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Altered Protein Metabolism in Aging

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Special Focus on the Biology of Aging
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Abstract

The 20th century has witnessed a remarkable increase in the mean life expectancy of people in the developed countries. In the United States this increase amounts to about 25 years, or 50%. It is, however, widely recognized that the maximal human life-span, of about 100 years, has not changed at all during this period, and has possibly increased only marginally during the whole of recorded history. Most of the recent success in life extension was the result of the development of effective cures for infectious diseases, thereby greatly reducing mortality at young age. Significantly extending human maximal life-span by similarly curing “old age diseases” appears much more difficult because it is well documented (Kohn, 1963) that the mortality from almost any disease increases exponentially with age. Thus, even a small increase in maximal life-span, as a result of eliminating an “old age disease” will expose us to an ever-increasing number of new life-threatening diseases. Such strategy is, therefore, expensive and inefficient.

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References

  • Cerami, A., Vlassara, H., & Brownlee, M. (1987). Glucose and aging. Scientific American, 256, 90–96.

    Article  PubMed  CAS  Google Scholar 

  • Cini, J. K., Cook, P. F., & Gracy, R. W. (1988). Molecular basis for the isozymes of bovine glucose-6-phosphate isomerase. Archives of Biochemistry and Biophysics, 263, 96–106.

    Article  PubMed  CAS  Google Scholar 

  • Cook, L. L., & Gafni, A. (1988). Protection of phosphoglycerate kinase against in vitro aging by selective cysteine methylation. The Journal of Biological Chemistry, 263, 13991–13993.

    PubMed  CAS  Google Scholar 

  • Cutler, R. G. (1983). Species probes, longevity and aging. Modern Aging Research, Vol. 3B, (pp. 69–144). New York: Alan R. Liss.

    Google Scholar 

  • Davies, K. J. A. (1987). Protein damage and degradation by oxygen radicals. I. General aspects. The Journal of Biological Chemistry, 262, 9895–9901.

    PubMed  CAS  Google Scholar 

  • Gafni, A. (1983). Molecular origin of the aging effects in glyceraldehyde-3-phosphate dehydrogenase. Biochimica et Biophysica Acta, 742, 91–99.

    Article  PubMed  CAS  Google Scholar 

  • Gafni, A. (1985). Age-related modifications in a muscle enzyme. Modifications of Proteins During Aging, (pp. 19–39). New York: Alan R. Liss.

    Google Scholar 

  • Gafni, A. (1990). Age-related effects in enzyme metabolism and catalysis. Review of Biological Research in Aging Vol. 4, (pp. 315–336). New York: Alan R. Liss.

    Google Scholar 

  • Gafni, A., & Yuh, K. C. M. (1989). A comparative study of the Ca2+ — Mg2+ dependent ATPase from skeletal muscles of young, adult and old rats. Mechanisms of Ageing and Development, 49, 105–117.

    Article  PubMed  CAS  Google Scholar 

  • Gershon, H., & Gershon, D. (1970). Detection of inactive enzyme molecules in aging organisms. Nature, 227, 1214–1218.

    Article  PubMed  CAS  Google Scholar 

  • Gordillo, E., Ayala, A., F-Lobato, M., Bautista, J., Machado, A. (1988). Possible involvement of histidine residues in the loss of enzymatic activity of rat liver malic enzyme during aging. The Journal of Biological Chemistry, 263, 8053–8057.

    PubMed  CAS  Google Scholar 

  • Gracy, R. W., Yuksel, K. U., Chapman, M. L., Cini, J. K., Jahani, M., Lu, H. S., Oray, B., & Talent, J. M. (1985). Impaired protein degradation may account for the accumulation of “abnormal” proteins in aging cells. Modification of Proteins During Aging, (pp. 1–18). New York: Alan R. Liss.

    Google Scholar 

  • Gutterridge, J. M. C., Westermarck, T., & Halliwell, B., (1986). Oxygen radical damage in biological systems. Free Radicals, Aging and Degenerative Diseases, (pp. 99–140). New York: Alan R. Liss.

    Google Scholar 

  • Harman, D. (1956). Aging: a theory based on free radical and radiation chemistry. The Journal of Gerontology, 11, 298–300.

    Article  CAS  Google Scholar 

  • Harman, D. (1962). Role of free radicals in mutation, cancer, aging, and the maintenance of life. Radiation Research16, 753–763.

    Article  PubMed  CAS  Google Scholar 

  • Harman, D. (1988). Free radicals in aging. Molecular and Cellular Biochemistry, 84, 155–161.

    Article  PubMed  CAS  Google Scholar 

  • Kohn, R. R. (1963). Human aging and disease. Journal of Chronic Diseases, 16, 5–21.

    Article  PubMed  CAS  Google Scholar 

  • Mauron, J. (1981). The Maillard reaction in food; a critical review from the nutritional standpoint. Progress in Food and Nutrition Science, 5, 5–35.

    PubMed  CAS  Google Scholar 

  • Narayanan, N. (1987). Comparison of ATP dependent calcium transport and calcium activated ATPase activities of cardiac sarcoplasmic reticulum and sarcolemma from rats of various ages. Mechanisms of Ageing and Development, 38, 127–143.

