Expression of heat shock proteins in a linear rodent wound.

Heat shock proteins (hsps) are ubiquitous and known to be expressed in all organisms. These stress proteins are likely to be induced in the wound environment and may play a critical role in the overall process of wound repair. Linear incisions were made in Sprague-Dawley rats. Serial skin biopsies were taken, the dermis and epidermis were separated and a protein lysate made. The expression of hsp 72, 47, and 32 were analyzed by Western blotting and immunohistochemistry. There were distinct patterns of expression of hsp 72, 47, and 32 in the wound. In unwounded dermis, there was no constitutive expression of any of the heat shock proteins studied. In the epidermis, there was constitutive expression of hsp 32 and 72, but not hsp 47. With wounding, all hsps exhibited increased expression both in the dermis and epidermis. These patterns of protein expression are suggestive of the individual heat shock proteins' molecular function, such as hsp 72's role as an indicator of cellular stress and injury, hsp 47's role in collagen synthesis, and hsp 32's role as an antioxidant.