Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid
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...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Kwak, Min-Kyu [verfasserIn] |
|---|
| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
|---|
| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 589(2015), 15, Seite 1863-1871 |
|---|---|
| Übergeordnetes Werk: |
volume:589 ; year:2015 ; number:15 ; pages:1863-1871 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.febslet.2015.04.050 |
|---|
| Katalog-ID: |
OLC1965547818 |
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| 245 | 1 | 0 | |a Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid |
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| 520 | |a 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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. | ||
| 540 | |a Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies | ||
| 540 | |a Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | ||
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| 650 | 4 | |a erythroascorbate peroxidase | |
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| 650 | 4 | |a Ascorbate Peroxidases - genetics | |
| 650 | 4 | |a Glutathione - metabolism | |
| 650 | 4 | |a Ascorbate Peroxidases - metabolism | |
| 650 | 4 | |a Candida albicans - growth & development | |
| 650 | 4 | |a Ascorbic Acid - metabolism | |
| 650 | 4 | |a Candida albicans - pathogenicity | |
| 650 | 4 | |a Ascorbate Peroxidases - chemistry | |
| 650 | 4 | |a Candida albicans - enzymology | |
| 650 | 4 | |a Reactive Oxygen Species - metabolism | |
| 650 | 4 | |a Pyruvaldehyde - metabolism | |
| 700 | 1 | |a Song, Sung-Hyun |4 oth | |
| 700 | 1 | |a Ku, MyungHee |4 oth | |
| 700 | 1 | |a Kang, Sa-Ouk |4 oth | |
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| 856 | 4 | 2 | |u http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract |
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10.1016/j.febslet.2015.04.050 doi PQ20160617 (DE-627)OLC1965547818 (DE-599)GBVOLC1965547818 (PRQ)p1777-d3b6820210f266a0fb7d266c4acf52329547a615dfdf59bd3533066437ed13660 (KEY)0045922420150000589001501863candidaalbicanserythroascorbateperoxidaseregulates DE-627 ger DE-627 rakwb eng 570 530 610 DNB Kwak, Min-Kyu verfasserin aut Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. erythroascorbic acid methylglyoxal PAGE ROS EASC reactive oxygen species GSH glutathione peroxidase Candida albicans KatG EAPX1 open reading frame rpm ORF CCP1 catalase peroxidase revolutions per minute cytochrome erythroascorbate peroxidase polyacrylamide gel electrophoresis Ascorbate Peroxidases - genetics Glutathione - metabolism Ascorbate Peroxidases - metabolism Candida albicans - growth & development Ascorbic Acid - metabolism Candida albicans - pathogenicity Ascorbate Peroxidases - chemistry Candida albicans - enzymology Reactive Oxygen Species - metabolism Pyruvaldehyde - metabolism Song, Sung-Hyun oth Ku, MyungHee oth Kang, Sa-Ouk oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 15, Seite 1863-1871 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:15 pages:1863-1871 http://dx.doi.org/10.1016/j.febslet.2015.04.050 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract http://www.ncbi.nlm.nih.gov/pubmed/25957768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 15 1863-1871 |
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10.1016/j.febslet.2015.04.050 doi PQ20160617 (DE-627)OLC1965547818 (DE-599)GBVOLC1965547818 (PRQ)p1777-d3b6820210f266a0fb7d266c4acf52329547a615dfdf59bd3533066437ed13660 (KEY)0045922420150000589001501863candidaalbicanserythroascorbateperoxidaseregulates DE-627 ger DE-627 rakwb eng 570 530 610 DNB Kwak, Min-Kyu verfasserin aut Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. erythroascorbic acid methylglyoxal PAGE ROS EASC reactive oxygen species GSH glutathione peroxidase Candida albicans KatG EAPX1 open reading frame rpm ORF CCP1 catalase peroxidase revolutions per minute cytochrome erythroascorbate peroxidase polyacrylamide gel electrophoresis Ascorbate Peroxidases - genetics Glutathione - metabolism Ascorbate Peroxidases - metabolism Candida albicans - growth & development Ascorbic Acid - metabolism Candida albicans - pathogenicity Ascorbate Peroxidases - chemistry Candida albicans - enzymology Reactive Oxygen Species - metabolism Pyruvaldehyde - metabolism Song, Sung-Hyun oth Ku, MyungHee oth Kang, Sa-Ouk oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 15, Seite 1863-1871 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:15 pages:1863-1871 http://dx.doi.org/10.1016/j.febslet.2015.04.050 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract http://www.ncbi.nlm.nih.gov/pubmed/25957768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 15 1863-1871 |
