Fungi responsible for skin mycoses in Turin (Italy).

There has been a recent increase in the frequency of skin mycoses, coupled with changes in the epidemiology and distribution of the species responsible. Periodic epidemiological analyses of these disease are thus required to ensure their efficacious control. Hair fragments, skin scrapings, specimens from vesicles and blisters and nail parings were seeded on Petri dishes loaded with Sabouraud or Mycosel agar, supplemented with chloramphenicol and with chloramphenicol plus cycloheximide respectively. Parts of each specimen were also mounted in 10% potassium hydroxide for examination under the microscope. Yeasts prevailed over dermatophytes. Microsporum canis was the most frequent dermatophyte, followed by Trichophyton rubrum, T. mentagrophytes and Epidermophyton floccosum. Tinea corporis was the most common mycosis, followed by tinea unguis, tinea capitis and tinea pedis. Men were chiefly bearers of tinea cruris and tinea pedis, women of tinea corporis, and children and teenagers of tinea capitis. Some examples of the transmission of infection through interhuman contact, via animals and from the soil are also presented.

Isolation of a novel beta4 integrin-binding protein (p27(BBP)) highly expressed in epithelial cells.

The integrin beta4 has a long cytodomain necessary for hemidesmosome formation. A yeast two-hybrid screen using beta4 cytodomain uncovered a protein called p27(BBP) that represents a beta4 interactor. Both in yeast and in vitro, p27(BBP) binds the two NH2-terminal fibronectin type III modules of beta4, a region required for signaling and hemidesmosome formation. Sequence analysis of p27(BBP) revealed that p27(BBP) was not previously known and has no homology with any isolated mammalian protein, but 85% identical to a yeast gene product of unknown function. Expression studies by Northern analysis and in situ hybridization showed that, in vivo, p27(BBP) mRNA is highly expressed in epithelia and proliferating embryonic epithelial cells. An antibody raised against p27(BBP) COOH-terminal domain showed that all beta4-containing epithelial cell lines expressed p27(BBP). The p27(BBP) protein is insoluble and present in the intermediate filament pool. Furthermore, subcellular fractionation indicated the presence of p27(BBP) both in the cytoplasm and in the nucleus. Confocal analysis of cultured cells showed that part of p27(BBP) immunoreactivity was both nuclear and in the membrane closely apposed to beta4. These results suggest that the p27(BBP) is an in vivo interactor of beta4, possibly linking beta4 to the intermediate filament cytoskeleton.