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Influence of cleansing on stratum corneum tryptic enzyme in human skin
Authors:Schepky A G  Holtzmann U  Siegner R  Zirpins S  Schmucker R  Wenck H  Wittern K P  Biel S S
Affiliation:R&D Beiersdorf AG, Unnastrasse 48, D-20245 Hamburg, Germany
Abstract:Desquamation in human skin is a well-balanced process of de novo production of corneocytes and their shedding from the skin surface. The proteolysis of corneodesmosomes is an important step in the final desquamation process. In the degradation of these adhesion molecules, the stratum corneum tryptic enzyme (SCTE) plays a key role. In initial studies with extracts of porcine epidermis, SCTE was shown to be inactivated by low concentrations of sodium lauryl ether sulphate (SLES). These in vitro findings were supported by in situ results obtained by measuring the release of fluorescent dyes coupled to trypsin-specific substrates incubated on human skin cross-sections. Moreover, in further studies, it could be demonstrated that the SCTE activity in the human horny layer decreases after in vivo application of cleansing products containing SLES. After repeated washing of human volunteers with tap water, a standard market cleansing product (SLES/betaine system) or a new improved cleansing product (SLES/betaine/disodium cocoyl glutamate system), the specific SCTE activity was determined in extracts from the uppermost layers of the stratum corneum. It could be shown that after application of the new formula the remaining SCTE activity was significantly higher than after use of the standard market formula. This ex vivo approach has proven to be very helpful for measuring surfactant effects on human skin enzymes. Using this assay, we developed an improved shower gel formula, which leads to a significantly higher skin enzyme activity after application, compared to a standard market formula.
Keywords:corneocytes  corneodesmosomes  desquamation  disodium cocoyl glutamate  enzyme activity  human skin  fluorescent dyes  sodium lauryl ether sulfate  stratum corneum tryptic enzyme  washing
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