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10.1016/j.febslet.2015.04.050 doi PQ20160617 (DE-627)OLC1965547818 (DE-599)GBVOLC1965547818 (PRQ)p1777-d3b6820210f266a0fb7d266c4acf52329547a615dfdf59bd3533066437ed13660 (KEY)0045922420150000589001501863candidaalbicanserythroascorbateperoxidaseregulates DE-627 ger DE-627 rakwb eng 570 530 610 DNB Kwak, Min-Kyu verfasserin aut Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. erythroascorbic acid methylglyoxal PAGE ROS EASC reactive oxygen species GSH glutathione peroxidase Candida albicans KatG EAPX1 open reading frame rpm ORF CCP1 catalase peroxidase revolutions per minute cytochrome erythroascorbate peroxidase polyacrylamide gel electrophoresis Ascorbate Peroxidases - genetics Glutathione - metabolism Ascorbate Peroxidases - metabolism Candida albicans - growth & development Ascorbic Acid - metabolism Candida albicans - pathogenicity Ascorbate Peroxidases - chemistry Candida albicans - enzymology Reactive Oxygen Species - metabolism Pyruvaldehyde - metabolism Song, Sung-Hyun oth Ku, MyungHee oth Kang, Sa-Ouk oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 15, Seite 1863-1871 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:15 pages:1863-1871 http://dx.doi.org/10.1016/j.febslet.2015.04.050 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract http://www.ncbi.nlm.nih.gov/pubmed/25957768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 15 1863-1871 |
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10.1016/j.febslet.2015.04.050 doi PQ20160617 (DE-627)OLC1965547818 (DE-599)GBVOLC1965547818 (PRQ)p1777-d3b6820210f266a0fb7d266c4acf52329547a615dfdf59bd3533066437ed13660 (KEY)0045922420150000589001501863candidaalbicanserythroascorbateperoxidaseregulates DE-627 ger DE-627 rakwb eng 570 530 610 DNB Kwak, Min-Kyu verfasserin aut Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. erythroascorbic acid methylglyoxal PAGE ROS EASC reactive oxygen species GSH glutathione peroxidase Candida albicans KatG EAPX1 open reading frame rpm ORF CCP1 catalase peroxidase revolutions per minute cytochrome erythroascorbate peroxidase polyacrylamide gel electrophoresis Ascorbate Peroxidases - genetics Glutathione - metabolism Ascorbate Peroxidases - metabolism Candida albicans - growth & development Ascorbic Acid - metabolism Candida albicans - pathogenicity Ascorbate Peroxidases - chemistry Candida albicans - enzymology Reactive Oxygen Species - metabolism Pyruvaldehyde - metabolism Song, Sung-Hyun oth Ku, MyungHee oth Kang, Sa-Ouk oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 15, Seite 1863-1871 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:15 pages:1863-1871 http://dx.doi.org/10.1016/j.febslet.2015.04.050 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract http://www.ncbi.nlm.nih.gov/pubmed/25957768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 15 1863-1871 |
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10.1016/j.febslet.2015.04.050 doi PQ20160617 (DE-627)OLC1965547818 (DE-599)GBVOLC1965547818 (PRQ)p1777-d3b6820210f266a0fb7d266c4acf52329547a615dfdf59bd3533066437ed13660 (KEY)0045922420150000589001501863candidaalbicanserythroascorbateperoxidaseregulates DE-627 ger DE-627 rakwb eng 570 530 610 DNB Kwak, Min-Kyu verfasserin aut Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. erythroascorbic acid methylglyoxal PAGE ROS EASC reactive oxygen species GSH glutathione peroxidase Candida albicans KatG EAPX1 open reading frame rpm ORF CCP1 catalase peroxidase revolutions per minute cytochrome erythroascorbate peroxidase polyacrylamide gel electrophoresis Ascorbate Peroxidases - genetics Glutathione - metabolism Ascorbate Peroxidases - metabolism Candida albicans - growth & development Ascorbic Acid - metabolism Candida albicans - pathogenicity Ascorbate Peroxidases - chemistry Candida albicans - enzymology Reactive Oxygen Species - metabolism Pyruvaldehyde - metabolism Song, Sung-Hyun oth Ku, MyungHee oth Kang, Sa-Ouk oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 15, Seite 1863-1871 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:15 pages:1863-1871 http://dx.doi.org/10.1016/j.febslet.2015.04.050 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract http://www.ncbi.nlm.nih.gov/pubmed/25957768 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 15 1863-1871 |
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Kwak, Min-Kyu ddc 570 misc erythroascorbic acid misc methylglyoxal misc PAGE misc ROS misc EASC misc reactive oxygen species misc GSH misc glutathione misc peroxidase misc Candida albicans misc KatG misc EAPX1 misc open reading frame misc rpm misc ORF misc CCP1 misc catalase peroxidase misc revolutions per minute misc cytochrome misc erythroascorbate peroxidase misc polyacrylamide gel electrophoresis misc Ascorbate Peroxidases - genetics misc Glutathione - metabolism misc Ascorbate Peroxidases - metabolism misc Candida albicans - growth & development misc Ascorbic Acid - metabolism misc Candida albicans - pathogenicity misc Ascorbate Peroxidases - chemistry misc Candida albicans - enzymology misc Reactive Oxygen Species - metabolism misc Pyruvaldehyde - metabolism Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid |
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570 530 610 DNB Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid erythroascorbic acid methylglyoxal PAGE ROS EASC reactive oxygen species GSH glutathione peroxidase Candida albicans KatG EAPX1 open reading frame rpm ORF CCP1 catalase peroxidase revolutions per minute cytochrome erythroascorbate peroxidase polyacrylamide gel electrophoresis Ascorbate Peroxidases - genetics Glutathione - metabolism Ascorbate Peroxidases - metabolism Candida albicans - growth & development Ascorbic Acid - metabolism Candida albicans - pathogenicity Ascorbate Peroxidases - chemistry Candida albicans - enzymology Reactive Oxygen Species - metabolism Pyruvaldehyde - metabolism |
