30-kDa trypsin-like proteases in the plantar stratum corneum.
The casein digestible proteases in human plantar stratum corneum were determined to be about 75-kDa, 30-kDa and 25-kDa in molecular weight by zymography. The enzymatic activity of the 75-kDa and 25-kDa proteases was specifically inhibited by chymostatin, which is an inhibitor of chymotrypsin-like serine proteases, and the proteases around 30-kDa were inhibited by leupeptin, a trypsin-like serine protease inhibitor. The enzymatic activity of all these proteases was inhibited by aprotinin. The 30-kDa trypsin-like proteases were heat-stable; their enzymatic activity still remained even after heating at 100 degrees C for 60 minutes. Their optimal pH was around 9, and the activity was higher in the outer part of the stratum corneum than in the inner part.
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Department of Dermatology, Kinki University School of Medicine, Osaka, Japan.
Takahashi
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Tezuka
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D007611:Aprotinin / Q000494:pharmacology; D046508:Culture Techniques; D004817:Epidermis / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D012697:Serine Endopeptidases / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D014357:Trypsin / Q000032:analysis / Q000187:drug effects / Q000378:metabolism
D015842:Serine Proteinase Inhibitors; D007611:Aprotinin; D012697:Serine Endopeptidases; D014357:Trypsin