No abstract available.
Hyperkeratosis, Epidermolytic*

Radical changes were made last year in the educational program of liberal arts at Juntendo University School of Medicine. The number of required courses was decreased, and students were given more freedom to choose electives. A survey at the end of the first semester evaluating the reforms showed great satisfaction on both sides: students were highly motivated to study, and the teachers were ready to answer their needs.

Recent topics of biochemical and biological progress in keratinization and dyskeratosis were reviewed and discussed. The main topics were as follows: (1) what is keratin (2) Differentiation of keratinocytes (keratinization), (3) Components of horny substances and their derivation, (4) Keratin filament and keratohyaline granule, (5) Synthesis of horny cell membrane (disulfide bonds, e- (T-glutamyl) lysine bonds), (6) Biochernical analysis of dyskeratosis (harlequin fetus, ichthyosis vulgaris, X-linked ichthyosis, lamellar ichthyosis, bullous congenital ichthyosiform erythroderma, psoriasis vulgaris, Dariers disease, M:enke's syndrome, Netherton's disease, Richner-Hanhart syndrome). These findings should lead to a more cornplete understanding of the pathologic events that occur in the process of keratinization and more rational therapy for many disorders in keratinization.
Cell Membrane ; Darier Disease ; Fetus ; Hyperkeratosis, Epidermolytic ; Ichthyosis ; Ichthyosis Vulgaris ; Ichthyosis, Lamellar ; Keratinocytes ; Lysine ; Psoriasis

Candida albicans produced a karatinolytic proteinase (KPase) or C. albicans producing proteinase (CAPP), a proposed new term for this enzyme, and Trichophyton mentagrophytes also produced KPase when cultivated in liquid medium containing human stratum corneum (HSC) as the nitrogen source, but were unable to do so when cultivated in sabouraud dextrose broth. Purified KPase from the culture supernatants of C. albicans had a molecular weight of 42,000 and an optimum pH at 4.0. The KPase was found to belong to the carboxyl proteinases group and its activity was strongly inhibited by pepstatin. Both fungi were able to grow by secreting KPase which digested HSC for nutrients. KPase from both fungi had high activity in each optimum pH, such as weakly acidic pH on C. albicans and neutral pH on T. mentagrophytes to adapt their surrounding environment by changing the environmental pH into their own optimum pH.
Candida albicans/*enzymology/growth & development ; Culture Media ; Endopeptidases/*physiology ; Hydrogen-Ion Concentration ; Molecular Weight ; Trichophyton/*enzymology/growth & development