期刊
AUTOIMMUNITY REVIEWS
卷 8, 期 5, 页码 388-393出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.autrev.2008.12.004
关键词
Autoimmunity; Heat-shock proteins; Immunomodulation; Inflammation; Molecular mimicry; Stress proteins
类别
资金
- National Institutes of Health
- Arthritis Foundation (National Office and the Maryland Chapter)
Heat-shock proteins (Hsps) are among the most highly conserved and immunogenic proteins shared by microbial agents and mammals. Under physiological conditions, the ubiquitously distributed Hsps maintain the integrity and function of other cellular proteins when cells are exposed to stressful stimuli. However, owing to their conserved nature and stress inducibility, Hsps may become targets of immune response. The T cells and/or antibodies induced by a microbial lisp may crossreact with the corresponding mammalian lisp (molecular mimicry) and trigger an autoimmune response, which if unchecked can lead to immune pathology and clinical manifestations. Furthermore, enhanced expression of Hsp under stress can unveil previously hidden antigenic determinants that can initiate and perpetuate autoimmune reactivity. Also, the innate immune mechanisms activated by an lisp can reinforce and even direct the type of adaptive immune response to that protein. Hsps have been implicated in the induction and propagation of autoimmunity in several diseases, including rheumatoid arthritis, atherosclerosis and type 1 diabetes. However, Hsps possess immunoregulatory attributes as well and therefore, are being exploited for immunomodulation of various immune-mediated disorders. (C) 2008 Elsevier B.V. All rights reserved.
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