IMMUNOLOCALIZATION OF LOW-MOLECULAR-WEIGHT STRESS PROTEIN HSP-27 IN NORMAL SKIN AND COMMON CUTANEOUS LESIONS

Stress proteins, which are found ubiquitously in mammalian cells, appear to be implicated in the regulation of cell growth and protection from environmental insult. Although we previously demonstrated the expression of low-molecular-weight stress protein, HSP 27, in cultured keratinocytes, HSP 27 has not yet been identified in human skin. Using standard immunohistochemistry on routinely processed paraffin sections, we examined specimens of common epidermal lesions and normal skin with a monoclonal antibody to HSP 27. Normal skin from the breast, foreskin, and lower extremity demonstrated strong cytoplasmic staining in the suprabasal epidermis. There was no change in the intensity of staining or cellular localization related to age, body location, or gender. Sections of actinic keratosis, superficial basal cell carcinoma, seborrheic keratosis, and psoriasis also exhibited strong cytoplasmic staining in the suprabasal layers of the epidermis. In contrast, cutaneous squamous cell carcinoma demonstrated only weak cytoplasmic staining throughout the infiltrating tumor. This is of particular interest, since other investigators have reported a loss of HSP 27 expression in oncogenically transformed cells that exhibit a tumorigenic phenotype. To our knowledge, this study provides the first demonstration of HSP 27 expression in human skin.