Biochemical Genetics

, Volume 27, Issue 9–10, pp 487–495 | Cite as

Plasma trehalase activity and diabetes mellitus

  • L. C. Eze


Trehalase is an enzyme which hydrolyzes the disaccharide trehalose, yielding glucose. It is widespread in nature and found in various human tissues as well as in human plasma. The synthesis and degradation of its substrate trehalose have been considered as being implicated in carbohydrate transport mechanisms. Trehalase activity has been examined in both normal subjects and diabetic patients. In the normal subjects, the frequency histogram of the enzyme activity is bimodal, indicating the existence of genetic polymorphism. The proposed model of a single autosomal locus with two alleles has been verified, with 27% of the population tested belonging to the “low-activity” phenotype and 73% being of the “high-activity” phenotype. Males have higher mean plasma trehalase activity than females. Apparently, the reverse appears to be the case in the diabetic subjects. The mean value for all nondiabetics and that of diabetics were computed and the difference was found to be statistically significant (F=7.02,Nl=3,N2=56,P<0.01). An experiment showed that neither the abnormally high concentration of glucose in diabetics nor any other constituent of the diabetic plasma caused an increase in plasma trehalase activity (t=0.0724,P>0.10). A Woolf and Haldane test to determine association of diabetes mellitus and plasma trehalase phenotype indicated a highly significant association with the high-activity phenotype (X2=18.5350,P<0.01). Thus the inference is that people with high plasma trehalase activity are more prone to develop diabetes mellitus than people with low enzyme activity.

Key words

trehalose trehalase diabetes mellitus 


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  1. Bourquelot, E. (1893). Transformation du trehalose en glucose dans les Champignons par un ferment soluble: La trehalase.Bull. Soc. Mycol. France 9189.Google Scholar
  2. Cooper, G. R., and McDanile, V. (1970).Standard Methods Clin. Chem. 6159.Google Scholar
  3. Courtois, J. E., and Demelier, J. F. (1966). Reparatition de la trehalase chez l'homme et quelques mammiferes.Bull. Soc. Chim. Biol. 48277.PubMedGoogle Scholar
  4. Courtois, J. E., Debris, M., and Georget, J. C. (1962). Mise en evidence d'une trehalase dans le serum humain.Bull. Acad. Natl. Med. 146599.PubMedGoogle Scholar
  5. Evans, D. A. P., Eze, L. C., and Whibley, E. J. (1983). The association of the slow acetylator phenotype with bladder cancer.J. Med. Genet. 20(5):330.PubMedGoogle Scholar
  6. Eze, L. C., Tweedie, M. C. K., and Evans, D. A. P. (1970). Genetic factors influencing human serum trehalase activity.J. Med. Genet. 7(1):5.PubMedGoogle Scholar
  7. Friedman, S. (1968). Trehalase regulation of glucose-6-phosphate hydrolysis in blowfly extracts.Science 159110.PubMedGoogle Scholar
  8. Glowinski, I. B., Weber, W. W., Fysh, J. M., Vaught, J. B., and King, C. M. (1980). Evidence that arylhydroxamic acid N,0-acyltransferase and the genetically polymorphic N-acetyltransferase are properties of the same enzyme in rabbit liver.J. Biol. Chem. 2557883.PubMedGoogle Scholar
  9. Haldane, J. (1955). The estimation and significance of logarithm of a ratio of frequencies.Ann. Hum. Genet. 20309.Google Scholar
  10. Kalf, G. F., and Reider, S. V. (1958). The purification and properties of trehalase.J. Biol. Chem. 12051.Google Scholar
  11. Kenny, A. J., and Maroux, S. (1982). Topology of microvillar membrane hydrolases of kidney and intestine.Physiol. Rev. 6291.PubMedGoogle Scholar
  12. Madzarovova-Nohejlova, J. (1973). Gastroenterology65130.PubMedGoogle Scholar
  13. Mazon, M. J., Gancedo, J. M., and Gancedo, C. (1982). Phosphorylation and inactivation of yeast fructose-biphosphatase in vivo by glucose and by proton ionophores—a possible role for cAMP.Eur. J. Biochem. 127605.PubMedGoogle Scholar
  14. Sacktor, B. (1968). Trehalase and the transport of glucose in the mammalian kidney and intestine.Proc. Natl. Acad. Sci. USA 601007.PubMedGoogle Scholar
  15. Sacktor, B., and Berger, S. J. (1969). Formation of trehalose from glucose in the renal cortex.Biochim. Biophys. Res. Commun. 35796.Google Scholar
  16. Scheffe, H. (1953). A method for judging all contrasts in the analysis of variance.Biometrika 6087.Google Scholar
  17. Toyoda, Y., Fujii, H., Miwa, I., Okuda, J., and Sy, J. (1987). Anomeric specificity of glucose effect on cAMP fructose 1,6-biphosphatase, and trehalase in yeast.Biochem. Biophys. Res. Commun. 143(1):212.PubMedGoogle Scholar
  18. Woolf, B. (1955). On estimating the relation between blood group and disease.Ann. Hum. Genet. 19251.PubMedGoogle Scholar

Copyright information

© Plenum Publishing Corporation 1989

Authors and Affiliations

  • L. C. Eze
    • 1
  1. 1.Department of BiochemistryUniversity of NigeriaNsukkaNigeria

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