R. Gandouredwards et al., IMMUNOLOCALIZATION OF LOW-MOLECULAR-WEIGHT STRESS PROTEIN HSP-27 IN NORMAL SKIN AND COMMON CUTANEOUS LESIONS, The American journal of dermatopathology, 16(5), 1994, pp. 504-509
Stress proteins, which are found ubiquitously in mammalian cells, appe
ar to be implicated in the regulation of cell growth and protection fr
om environmental insult. Although we previously demonstrated the expre
ssion of low-molecular-weight stress protein, HSP 27, in cultured kera
tinocytes, HSP 27 has not yet been identified in human skin. Using sta
ndard immunohistochemistry on routinely processed paraffin sections, w
e 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. Se
ctions of actinic keratosis, superficial basal cell carcinoma, seborrh
eic keratosis, and psoriasis also exhibited strong cytoplasmic stainin
g in the suprabasal layers of the epidermis. In contrast, cutaneous sq
uamous cell carcinoma demonstrated only weak cytoplasmic staining thro
ughout the infiltrating tumor. This is of particular interest, since o
ther investigators have reported a loss of HSP 27 expression in oncoge
nically transformed cells that exhibit a tumorigenic phenotype. To our
knowledge, this study provides the first demonstration of HSP 27 expr
ession in human skin.