N-Acetyl-d-Glucosamine Induces Germination in Candida albicans through a Mechanism Sensitive to Inhibitors of cAMP-Dependent Protein Kinase |
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Authors: | Roc o Castilla, Susana Passeron,Mar a L Cantore |
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Affiliation: | Rocı́o Castilla, Susana Passeron,Marı́a L Cantore, |
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Abstract: | 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. |
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Keywords: | Candida albicans In vivo PKA inhibition Morphogenesis |
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