Méhul Bruno, Bernard Dominique, Brouard Michel, Delattre Caroline, Schmidt Rainer
Galderma R&D, Biot, France.
Exp Dermatol. 2006 Jun;15(6):469-77. doi: 10.1111/j.1600-0625.2006.00433.x.
The calmodulin-like skin protein (CLSP) or so-called calmodulin-like protein 5, a recently discovered skin-specific calcium-binding protein, is closely related to keratinocyte differentiation. The 16-kDa protein is proteolytically degraded in the upper layers of the stratum corneum (SC) of healthy skin. With the use of specific new monoclonal antibodies to CLSP, we were able to demonstrate that the abnormal elevated levels of CLSP, characteristic of psoriatic epidermis, were probably not due to an overexpression of the protein, but most likely the result of its non-degradation. Further in vitro experiments using recombinant CLSP and in situ data clearly showed that calcium protected and chelator accelerated CLSP degradation. These data indicate that CLSP degradation in the SC of psoriatic skin might be hindered by the abnormally elevated calcium concentration. No degradation of CLSP in psoriatic epidermis keeping its ability to bind protein as transglutaminase 3 may have a physiological role in skin diseases such as psoriasis.