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ddc 570 misc erythroascorbic acid misc methylglyoxal misc PAGE misc ROS misc EASC misc reactive oxygen species misc GSH misc glutathione misc peroxidase misc Candida albicans misc KatG misc EAPX1 misc open reading frame misc rpm misc ORF misc CCP1 misc catalase peroxidase misc revolutions per minute misc cytochrome misc erythroascorbate peroxidase misc polyacrylamide gel electrophoresis misc Ascorbate Peroxidases - genetics misc Glutathione - metabolism misc Ascorbate Peroxidases - metabolism misc Candida albicans - growth & development misc Ascorbic Acid - metabolism misc Candida albicans - pathogenicity misc Ascorbate Peroxidases - chemistry misc Candida albicans - enzymology misc Reactive Oxygen Species - metabolism misc Pyruvaldehyde - metabolism |
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candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid |
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Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid |
| abstract |
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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. |
| abstractGer |
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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. |
| abstract_unstemmed |
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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence. |
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| title_short |
Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of d‐erythroascorbic acid |
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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. Erythroascorbate peroxidase (EAPX1) regulates respiration via erythroascorbic acid (EASC). EAPX1 deficiency accumulates methylglyoxal and ROS independently of EASC content. EAPX1 deficiency strongly induces plant‐like homologue peroxidases in budding yeast. EAPX1 is involved in hyphal formation independently of plant‐like homologue peroxidases. EAPX1 is necessary for Candida albicans hyphal growth and full virulence.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">erythroascorbic acid</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">methylglyoxal</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">PAGE</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">ROS</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">EASC</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">reactive oxygen species</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">GSH</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">glutathione</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">peroxidase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Candida albicans</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">KatG</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">EAPX1</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">open reading frame</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">rpm</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">ORF</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">CCP1</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">catalase peroxidase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">revolutions per minute</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">cytochrome</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">erythroascorbate peroxidase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">polyacrylamide gel electrophoresis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Ascorbate Peroxidases - 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metabolism</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Song, Sung-Hyun</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ku, MyungHee</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kang, Sa-Ouk</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">FEBS letters</subfield><subfield code="d">Amsterdam [u.a.] : Elsevier, 1968</subfield><subfield code="g">589(2015), 15, Seite 1863-1871</subfield><subfield code="w">(DE-627)129522023</subfield><subfield code="w">(DE-600)212746-5</subfield><subfield code="w">(DE-576)014938014</subfield><subfield code="x">0014-5793</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:589</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:15</subfield><subfield code="g">pages:1863-1871</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1016/j.febslet.2015.04.050</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.04.050/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/25957768</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_21</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_211</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">589</subfield><subfield code="j">2015</subfield><subfield code="e">15</subfield><subfield code="h">1863-1871</subfield></datafield></record></collection>
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