Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?

Abstract

Heat shock proteins (Hsps) can be found in two forms, intracellular and extracellular. The intracellular Hsps are induced as a result of stress and have been found to be cytoprotective in many instances due to their chaperone functions in protein folding and in protein degradation. The origin and role of extracellular Hsps is less clear. Although they were suspected originally to be released from damaged cells (necrosis), their presence in most normal individuals rather suggests that they have regulatory functions in circulation. As immunodominant molecules, Hsps can stimulate the immune system, leading to the production of autoantibodies recognizing epitopes shared by microbial and human Hsps. Thus, extracellular Hsps can influence the inflammatory response as evidenced by the production of inflammatory cytokines. Antibodies to Hsps have been found under normal conditions but seem to be increased in certain stresses and diseases. Such antibodies could regulate the inflammatory response positively or negatively. Here, we review the literature on the findings of antibodies to Hsps in situations of environmental or occupational stress and in a number of diseases and discuss their possible significance for the diagnosis, prognosis, or pathogenesis of these diseases.

The role of Hsp90α in heat-induced apoptosis and cell damage in primary myocardial cell cultures of neonatal rats

“…Heat shock proteins can inhibit or aid the apoptotic mechanism through their chaperone functions by affecting protein folding, ubiquitin degradation pathways, and protein translocation (Takayama et al, 2003). Their most prominent abilities are to protect and repair cells and tissues (Luh et al, 2007), including the myocardial cells, by suppressing apoptosis from the damaging effects of ischemia and reperfusion (Currie et al, 1988;Samali and Orrenius, 1998;Wu and Tanguay, 2006;Seok et al, 2007).…”

Influence of hyperthermal regimes on experimental teratoma development in vitro

“…However, extracellularly localized and membrane‐bound HSPs elicit an immunological response against cancer and are the basis of anticancer vaccines 66. Whether antibodies against HSPs, sometimes found in the organism of cancer or other patients, are “a friend or a foe” is questionable 67. Regardless of this dilemma, our result suggests the benefit of anti‐HSP therapy with the therapeutic hyperthermia of cancer.…”

Peran Heat Shock Protein 47 sebagai Faktor Prediktor PrognosisExperimental Autoimmune Neuritis Studi eksperimental untuk mempelajari perjalanan penyakit Sindrom Guillain Barre menggunakan mencit Mus musculus Balb/C

“…Adanya induksi Hsp47 menyebabkan sel Th0 (T cell helper) berdiferensiasi menjadi sel Th1 dan sel Th2 yang memproduksi sitokin, sitokin pro-inflamasi baik yang dihasilkan oleh Th maupun makrofag menyebabkan semakin memperberat kerusakan mielin. [6][7][8][9][10] Selama ini imunopatogenesis SGB dipelajari melalui experimental autoimmune neuritis (EAN) yang merupakan model pada mencit dari SGB yang mencerminkan SGB pada manusia. 2,[11][12][13] Terjadinya EAN dapat diinduksi dengan myelin protein melalui subkutan.…”

“…Adanya induksi Hsp47 menyebabkan sel Th0 (Tcell helper) berdiferensiasi menjadi sel Th1 dan sel Th2 yang memproduksi sitokin, sitokin pro-inflamasi baik yang dihasilkan oleh Th maupun makrofag menyebabkan semakin memperberat kerusakan mielin. 6,7,8,9,10 Inokulasi myelin protein pada mencit pada penelitian kami menyebabkan peningkatan ekspresi Hsp47. Jika pengaruh Hsp47 pada sel T helper lebih ke arah sitokin inflamasi akan terjadi EAN berat apabila pengaruh pada sitokin anti-inflamasi maka, kerusakan mielin lebih ringan yang menyebabkan EAN ringan.…”