Expressions Of Heat Shock Protein 60 And Heat Shock Protein 70 In Lichen Planus

Heat shock proteins (HSP), also called stress proteins, are expressed by most living cells and are among the most conserved proteins known in phylogeny with respect to both structure and function. They play fundamental roles in many biological processes. Under normal physiological conditions, HSP are expressed constitutively at low levels and play a role in maintaining cell function. Their synthesis increases by a variety of stresses in order to enable cellular survival. When a cell is stressed, there is disassembly of oligomeric complexes and unfolding of polypeptides. Under these circumstances, a proposed role of HSP is to reverse such events, although once refolding becomes impossible, HSP may accelerate the disposal of denatured proteins. Moreover, HSP are also involved in immune responses and HSP even can be recognized by the immune system as predominant antigens during infections and the progression of certain autoimmune diseases. Although it is known that HSP, especially HSP60 and HSP70, are associated with the pathogenesis of many diseases, the role of HSP in the pathogenesis of skin diseases has been studied in only limited skin diseases.Lichen planus (LP) is a relatively common papulosquamous dermatosis. But, the aetiology of LP is unknown. The histology of lichen planus is characterized by epidermis basal cell destruction and a band-like histiolymphocytic infiltrate in the superficial dermis. Recent studies have confirmed the T-lymphocytic nature of this infiltrate and suggest that T...