, Volume 138, Issue 3, pp 109–115 | Cite as

Different protein kinase C isoforms are present in the yeast and mycelium forms of Sporothrix schenckii

  • Edna E. Aquino-Piñero
  • Nuri Rodríguez-del Valle


Protein kinase C (PKC) plays an important role in the control of proliferation and differentiation of a wide range of cell types, and fungi are no exception. Previous results reported by us on the effects of the phorbol ester, 12-myristate-13-acetate phorbol (PMA) and other PKC effector molecules, on dimorphism in Sporothrix schenckii suggested the presence of this enzyme in the fungus and its involvement in the control of morphogenetic transitions. The work summarized here confirms the presence of PKC in yeast and mycelium extracts of S. schenckii. Different isoforms of this enzyme were found to be present in the yeast and mycelium forms of the fungus and were identified by Western blot analysis using affinity purified anti-PKC isoforms specific antibodies: the γ and ζ isoforms were detected in both the yeast and mycelium forms of the fungus, while the β isoform was only detected in the yeast form. The presence of PKC was confirmed biochemically by measuring total enzyme activity in both forms of the fungus. No significant differences were observed for the PKC activity level recorded for both the mycelium and yeast forms of the fungus (p ≤ 0.05). These data confirm the presence of PKC activity in Sporothrix schenckii and constitutes the first evidence concerning the differential expression of PKC isoforms in the mycelium and yeast forms of a dimorphic fungus, supporting the possible involvement of this important signal transduction enzyme in the control of morphogenesis in this fungus.

