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KMID : 0371919880010010161
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Journal of Wonju College of Medicine
1988 Volume.1 No. 1 p.161 ~ p.169
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Inhibitors Against Purified Keratinolytic Proteinase from Microsporum canis and Substrte Specificity
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Abstract
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Dermatophytes are parasitic fungi which cause superficial infections called dermatophytosis in humans and animals. They usually invade and thrive only on the keratinized layers of the skin, nail and hair. The hydrolysis of keratin by fungal kerationolytic proteinases (KPase) is an important factor in pathogenesis. Recently, KPase were isolated and purified from different dermatophytes. These enzymes may play a prominant role not only in the penetration of keratin layers and multiplication of dermatophytes, but also in the hypersensitive reactions associated with dermatophytosis.
Microsporum canis (M. canis), a zoophilic dermatophyte, is frequently transmitted by pets such as cats and dogs to man or through animal contact in rural areas. with the recent world-wide increase in the incidence of M. canis infection, it is now considered to be an important public health problem in view of its epidemiologic aspects.
In the present study, a KPase was isolated and purified from M. canis cluture filltrates by ionexchange chromatography and gel filtration and the effect of various inhibitors against KPase activity was investigated. To determine its substrate specificity, a variety of substrates for KPase including human stratum corneum, human scalp hair, and human nail were tested. SDS-polyacrylamide gel electrophoresis was used to determine the degradation of stratum corneum components by KPase. The results are summarized as follows:
1. PMSF (phenylmethylsulfonylfluoride) inhibited the KPase activity in a dose-dependent manner: however, none of the other group specific inhibitors tested showed any effect against the KPase activity.
2. Among the various substrates for proteinases, KPase digested ovalbumin and bovine hemoglobin and also digested much more human scalp hair than human stratum corneum and human nail.
3. α-Fibrous protein prepared from human stratum corneum of soles was susceptible to degradation by KPase. On the SDS-poly acrylamide gel electrophoresis patterns, staining of main bands of α-fibrous protein appreared weakly, while few new low molecular weight bands appeared.
This study suggests that KPase from M. canis may be a kind of serine proteinase and may play an important role in tinea capitis by affecting the human hair.
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