Interaction of Candida Species with the Skin

The human skin is commonly colonized by diverse fungal species. Some Candida species, especially C. albicans, do not only reside on the skin surface as commensals, but also cause infections by growing into the colonized tissue. However, defense mechanisms at the skin barrier level are very efficient, involving residential non-immune and immune cells as well as immune cells specifically recruited to the site of infection. Therefore, the skin is an effective barrier against fungal infection. While most studies about commensal and pathogenic interaction of Candida species with host epithelia focus on the interaction with mucosal surfaces such as the vaginal and gastrointestinal epithelia, less is known about the mechanisms underlying Candida interaction with the skin. In this review, we focus on the ecology and molecular pathogenesis of Candida species on the skin and give an overview of defense mechanisms against C. albicans in this context. We also discuss new research avenues in dermal infection, including the involvement of neurons, fibroblasts, and commensal bacteria in both mouse and human model systems

Studies of membrane bound selenoproteins involved in redox processes and antioxidant system

Selenium is an essential element, present in the mammalian organism at relatively low concentration. Selenium is very unevenly distributed among the tissues of the rat. Investigations were performed on rats to obtain information on the distribution of selenoproteins in subcellular organelles, especially in the microsomal and endoplasmatic reticulum fraction of the kidney. The membrane bound selenium containing proteins were detected by labeling of rats with 75Se selenite, subcellular fractionation of the tissue homogenates, separation of the proteins by chromatography, electrophoresis and detection of 75Se proteins by autoradiography. In this way at least seventeen membrane bound selenium containing proteins could be distinguished in the microsomal fraction of the kidney. Of those, eight selenium containing proteins with molecular masses of 15, 16, 20, 23 25, 28, 42 44, 58 60 and 72 75 kDa were localized in the endoplasmatic reticulum. The labeled bands with the molecular masses of 15, 16, 42 44, 58 60 were identified as known selenoproteins. The 75Se labeled bands with the molecular masses of 20, 23 25, and 28 kDa were detected as selenoproteins which are involved in the redox processes. At the current time the 72 kDa protein was only identified as selenium containig protei