EVIDENCE FOR A ROLE OF CORNEODESMOSIN, A PROTEIN WHICH MAY SERVE TO MODIFY DESMOSOMES DURING CORNIFICATION, IN STRATUM-CORNEUM CELL COHESION AND DESQUAMATION

Corneodesmosin, defined as the protein recognized by the monoclonal antibody G36-19, is a recently described late differentiation protein of human cornified epithelium. In the stratum corneum it is localized in the extracellular parts of modified desmosomes (corneodesmosomes) and adjacent parts of the cornified cell envelope. The aim of the present study was to investigate whether corneodesmosin undergoes changes in the stratum corneum which can be related to the cohesive state of the tissue and to desquamation. Extracts of plantar stratum corneum from various tissue levels and tape-stripped non-palmoplantar stratum corneum were analysed by immunoblotting with G36-19. In addition, the fate of corneodesmosin during shedding of surface cells in a recently described in vitro model of desquamation in plantar stratum corneum was investigated and compared with the degradation of the desmosomal protein desmoglein I in this system. The apparent molecular weights of the major G36-19-positive components in plantar stratum corneum ranged between 33 and 48 kDa. The components with the highest molecular weights were predominant in the deepest tissue layers. In the intermediate tissue layers G36-19-positive components of molecular weight 33-36, 39 and 44-48 kDa were found. There seemed to be a further degradation of the 33 to 36-kDa components in the most superficial parts of the tissue. In surface cells dissociated in vivo as well as in vitro no G36-19-positive components with molecular weights above 36 kDa were detected. Results from analyses of nonpalmoplantar stratum corneum suggested that corneodesmosin is degraded in this tissue in a way that may be similar to that in plantar stratum corneum. In the in vitro system, EDTA caused a marked stimulation of the further degradation of the 33 to 36-kDa G36-19-positive components, but appeared not to affect the degradation of desmoglein I. The results are compatible with a role of corneodesmosin in stratum corneum cell cohesion. The degradation of this protein may be one of the biochemical changes in the stratum corneum which ultimately leads to desquamation.