Lundström A, Egelrud T
DOI: 10.2340/0001555571471474

A chymotrypsin-like proteinase that may be involved in the desquamation process in plantar stratum corneum has recently been partially characterized. The aim of the present study was to elucidate whether a similar proteinase is also present in non-palmo-plantar stratum corneum. Stratum corneum was obtained by tape stripping of volar forearm skin after the skin surface had been painted with colourless nail varnish. The adherent tissue was released from the tape strips by acetone treatment, then extracted with diethyl ether and dried. Extracts of this acetone-ether powder were analyzed with respect to proteolytic activity by means of electrophoresis under non-reducing conditions in polyacrylamide gels containing sodium dodecyl sulphate and casein. The extracts were found to contain one major chymotrypsin-like proteinase with an apparent molecular weight of around 25 kDa, and several minor proteinases with trypsin-like activity. The 25 kDa proteinase was active at pH 5.5-8, and could be inhibited by aprotinin, chymostatin and zinc ion, but not by leupeptin. No difference could be found between the 25 kDa enzyme in forearm stratum corneum and the recently described chymotrypsin-like enzyme in dissociated plantar stratum corneum cells as regards electrophoretic mobility, pH dependency, and inhibitor profile. The fact that the enzyme could degrade casein at pH 5.5 and that it appears to be present in stratum corneum in general suggests that it may play a role in the desquamation process under in vivo conditions. The tentative name "stratum corneum chymotryptic enzyme" is proposed for this newly discovered proteinase.