Abstract
Abstract Introduction As a result of the high sequence similarity between 60-kDa heat shock proteins (HSP60), found in both prokaryotic and eukaryotic cells, it has been suggested, but never concluded, that anti-HSP60 antibodies could be of importance in the pathology of arthritis diseases explained by a concept named molecular mimicry. In a number of clinical studies, antibodies to both human and bacterial HSP60 have been detected in serum from patients with different inflammatory diseases, but divergent results have been published. Recent progress, however, has increased the specificity in tests used to determine the humoral response to HSP60. In this review, these new findings are compared with old questioning the durability of molecular mimicry as a hypothesis for arthritis pathogenesis. The current literature was examined through a thorough PubMed search using appropriate keywords in relation to anti-HSP60 antibodies and arthritisrelated disease. Main research articles were selected for review. Discussion Recent reports have added new information to the interpretation of the humoral immune response to HSP60. By introducing determination of IgG A role for anti-HSP60 antibodies in arthritis: a critical review
Highlights
As a result of the high sequence similarity between 60-kDa heat shock proteins (HSP60), found in both prokaryotic and eukaryotic cells, it has been suggested, but never concluded, that anti-HSP60 antibodies could be of importance in the pathology of arthritis diseases explained by a concept named molecular mimicry
This suggests a multifunctional role for HSP60 and introduces the concept of moonlighting proteins reviewed in the literature[10]
A large part of HSP60 secretion has been observed from cancer cells, in which alternative forms of HSP60 transcripts are suggested to lead the protein through specific internal cellular membrane structures referred to as the endoplasmic reticulum (ER)-Golgi pathway[13]
Summary
A disease-related role for antibodies against 60-kDa heat shock proteins (anti-HSP60) in arthritis was suggested in 1984 by Lakomek et al.[1]. The group demonstrated by the use of immunofluorescence staining that antibodies from a significant amount of sera from ankylosing spondylitis (AS) patients (39% of 62 patients) did bind antigens present in the puffs generated in polytene chromosomes of Drosophila melanogaster by heat shock These antigens were induced from a specific locus (93D) by heat shock and the proteins were called HSPs2. It was recently revealed that the mouse model of arthritis poorly mimics the human inflammatory disease[7] This critical review will first address HSP60 biology and its interaction with the immune system. It will discuss the literature regarding anti-HSP60 cross-reactivity in human clinical studies, and lastly end up questioning its potential relevance as a bacterial trigger of arthritis
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