, Volume 131, Issue 2, pp 93–97 | Cite as

Influence of carbon and nitrogen sources on glutathione catabolic enzymes inCandida albicans during dimorphism

  • Suresh Gunasekaran
  • Munyaradzi Imbayagwo
  • Louise McDonald
  • Muthukumaran Gunasekaran
  • Elias Manavathu
Human And Animal Mycology


The effect of carbon sources, glucose and sucrose, and nitrogen sources such as ammonia, glutamate andl-citrulline on the activities of glutathione metabolic enzymes has been studied. Yeast and mycelial cells were used to identify changes in activity levels of glutathione reductase (GSSGR), glutathione transferase (GST), glutathione peroxidase (GPX) and γ-glutamyl transpeptidase (GGT). Enzyme activities from cells grown in sucrose media were lower than in glucose media regardless of the enzyme tested, morphological form, or the growth interval. In all enzymes except GST, activity was higher in yeast form than in mycelia, regardless of nitrogen source, with lower activity from 24 to 72 h than at 96 h. In citrulline media, yeast form showed the maximum GST, GGT, and GPX activity. In ammonia-amended media, mycelia showed maximum activity in GGT, whereas in glutamate media, mycelia showed the maximum activity in GST. Also, the type of nitrogen source had no effect on GPX activity in the mycelial form. Finally, changing the nitrogen source showed no significant effect on GSSGR activity, either in the yeast or mycelial form.

Key words

Candida Glutathione Dimorphism Glutathione reductase GlutathioneS-transferase Glutathione peroxidase γ-Glutamyl transpeptidase 


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  1. 1.
    Vanden Bossche H, Kobayashi GS, Edman JC, Keath EJ, Maresca B, Soll DR. Molecular determinants of fungal dimorphism. J of Med and Vet Mycol 1992; 30: 73–76.Google Scholar
  2. 2.
    Datta A, Ganesan K, Natarajan K. Current trends inCandida albicans Research. Adv Microbiol Physiol 1989; 30: 53–88.Google Scholar
  3. 3.
    Nishioka Y, Silva-Hunter M. Dimorphism, sensitivity to nystatin and acriflavine uptake in a strain ofCandida albicans grown with glutamate as sole nitrogen and carbon source. Sabouraudia 1974; 12: 295–301.PubMedGoogle Scholar
  4. 4.
    Dabrowa N, Howard DH, Landau JW, Shechter Y. Synthesis of nucleic acid and protein in the dimorphic form ofCandida albicans. Sabouraudia 1970; 8: 163–69.PubMedGoogle Scholar
  5. 5.
    Meister A. New aspects of glutathione biochemistry and transport-selective alteration of glutathione metabolism. Nutritional Rev 1984; 42: 397–410.Google Scholar
  6. 6.
    Thornally PJ. The glyoxalate system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem J 1990; 269: 1–11.PubMedGoogle Scholar
  7. 7.
    Thomas D, Klein K, Manavathu E. Dimmock JR, Mutus B. Glutathione levels during thermal induction of the yeast to mycelial transition inCandida albicans. FEMS Letters 1991; 77: 331–334.Google Scholar
  8. 8.
    Penninckx MJ, Elskens MT. Metabolism and functions of glutathione in microorganisms. Adv Microbial Physiol 1993; 34: 239–304.Google Scholar
  9. 9.
    Penninckx MJ, Jaspers CJ, Wiame JM. Glutathione metabolism in relation to the amino acid permeation systems of the yeastSaccharomyces cerevisiae. Eur J Biochem 1980; 104: 119–123.PubMedGoogle Scholar
  10. 10.
    Lee KL, Buckley HR, Campbell CC. An amino acid liquid synthetic medium for the development of mycelial and yeast forms ofCandida albicans. Sabouridia 1975; 13: 148–153.Google Scholar
  11. 11.
    Carlberg I, Mannervik B. Glutathione reductase. In SP Colowick and NO Kaplan (eds.), Methods in Enzymol 1985; 113: 484–485.Google Scholar
  12. 12.
    Mannervik B, Guthenberg G. Glutathione transferases from human liver. In SP Colowick and NO Kaplan (eds.), Methods in Enzymol 1985; 113: 499–501.Google Scholar
  13. 13.
    Meister A, Tate SS, Griffith OW. Gamma-glutamyl transpeptidase. In SP Colowick and NO Kaplan (eds.), Methods in Enzymol 1981; 77: 237–44Google Scholar
  14. 14.
    Flohe L, Gunzler WA. Assays of glutathione peroxidase. In SP Colowick and NO Kaplan (eds.), Methods in Enzymol 1984; 105: 114–121.Google Scholar
  15. 15.
    Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248–254.PubMedGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Suresh Gunasekaran
    • 1
  • Munyaradzi Imbayagwo
    • 1
  • Louise McDonald
    • 2
  • Muthukumaran Gunasekaran
    • 1
  • Elias Manavathu
    • 2
  1. 1.Department of BiologyFisk UniversityNashvilleUSA
  2. 2.Department of MedicineWayne State UniversityDetroitUSA

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