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Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d ‐erythroascorbic acid
Author(s) -
Kwak Min-Kyu,
Song Sung-Hyun,
Ku MyungHee,
Kang Sa-Ouk
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.04.050
Subject(s) - methylglyoxal , biochemistry , peroxidase , intracellular , reactive oxygen species , catalase , biology , chemistry , enzyme
Candida albicans d ‐erythroascorbate peroxidase (EAPX1), which can catalyze the oxidation of d ‐erythroascorbic acid (EASC) to water, was observed to be inducible in EAPX1 ‐deficient and EAPX1 ‐overexpressing cells via activity staining. EAPX1 ‐deficient cells have remarkably increased intracellular reactive oxygen species and methylglyoxal independent of the intracellular EASC content. The increased methylglyoxal caused EAPX1 ‐deficient cells to activate catalase‐peroxidase and cytochrome c peroxidase, which led to defects in cell growth, viability, mitochondrial respiration, filamentation and virulence. These findings indicate that EAPX1 mediates cell differentiation and virulence by regulating intracellular methylglyoxal along with oxidative stresses, regardless of endogenous EASC biosynthesis or alternative oxidase expression.