Localization of cathepsin H and its inhibitor in the skin and other stratified epithelia.
The rat-skin-derived cysteine proteinase, so-called BANA-hydrolase, which is capable of hydrolysing benzoylarginine naphthylamide and leucine naphthylamide was shown to be immunologically identical to cathepsin H purified from rat liver. The enzyme was immunocytochemically localized in the basal cell layer of rat epidermis. A natural inhibitor of cathepsin H with a molecular weight of about 13,000 was mainly localized in the keratinizing cell layers and showed only a weak reaction in the basal cells. Thus, cathepsin H appears to be a characteristic feature of the proliferating cell layer, whereas the cysteine-proteinase inhibitor is a characteristic feature of keratinizing cells.
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D056655:Cathepsin H; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003546:Cysteine Endopeptidases; D004848:Epithelium / Q000201:enzymology; D005260:Female; D008099:Liver / Q000201:enzymology; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D012867:Skin / Q000201:enzymology*; D013270:Stomach / Q000201:enzymology; D014621:Vagina / Q000201:enzymology
D002403:Cathepsins; D000626:Aminopeptidases; D003546:Cysteine Endopeptidases; D056655:Cathepsin H; C534128:Ctsh protein, rat