Sporothrix schenckii protein kinase C dimorphism 


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  1. 1.
    Alsina A, Rodríguez-del Valle N. Effects of divalent (cations and functionally related substances on the yeast to mycelium transition in Sporothrix schenckii. Sabouradia 1984; 22: 1–5.Google Scholar
  2. 2.
    Rodríguez-del Valle N, Debs-Elfas, N, Alsina A. Effects of caffeine, cyclic 3',5' guanosine monophosphate and cyclic 3',5' monophosphate in the development of the mycelial form of Sporothrix schenckii. Mycopathologia 1984; 86: 29–33.PubMedCrossRefGoogle Scholar
  3. 3.
    Serrano, S, Rodríguez-del Valle N. Calcium uptake and efflux during the yeast tomycelium transition in Sporothrix schenckii. Mycopathogia 1990; 112: 1–9.CrossRefGoogle Scholar
  4. 4.
    Rodríguez-del Valle N, Rodríguez-Medina J. Calcium stimulates molecular and cellular events during the yeast to mycelial transition in Sporothrix schenckii. J Med Vet Mycol 1993; 31: 43–53.PubMedGoogle Scholar
  5. 5.
    Kikkawa U, Kishimoto A, Nishizuka Y. The protein kinase C family: heterogeneity and its implications. Ann Rev Biochem 1989; 58: 31–44.PubMedCrossRefGoogle Scholar
  6. 6.
    Nishizuka Y. Studies and perspectives of protein Kinase C. Science 1989; 233: 305–312.Google Scholar
  7. 7.
    Nishizuka Y. The molecular heterogeneity of protein kinase C and its implication for cellular regulation. Nature 1988; 334: 661–665.PubMedCrossRefGoogle Scholar
  8. 8.
    Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992; 258: 607–614.PubMedGoogle Scholar
  9. 9.
    Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Water-field MD, Francke U, Ullrich A. Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science 1986; 233: 859–866.PubMedGoogle Scholar
  10. 10.
    Osada S, Mizuno K, Saido TC, Akita Y, Suzuki K, Kuroki T, Ohno S. A phorbol ester receptor/protein kinase, nPKCn, a new member of the protein kinase C family predominantly expressed in lung and skin. J Biol Chem 1990; 265: 22434–22440.PubMedGoogle Scholar
  11. 11.
    Berry N, Ase K, Kikkawa U, Kishimoto A, Nishizuka Y. Human T cell activation by phorbol esters and diacylglycerol analogues. J Immunol 1989; 143: 1407–1413.PubMedGoogle Scholar
  12. 12.
    Farooqui AA, Farooqui T, Yates AJ, Horrocks LA. Regulation of protein kinase C activity by various lipids. Neurochem, Res 1988; 13: 499–511.CrossRefGoogle Scholar
  13. 13.
    Colón-Colón W, Rodríguez-del Valle N. Studies on phase transitions in Sporothrix schenckii: Possible involvement of Protein Kinase C. In: Vanden Bossche, H, Odds, FC., Kerridge, D, eds. Dimorphic Fungi in Biology and Medicine. New York: Plenum Publishing Co., 1993: 225–246.Google Scholar
  14. 14.
    Levin DE, Fields FO, Kunisawa R, Bishop JM, Thorner J A. A candidate protein kinase C gene, PKC-1, is required for the S. cerevisiae cell cycle. Cell 1990; 62: 213–224.PubMedCrossRefGoogle Scholar
  15. 15.
    Parvicini G, Mendoza A, Antonsson B, Cooper M, Losberger C, Payton MA. The Candida albicans PKC-1 gene encodes a protein kinase C homolog necessary for cellular integrity but not dimorphism. Yeast 1996; 12: 741–756.CrossRefGoogle Scholar
  16. 16.
    Betancourt S, Torres-Bauz´a LJ, Rodríguez-del Valle N. Molecular and cellular events during the yeast to mycelium transition in Sporothrix schenckii. Sabouraudia 1985; 23: 207–209.PubMedGoogle Scholar
  17. 17.
    Mendonça L, Gorin PAJ, Lloyd KO, Travassos, LR Polymophism of S. schenckii surface polysaccharides as a function of morphological differentiation. Biochemistry 1976; 15: 2423–2431.PubMedCrossRefGoogle Scholar
  18. 18.
    Resto S, Rodríguez-del Valle N. Yeast cell cycle of Sporothrix schenckii. J Med Vet Mycol 1988; 26: 13–24.PubMedGoogle Scholar
  19. 19.
    Laemmli UK. Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 1970; 227: 680–685.PubMedCrossRefGoogle Scholar
  20. 20.
    Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some application. Proc Natl Acad Sci (USA) 1979; 76: 4350–4354.CrossRefGoogle Scholar
  21. 21.
    Henrich CJ. Tools for the study of protein kinase C and its isozymes. Focus 1991; 13: 133–136.Google Scholar
  22. 22.
    Beh I, Schmidt R, Hecker E. Two isozymes of PKC found in HL-60 cells show a difference in activation by phorbol ester TPA. FEBS Lett. 1989; 249: 264–266.PubMedCrossRefGoogle Scholar
  23. 23.
    Borner C, Ueffing M, Jaken S, Parker PJ, Weistein IB. Two closely related isoforms of Protein kinase C produces recipro115 cal effects on the growth of rat fibroblasts. J Biol Chem 1995; 270: 78–86.PubMedCrossRefGoogle Scholar
  24. 24.
    Ono Y, Fujii T, Ogita K, Kikawa U, Igaroshi K, Nizhizuka Y. Protein kinase C μ form rat brain: Its structure, expression and properties. Proc Natl Acad Sci (USA) 1988; 86: 3099–3103.CrossRefGoogle Scholar
  25. 25.
    Yoshitaka O, Tomoko F, Kouji O, Ushio K, Koichi I, Nishizuka Y. Protein kinase C μ subspecies from rat brain: Its structure, expression and properties. Proc Natl Acad Sci (USA) 1989; 86: 3099–3103.CrossRefGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1997

Authors and Affiliations

  • Edna E. Aquino-Piñero
    • 1
  • Nuri Rodríguez-del Valle
    • 1
  1. 1.Department of Microbiology and Medical Zoology, Medical Sciences CampusUniversity of Puerto RicoPuerto Rico

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