14742-14747.
41. Schraufstätter I.U., Hyslop P.A., Hinshaw D.B., Spragg R.G., Sklar L.A., Cochrane C.G. Hydrogen peroxide-induced injury of cells and its prevention by inhibitors of poly(ADP-ribose) polymerase. Proc. Natl. Acad. Sci. USA. 83:1986;4908-4912.
42. Hyslop P.A., Hinshaw D.B., Halsey W.A. Jr, Schraufstätter I.U., Sauerheber R.D., Spragg R.G., Jackson J.H., Cochrane C.G. Mechanisms of oxidant-mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J. Biol. Chem. 263:1988;1665-1675.
43. Giovane A., Servillo L., Quagliuolo L., Balestrieri C. Purification of elongation factor 2 from human placenta and evidence of its fragmentation patterns in various eukaryotic sources. Biochem. J. 244:1987;337-344.
44. Davies K.J.A. Protein damage and degradation by oxygen radicals: I. General aspects. J. Biol. Chem. 262:1987;9895-9901.
45. Grune T., Reinheckel T., Davies K.J.A. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J. Biol. Chem. 271:1996;15504-15509.
46. Dean R.T., Gieseg S., Davies M.J. Reactive species and their accumulation on radical-damaged proteins. Trends Biochem. Sci. 18:1993;437-441.
47. Dean R.T., Fu S., Stocker R., Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 32:1997;1-18.