Document Detail

The possible role of dermatophyte cysteine dioxygenase in keratin degradation.
MedLine Citation:
PMID:  23758130     Owner:  NLM     Status:  In-Data-Review    
Abstract Cysteine dioxygenase (CDO, EC is a key enzyme involved in the homeostatic regulation of cysteine level and in production of important oxidized metabolites of cysteine such as pyruvate, sulphite, sulphate, hypotaurine, and taurine in all eukaryotic cells. The intracellular CDO concentration is regulated at both transcriptional and posttranslational levels. In several fungi, CDO plays an important role as a virulence factor involved in morphological transition from yeast to mycelial forms. CDO is crucial for oxidation of cysteine to cysteine sulphinic acid and therefore for sulphite production and secretion. Because sulphite cleaves disulphide bridges as a first unavoidable step in keratinolysis, it is hypothesized that in dermatophytes, CDO is a virulence factor crucial for keratin degradation.
Alena Kasperova; Jiri Kunert; Milan Raska
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Medical mycology : official publication of the International Society for Human and Animal Mycology     Volume:  51     ISSN:  1460-2709     ISO Abbreviation:  Med. Mycol.     Publication Date:  2013 Jul 
Date Detail:
Created Date:  2013-06-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9815835     Medline TA:  Med Mycol     Country:  England    
Other Details:
Languages:  eng     Pagination:  449-54     Citation Subset:  IM    
* Department of Biology, Faculty of Medicine and Dentistry, Palacky University in Olomouc , Olomouc , Czech Republic.
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