Malassezin, a novel agonist of the aryl hydrocarbon receptor from the yeast Malassezia furfur, induces apoptosis in primary human melanocytes
Autor: | Peter Mayser, Wolfgang Kummer, August Bernd, Bernhard Irlinger, Wolfgang Steglich, Andrea Bartsch, Hans-Joachim Krämer, Monika Podobinska, Achim Battmann, Wiebke Thoma |
---|---|
Rok vydání: | 2005 |
Předmět: |
Agonist
Indoles medicine.drug_class Human skin Apoptosis Biochemistry Microbiology Depigmentation medicine Humans Receptor Molecular Biology Mycosis Cells Cultured Indole test Malassezia integumentary system biology L-Lactate Dehydrogenase Molecular Structure Organic Chemistry Pityriasis medicine.disease Aryl hydrocarbon receptor Caspase 9 Microscopy Electron Receptors Aryl Hydrocarbon Caspases biology.protein Molecular Medicine Melanocytes Chromatography Thin Layer Comet Assay medicine.symptom |
Zdroj: | Chembiochem : a European journal of chemical biology. 6(5) |
ISSN: | 1439-4227 |
Popis: | Pityriasis versicolor is the most common skin mycosis in humans worldwide. Yeasts of the genus Malassezia, particularly M. furfur, a saprophyte occurring widely on human skin, are generally regarded as the causative agents. Pityriasis versicolor is often accompanied by a long-lasting depigmentation that persists even after successful antimycotic therapy. M. furfur is able to convert tryptophan into a variety of indole alkaloids, some of them showing biological properties that correlate well with certain clinical features of pityriasis versicolor. This suggests a possible role for these compounds in the depigmentation process. We now report that human melanocytes undergo apoptosis when exposed to the crude mixture of tryptophan metabolites from M. furfur. The active compound was identified as malassezin, previously isolated by us from the same source and characterized as an agonist of the aryl hydrocarbon (Ah) receptor. The compound could, therefore, contribute to the marked depigmentation observed during the course of pityriasis versicolor. |
Databáze: | OpenAIRE |
Externí odkaz: |