Heat shock proteins and molecular chaperones: Implications for adaptive responses in the skin

Abstract

Recent advances in the biology of heat-shock proteins (hsps) are reviewed. These abundant and evolutionarily highly conserved proteins (also called stress proteins) act as molecular escorts. Hsps bind to other cellular proteins, help them to fold into their correct secondary structures, and prevent misfolding and aggregation during stress. Cytoplasmic hsp70 and hsp60 participate in complicated protein-folding pathways during the synthesis of new polypeptides. Close relatives of hsp70 and hsp60 assist in the transport and assembly of proteins inside intracellular organelles. Hsp90 may have a unique role, binding to the glucocorticoid receptor in a manner essential for proper steroid hormone action. Hsps may also be essential for thermotolerance and for prevention and repair of damage caused by ultraviolet B light. A unique class of T lymphocytes, the γδ T cells, exhibits a restricted specificity against hsps. These T cells may constitute a general, nonspecific immune mechanism directed against the hsps within invading organisms or against very similar hsps expressed by infected (stressed) keratinocytes. Immunologic cross-reactivity between hsps of foreign organisms and of the host may play a role in some autoimmune diseases. Although hsps are expressed in the skin, many questions remain about their role during injury, infection, and other types of cutaneous pathophysiology.