Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway.

Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Research Abstract Details 

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Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Abstract Text:

Slavena Vylkova,Woong Sik Jang,Wansheng Li,Namrata Nayyar,Mira Edgerton,Slavena Vylkova,Woong Sik Jang,Wansheng Li,Namrata Nayyar,Mira Edgerton,

Histatin 5 (Hst 5) is a salivary cationic peptide that has toxicity for Candida albicans by inducing rapid cellular ion imbalance and cell volume loss. Microarray analyses of peptide-treated cells were used to evaluate global gene responses elicited by Hst 5. The major transcriptional response of C. albicans to Hst 5 was expression of genes involved in adaptation to osmotic stress, including production of glycerol (RHR2, SKO1, and PDC11) and the general stress response (CTA1 and HSP70). The oxidative-stress genes AHP1, TRX1, and GPX1 were mildly induced by Hst 5. Cell defense against Hst 5 was dependent on the Hog1 mitogen-activated protein kinase (MAPK) pathway, since C. albicans hog1/hog1 mutants were significantly hypersensitive to Hst 5 but not to Mkc1 MAPK or Cek1 MAPK mutants. Activation of the high-osmolarity glycerol (HOG) pathway was demonstrated by phosphorylation of Hog1 MAPK as well as by glycerol production following Hst 5 treatment in a dose-dependent manner. C. albicans cells prestressed with sorbitol were less sensitive to subsequent Hst 5 treatment; however, cells treated concurrently with osmotic stress and Hst 5 were hypersensitive to Hst 5. In contrast, cells subjected to oxidative stress had no difference in sensitivity to Hst 5. These results suggest a common underlying cellular response to osmotic stress and Hst 5. The HOG stress response pathway likely represents a significant and effective challenge to physiological levels of Hst 5 and other toxic peptides in fungal cells.

Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Publishing Authors By Initials

S Vylkova,WS Jang,W Li,N Nayyar,M Edgerton,S Vylkova,WS Jang,W Li,N Nayyar,M Edgerton,

For similar genetic processes: gene expression: transcription, genetic research abstracts see: genetic processes: gene expression: transcription, genetic research

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Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Eukaryotic cell

VOLUME: 6

Page Numbers: 1876-88

Journal Abbreviation: Eukaryotic Cell

ISSN: 1535-9778

DAY: 22

MONTH: 08

YEAR: 2007

Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101130731

Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Keywords Mesh Terms:

KEYWORDS: Transcription, Genetic

MESH TERMS: drug effects

Chemical & Substance for Abstract: Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway. Information

Substance Name: Mitogen-Activated Protein Kinases

Registry Number: EC 2.7.1.37

Grant and Affiliation Information for Histatin 5 initiates osmotic stress response in Candida albicans via activation of the Hog1 mitogen-activated protein kinase pathway.

AFFILIATION: Department of Oral Biology, SUNY at Buffalo Main Street Campus, Buffalo, NY 14214, USA.

Country: United States

AGENCY: United States NIDCR

GRANT: R01 DE010641

ACRONYM: DE

MEDLINETA: Eukaryot Cell

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