Stress Proteins (Heat Shock Proteins). Its function and relation to diseases.:Its function and relation to diseases

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All organisms respond to stress conditions by transiently accelerating the synthesis of the so-called heat shock or stress proteins. These proteins have been highly conserved across evolution and shown to be expressed not only in the stress conditions but also constitutively. Stress proteins have essential roles in the synthesis, transport, and folding of proteins and are often referred to as molecular chaperones.<BR>Abnormal expression of stress proteins has been widely observed in a number of disease states. Many members of the stress protein family are highly immunogenic. Lymphocytes reactive to stress proteins have been shown to play a role in the pathogenesis of several experimental autoimmune diseases.γδT cells which respond specifically to 65kD stress protein are isolated from rheumatoid arthritis patients. Several mutant, but not wild-type, p53 proteins form complexes with stress proteins. Such complexes are stable and intracellular levels of p53 proteins are frequently elevated in transformed cells. Several reports suggest that stress proteins act as tumor rejection antigens.<BR>Stress proteins are induced in epidermal keratinocytes by heat shock, and other external stimuli. Ultraviolet irradiation is recognized as one of the inducers, but several studies indicated that the mechanism of induction differs from that of heat shock treatment.
日本皮膚科学会大阪地方会の論文