N-acetyl-D-glucosamine Induces Germination in Candida Albicans Through a Mechanism Sensitive to Inhibitors of cAMP-dependent Protein Kinase

Cell Signal. 1998 Nov;10(10):713-9. doi: 10.1016/s0898-6568(98)00015-1.


The present study examines the involvement of cAMP-dependent protein kinase (PKA) in the dimorphic transition of Candida albicans by assessing the in vivo effect of two permeable PKA inhibitors on N-acetyl-D-glucosamine (GlcNAc)- and serum-induced differentiation. The permeable myristoylated derivative of the heat-stable PKA inhibitor (MyrPKI), which inhibited C. albicans PKA in vitro, caused a concentration-dependent inhibition of germ-tube formation in cultures induced to germinate by GlcNAc; germination halted irrespective of the time of addition of the inhibitor. MyrPKI also blocked dibutyryl-cAMP (dbcAMP)- and glucagon-stimulated germination but did not affect serum-induced germination. H-89, another highly specific PKA inhibitor, displayed the same effect on germination. Neither MyrPKI nor H-89 had any effect on budding of yeast cells. In conclusion, our results indicate that cAMP-mediated activation of PKA plays a pivotal role in the biochemical mechanism underlying morphogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / pharmacology*
  • Bucladesine / pharmacology
  • Candida albicans / drug effects
  • Candida albicans / physiology*
  • Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Glucagon / pharmacology
  • Isoquinolines / pharmacology
  • Morphogenesis
  • Sulfonamides*


  • Enzyme Inhibitors
  • Isoquinolines
  • Sulfonamides
  • Bucladesine
  • Glucagon
  • Cyclic AMP-Dependent Protein Kinases
  • N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide
  • Acetylglucosamine