Investigation of the epidermal proteins related with skin barrier function

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A phosphorylated cystatin alpha (P-cystatin alpha), which was a cysteine proteinase inhibitor isolated from newborn rat epidermis, located in keratohyalin granules in the stratum granulosum and the cornified envelope of the stratum corneum. This location suggested that P-cystatin alpha could have barrier function on the skin surface. We repoted that P-cystatin alpha inhibited a cysteine proteinase activity from Staphylococcus aureus V8 and a growth of the bacteria. In this experiment, the inhibitoty properties of P-cystatin alpha and its crosslinked protein with filaggrin linker segment peptide by epidermal transglutaminase (P-cystatin alpha-FLSP) against polio virus were investigated. P-cystatin alpha and P-cystatin alpha-FLSP inhibitied the growth of polio virus and the production of cysteine proteinase from the virus.The antibody against human bactericidal permeability increasing protein reacted positively with the cytoplasm of the inner root sheath by immunohistochemical study and the 55 kDa protein in immunoblotting analysis. The antibody against lactoferricin B reacted with the cytoplasm of the stratum granulosum and the 40 kDa protein. The two proteins inhibited the growth of some bacteria, therefore, the proteins having similar properties of these proteins could exist in the skin and relate with an epidermal barrier function.