    Article  PubMed  CAS  Google Scholar 

  • Nohl, H. (1982). Age-dependent changes in the structure-function correlation of ADP/ ATP translocating mitochondrial membranes. Gerontology, 28, 354–359.

    Article  PubMed  CAS  Google Scholar 

  • Noy, N., Schwartz, H., & Gafni, A. (1985). Age-related changes in the redox status of rat muscle cells and their role in enzyme aging. Mechanisms of Ageing and Develop ment, 29, 63–69.

    Article  CAS  Google Scholar 

  • Oliver, C. N., Ahn, B., Moerman, E. J., Goldstein, S., & Stadtman, E. R. (1987). Age-related changes in oxidized proteins. The Journal of Biological Chemistry, 262, 5488–5491.

    PubMed  CAS  Google Scholar 

  • Orchard, C. H., & Lakatta, E. G. (1985). Intracellular calcium transients and developed tensions in rat heart muscle. A mechanism for the negative interval-strength relationship. Journal of General Physiology, 86, 637–651.

    Article  PubMed  CAS  Google Scholar 

  • Orgel, L. E. (1963). The maintenance of the accuracy of protein synthesis and its relevance to aging. Proceedings of the National Academy of Sciences, U.S.A., 49, 517–521.

    Article  CAS  Google Scholar 

  • Reiss, U., & Rothstein, M. (1974). Heat labile isozymes of isocitrate lyase from aging Turbatrix aceti. Biochemical and Biophysical Research Communications, 61, 1012–1016.

    Article  PubMed  CAS  Google Scholar 

  • Reznick, A. Z., Dovrat, A., Rosenfelder, L., Shpund, S., & Gershon, D. (1985). Defective enzyme molecules in cells of aging animals are partially denatured, totally inactive, normal degradation intermediates. Modification of Proteins During Aging, (pp. 69–81). New York: Alan R. Liss.

    Google Scholar 

  • Richardson, A., & Semsei, I. (1987). Effect of aging on translation and transcription. Review of Biological Research in Aging, vol. 3, (pp. 467–483). New York, Alan R. Liss.

    Google Scholar 

  • Rothstein, M. (1975). Aging and the alteration of enzymes: A review. Mechanisms of Ageing and Development, 4, 325–338.

    Article  PubMed  CAS  Google Scholar 

  • Rothstein, M. (1982). Enzymes and altered proteins. Biochemical Approaches to Aging, (pp. 213–255). New York: Academic Press.

    Chapter  Google Scholar 

  • Rothstein, M. (1985a). The alteration of enzymes in aging. Modification of Proteins During Aging, (pp. 53–67). New York: Alan R. Liss.

    Google Scholar 

  • Rothstein, M. (1985b). Age-related changes in enzyme levels and enzyme properties. Review of Biological Research in Aging, Vol. 2, (pp. 421–433). New York: Alan R. Liss.

    Google Scholar 

  • Sarkis, G. J., Ashcom, J. D., Hawdon, J. M., & Jacobson, L. A. (1988). Decline in protease activities with age in the nematode Caenorhabditis elegans. Mechanisms of Ageing and Development, 45, 191–201.

    Article  PubMed  CAS  Google Scholar 

  • Sharma, H. K., & Rothstein, M. (1978). Age-related changes in the properties of enolase from Turbatrix aceti. Biochemistry, 17, 2869–2876.

    Article  PubMed  CAS  Google Scholar 

  • Sharma, H. K., & Rothstein, M. (1984). Altered brain phosphoglycerate kinase from aging rats. Mechanisms of Ageing and Development, 25, 285–296.

    Article  PubMed  CAS  Google Scholar 

  • Sharma, H. K., Prasanna, H. R., & Rothstein, M. (1980). Altered phosphoglycerate kinase in aging rats. The Journal of Biological Chemistry, 255, 5043–5050.

    PubMed  CAS  Google Scholar 

  • Stadtman, E. R. (1988). Protein modification in aging. The Journal of Gerontology, 43, B112–120.

    Article  Google Scholar 

  • Yuh, K. C. M., & Gafni, A. (1987). Reversal of age-related effects in rat muscle phosphoglycerate kinase. Proceedings of the National Academy of Sciences, U.S.A., 84, 7458–7462.

    Article  CAS  Google Scholar 

  • Velez, M., Machado, A., & Satrustegui, J. (1985). Age-dependent modifications in rat heart succinate dehydrogenase. Mechanisms of Ageing and Development, 32, 131–140.

    Article  PubMed  CAS  Google Scholar 

  • Zuniga, A., & Gafni, A. (1988). Age-related modifications in rat cardiac phosphoglycerate kinase. Rejuvenation of the old enzyme by unfolding-refolding. Biochimica et Biophysica Acta, 955, 50–57.

    Article  PubMed  CAS  Google Scholar 

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© 1991 Springer Science+Business Media New York

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Gafni, A. (1991). Altered Protein Metabolism in Aging. In: Cristofalo, V.J., Lawton, M.P. (eds) Special Focus on the Biology of Aging. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-38445-9_7

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  • DOI: https://doi.org/10.1007/978-3-662-38445-9_7

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-37652-2

  • Online ISBN: 978-3-662-38445-9

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