title: Water modulation of stratum corneum chymotryptic enzyme activity and desquamation.
abstract: Exposure to a dry environment leads to depletion of water from the peripheral stratum corneum layers in a process dependent on the relative humidity (RH) and the intrinsic properties of the tissue. We hypothesized that by modulating the water content of the stratum corneum in the surface layers, RH effects the rate of desquamation by modulating the activity of the desquamatory enzymes, and specifically stratum corneum chymotryptic enzyme (SCCE). Using a novel air interface in vitro desquamatory model, we demonstrated RH-dependent corneocyte release with desquamatory rates decreasing below 80% RH. Application of 10% glycerol or a glycerol-containing moisturizing lotion further increased desquamation, even in humid conditions, demonstrating that water was the rate-limiting factor in the final stages of desquamation. Furthermore, even in humid conditions desquamation was sub-maximal. In situ stratum corneum SCCE activity showed a dependence on RH: activity was significantly higher at 100% than at 44% RH. Further increases in SCCE activity were induced by applying a 10% glycerol solution. Since SCCE, a water-requiring enzyme, must function in the water-depleted outer stratum corneum, we sought to determine whether this enzyme has a tolerance to lowered water activity. Using concentrated sucrose solutions to lower water activity, we analysed the activity of recombinant SCCE and compared it to that of trypsin and chymotrypsin. SCCE activity demonstrated a tolerance to water restriction, and this may be an adaptation to maintain enzyme activity even within the water-depleted stratum corneum intercellular space. Overall these findings support the concept that in the upper stratum corneum, RH modulates desquamation by its effect upon SCCE activity, and possibly other desquamatory hydrolases. In addition, SCCE may be adapted to function in the water-restricted stratum corneum intercellular space.
authors.affiliation: Skin & Hair Biology, Unilever Research, Sharnbrook, Bedford, UK. Allan.Watkinson@Unilever.com
authors.forename: A
authors.initials: A
authors.lastname: Watkinson
authors.forename: C
authors.initials: C
authors.lastname: Harding
authors.forename: A
authors.initials: A
authors.lastname: Moore
authors.forename: P
authors.initials: P
authors.lastname: Coan
mesh_terms: D000818:Animals; D006813:Humidity; D066298:In Vitro Techniques; D007610:Kallikreins; D012697:Serine Endopeptidases / Q000378:metabolism*; D012867:Skin / Q000187:drug effects* / Q000201:enzymology*; D012879:Skin Physiological Phenomena / Q000187:drug effects*; D013552:Swine; D014867:Water / Q000494:pharmacology*
chemical_list: D014867:Water; C082472:KLK7 protein, human; D007610:Kallikreins; D012697:Serine Endopeptidases