Hostname: page-component-586b7cd67f-vdxz6 Total loading time: 0 Render date: 2024-11-25T05:00:16.681Z Has data issue: false hasContentIssue false
  • English
  • Français

Elevated erythrocyte phosphoribosylpyrophosphate and ATP concentrations in Japanese sumo wrestlers

Published online by Cambridge University Press:  09 March 2007

Y. Nishida ,
I. Akaoka ,
E. Hayashi  and
T. Miyamoto
Y. Nishida
Affiliation:
Department of Medicine and Physical Therapy, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, Japan 113
I. Akaoka
Affiliation:
Department of Medicine and Physical Therapy, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, Japan 113
E. Hayashi
Affiliation:
Department of Medicine and Physical Therapy, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, Japan 113
T. Miyamoto
Affiliation:
Department of Medicine and Physical Therapy, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, Japan 113
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. Japanese sumo wrestlers have a diet rich in energy, which results in marked obesity. Their plasma urate and triglyceride levels were significantly elevated.

2. Erythrocyte phosphoribosylpyrophosphate (PRPP) and ATP concentrations in sumo wrestlers were significantly elevated when compared to the levels in control subjects.

3. There were no significant differences in erythrocyte PRPP synthetase (EC 2.7.6.1), purine nucleoside phosphorylase (EC 2.4.2.1) and hypoxanthine guanine phosphoribosyl transferase (EC 2.4.2.8) activities between sumo wrestlers and control subjects.

4. Erythrocyte adenosine kinase (EC 2.7.1.20), adenosine deaminase (EC 3.5.4.4) and adenine phosphoribosyl transferase (EC 2.4.2.7) activities in sumo wrestlers were significantly elevated.

5. It seems that sumo wrestlers have an increased turnover of adenine nucleotides which may contribute to hyperuricaemia.

Type
Papers of direct relevance to Clinical and Human Nutrition
Information
British Journal of Nutrition , Volume 49 , Issue 1 , January 1983 , pp. 3 - 7
Copyright
Copyright © The Nutrition Society 1983

References

Adam, L. (1972). In Methods in Enzymatic Analysis, p. 539 [Bergmeyer, H. V., editor]. Berlin: Weinhein Verlag Chemie.Google Scholar
Arnold, W. J. & Kelley, W. N. (1973). J. clin. Invest. 52, 970.CrossRefGoogle Scholar
Arnold, W. J., Meade, J. C. & Kelley, W. N. (1972). J. clin Invest. 51, 1805.CrossRefGoogle Scholar
Bode, J. Ch., Zelder, O., Rumpelt, H. J. & Wittkamp, U. (1973). Eur. J. clin. Invest. 3, 436.CrossRefGoogle Scholar
Bowering, J., Calloway, D. H., Margen, S. & Kaufmann, N. A. (1970). J. Nutr. 100, 249.CrossRefGoogle Scholar
Edwards, N. L., Recker, D. & Fox, I. H. (1979). J. clin. Invest. 63, 922.CrossRefGoogle Scholar
Emmerson, B. T. (1973). Aust. N.Z. Jl Med. 3, 410.CrossRefGoogle Scholar
Fox, I. H. & Kelley, W. N. (1971). Anns int Med. 74, 424.CrossRefGoogle Scholar
Hall, A. P., Barry, P. E., Dawber, T. R. & McNamara, P. M. (1967). Amer. J. Med. 42, 27.CrossRefGoogle Scholar
Hayashi, E. (1971). Ryumachi 11, 11.Google Scholar
Healey, L. A., Cancer, J. E. Z., Bassett, D. R. & Decker, J. L. (1966). J. Am. med. Ass. 196, 152.CrossRefGoogle Scholar
Henderson, J. F. & Khoo, M. K. Y. (1965). J. biol. Chem. 240, 2349.CrossRefGoogle Scholar
Hershko, A., Razin, A. & Mager, J. (1969). Biochim. biophys. Acta 184, 64.CrossRefGoogle Scholar
Hevia, P. & Clifford, A. J. (1977). J. Nutr. 107, 969.CrossRefGoogle Scholar
Hopkinson, D. A., Cook, P. J. L. & Harris, H. (1969). Ann. Hum. Genet. 32, 361.CrossRefGoogle Scholar
Itoh, R. & Tsushima, K. (1972). Biochim. Biophys. Acta. 273, 229.CrossRefGoogle Scholar
Katunuma, N., Matsuda, Y. & Kuroda, Y. (1970). Adv. Enzyme Regul. 8, 73.CrossRefGoogle Scholar
Liddle, L., Seegmiller, J. E. & Laster, L. (1959). J. Lab. clin. Med. 54, 903.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Meyskens, F. L. & Williams, H. (1970). Biochim. biophys. Acta 240, 170.CrossRefGoogle Scholar
Nicholls, A. & Scott, J. T. (1972). Lancet ii, 1223.CrossRefGoogle Scholar
O'Brien, W. M., Burch, T. A. & Bunim, J. J. (1966). Ann. rheum. Dis. 25, 117.CrossRefGoogle Scholar
Prior, I. A. M., Rose, B. S., Harvey, H. P. B. & Davidson, F. (1966). Lancet i, 333.CrossRefGoogle Scholar
Rose, B. S. & Prior, I. A. M. (1963). Ann rheum. dis. 22, 410.CrossRefGoogle Scholar
Sugiura, M., Oikawa, T., Hirano, K., Maeda, H., Yoshimura, H., Sugiyama, M. & Kuratsu, T. (1977). Clinica chim. Acta 81, 125.Google Scholar
Thomas, C. B., Arnold, W. J. & Kelley, W. N. (1973). J. biol. Chem. 248, 2529.CrossRefGoogle Scholar