Heat-shock proteins and immunopathology: Regulatory role of heat-shock protein-specific T cells

1991 ◽  
Vol 13 (1) ◽  
pp. 63-80 ◽  
Author(s):  
Kikuo Nomoto ◽  
Yasunobu Yoshikai
Keyword(s):  
T Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Regulatory Role ◽  
Shock Proteins

Molecular Pathways Induced by Tumor–Microenvironment Interactions in Myeloma and the Regulatory Role of Heat-Shock Proteins

2009 ◽  
Vol 9 ◽  
pp. S13-S14
Author(s):  
Constantine S. Mitsiades ◽  
Douglas W. McMillin ◽  
Jake Delmore ◽  
Joseph Negri ◽  
Steffen Klippel ◽  
...  
Keyword(s):  
Heat Shock ◽  
Tumor Microenvironment ◽  
Heat Shock Proteins ◽  
Regulatory Role ◽  
Molecular Pathways ◽  
Shock Proteins

scholarly journals Flagellin Contamination of Recombinant Heat Shock Protein 70 Is Responsible for Its Activity on T Cells

2006 ◽  
Vol 282 (7) ◽  
pp. 4479-4484 ◽  
Author(s):  
Zhiyong Ye ◽  
Yunn-Hwen Gan
Keyword(s):  
Escherichia Coli ◽  
T Cells ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Burkholderia Pseudomallei ◽  
Jurkat T Cells ◽  
Recombinant Hsp70 ◽  
Shock Proteins

Heat shock proteins (Hsp) 60 and 70 have been intensively studied for their ability to activate innate immunity. Heat shock proteins had been shown to induce the activation of dendritic cells, T cells, and B cells. However, the possible contamination of endotoxin in heat shock protein preparations makes their function as an activator of immune system ambiguous. Here, we examined the ability of bacterial Hsp60 and Hsp70 to activate Jurkat T cells and primary T cells. We found that Burkholderia pseudomallei Hsp70 and Mycobacterium tuberculosis Hsp70 could costimulate Jurkat T cells to make IL-2 and signal through TLR5. This costimulatory activity is not due to endotoxin or contaminants signaling via TLR2 nor TLR4. However, recombinant Hsp70 expressed in Escherichia coli ΔfliC strain completely lost its ability to costimulate T cells. Thus, the activation of T cells by recombinant Hsp70 is ascribed to flagellin contamination.

scholarly journals THE ROLE OF THE HEAT SHOCK PROTEIN 70 IN THE PATHOGENESIS OF CARDIOVASCULAR PATHOLOGY

2019 ◽  
Vol 21 (2) ◽  
pp. 201-208
Author(s):  
O. A. Ponasenko ◽  
L. V. Gankovskaya ◽  
O. A. Svitich
Keyword(s):  
Innate Immunity ◽  
Cardiovascular Diseases ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Arterial Hypertension ◽  
Heat Shock Protein 70 ◽  
Cardiovascular Pathology ◽  
Shock Proteins

The problem of studying cardiovascular diseases (CVD) for a long time remains extremely important, and, therefore, there are many works that offer new ways to diagnose and treat this group of diseases. Great opportunities are provided by the study of molecular interactions for a more accurate understanding of the pathogenesis of cardiovascular pathology. Many studies have recently been devoted to finding potential markers of CVD risk with the aim of more accurate and early diagnosis. In this review we analyze the latest literature data dedicated to the role of heat shock protein 70 (HSP70) in cardiovascular pathology. HSP70 take part in such processes as arterial hypertension, coronary heart disease, and atherosclerosis. In atherogenesis, serum heat shock proteins 70 play a major role. It has been proven that in patients with a high concentration of heat shock protein molecules circulating in the blood, increased values of the carotid intima-media complex were observed. The important role of antibodies to circulating HSP70 is noted. Found an association of high levels of these antibodies with atherosclerosis in patients with arterial hypertension in history, with myocardial infarction. Low levels of anti-HSP70 antibodies are observed in patients with acute coronary syndrome. This proves the complexity of the mechanism and the dual role of antibodies against serum heat shock proteins 70. Thus, antibodies against heat shock proteins 70 can be assessed as a protective marker, and as a predictor, which requires further study, and the HSP70 molecules themselves can somehow to participate in the development of cardiovascular pathologies. Much attention is paid to the role of the inflammatory process and the mechanisms of innate immunity in CVD. As it is currently believed that Danger-associated molecular patterns (DAMPs) are involved in the pathogenesis of these pathologies in the context of a “hazard/damage” model. According to this model, the triggering factor is stress, leading to the release of DAMPs and their binding to innate immunity receptors - Toll-like receptors (TLRs). Activation of TLRs triggers the signaling cascade in the cell leading to the synthesis of pro-inflammatory cytokines. This contributes to the development of inflammation, which can provoke the emergence of new pathological processes in the body and worsen the course of existing diseases. The identification of new potential markers and knowledge of the molecular mechanisms of the pathogenesis of CVD can play an important role in the development of a new individual approach to the prevention of cardiovascular diseases.

scholarly journals The regulatory role of heat shock protein 70-reactive CD4+ T cells during rat listeriosis.

1998 ◽  
Vol 10 (2) ◽  
pp. 117-130 ◽  
Author(s):  
Y. Kimura ◽  
K. Yamada ◽  
T. Sakai ◽  
K. Mishima ◽  
H. Nishimura ◽  
...  
Keyword(s):  
T Cells ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cd4 T Cells ◽  
Heat Shock Protein 70 ◽  
Regulatory Role

scholarly journals CLINICAL AND THERAPEUTIC SIGNIFICANCE OF HEAT SHOCK PROTEINS

2021 ◽  
Vol 9 (02) ◽  
pp. 961-964
Author(s):  
Sreeja Nannapaneni ◽  
◽  
Gnana Sri Deepika Vusthepalli ◽  
Pavan Santhosh Guptha Vusthepalli ◽  
Kusuma Naredla ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Cell Biology ◽  
Experimental Investigations ◽  
Immunological Responses ◽  
Immune Mediated ◽  
Clinical Biomarker ◽  
Shock Proteins

Multiple experimental investigations have been successful in suggesting the role of heat shock protein as a clinical biomarker and therapeutic target in several diseases. All living cells, from the simplest prokaryote to the most complex multicellular organism, contain heat shock proteins-molecular chaperones that are responsible for management of unfolded polypeptides within the cell. In view of the fundamental role of heat shock proteins in maintenance of protein homeostasis, it seems likely that malfunctions associated with members of heat shock protein families would have pathological effects. Such effects might be minimal under normal physiological conditions, but could be exacerbated at times. This review provides an overview of the cell biology and immunology of heat shock proteins focusing predominantly on immunological responses to heat shock proteins in a range of immune-mediated diseases and in infectious diseases.

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