scholarly journals Elevated circulating heat shock protein 70 and its antibody concentrations in chronic spontaneous urticaria

2017 ◽  
Vol 31 ◽  
pp. 039463201775044 ◽  
Author(s):  
Alicja Kasperska-Zając ◽  
Aleksandra Damasiewicz-Bodzek ◽  
Katarzyna Bieniek ◽  
Agnieszka Skrzypulec-Frankel ◽  
Krystyna Tyrpien-Golder ◽  
...  
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Chronic Spontaneous Urticaria ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Shock Proteins ◽  
And Function

Heat shock proteins (Hsp) play a complex role in cytoprotection, inflammation, and function of the immune system. They may be involved in pathogenesis of various diseases. Our aim was to determine circulating Hsp70 and anti-Hsp70 antibodies concentrations in patients with chronic spontaneous urticaria (CSU). Concentrations of Hsp70 in plasma and anti-Hsp70 antibodies in serum as well as serum C-reactive protein (CRP) were measured in CSU patients and in the controls. Plasma Hsp70 concentrations were significantly higher in CSU (all) and mild CSU patients as compared with the controls. Moderate–severe CSU patients tended to show higher Hsp70 concentration as compared with the controls, but not with mild activity of the disease. There were no significant differences in Hsp70 concentration between moderate–severe and mild CSU patients. Serum anti-Hsp70 antibodies concentrations were significantly higher in CSU (all) and mild CSU in comparison to the controls. Association was observed between anti-Hsp70 antibodies and increased CRP concentration; however, no correlation between anti-Hsp70 and Hsp70 concentrations was seen in the patients. It seems that up-regulation of Hsp70 in CSU may induce marked increase in anti-Hsp70 antibodies production, which are accompanied by parallel changes in CRP concentration. We suggest that Hsp may be released in CSU in response to stressful stimuli, such as inflammation.

scholarly journals Association of extracellular heat shock protein 70 and insulin resistance in type 2 diabetes; independent of obesity and C-reactive protein

2018 ◽  
Vol 24 (1) ◽  
pp. 69-75 ◽  
Author(s):  
Hamid Alemi ◽  
Pegah Khaloo ◽  
Soghra Rabizadeh ◽  
Mohammad Ali Mansournia ◽  
Hossein Mirmiranpour ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Type 2 Diabetes ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
C Reactive Protein ◽  
Reactive Protein

scholarly journals BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins

2017 ◽  
Vol 429 (1) ◽  
pp. 128-141 ◽  
Author(s):  
Jennifer N. Rauch ◽  
Eric Tse ◽  
Rebecca Freilich ◽  
Sue-Ann Mok ◽  
Leah N. Makley ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Small Heat Shock Proteins ◽  
Scaffolding Protein ◽  
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 Regulation of Apoptotic and Inflammatory Cell Signaling in Cerebral Ischemia

2008 ◽  
Vol 109 (2) ◽  
pp. 339-348 ◽  
Author(s):  
Rona G. Giffard ◽  
Ru-Quan Han ◽  
John F. Emery ◽  
Melissa Duan ◽  
Jean Francois Pittet
Keyword(s):  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Multiple Points ◽  
Inflammatory Cytokine Production ◽  
Response To Stress ◽  
Survival Signaling ◽  
Shock Proteins

Although heat shock proteins have been studied for decades, new intracellular and extracellular functions in a variety of diseases continue to be discovered. Heat shock proteins function within networks of interacting proteins; they can alter cellular physiology rapidly in response to stress without requiring new protein synthesis. This review focuses on the heat shock protein 70 family and considers especially the functions of the inducible member, heat shock protein 72, in the setting of cerebral ischemia. In general, inhibiting apoptotic signaling at multiple points and up-regulating survival signaling, heat shock protein 70 has a net prosurvival effect. Heat shock protein 70 has both antiinflammatory and proinflammatory effects depending on the cell type, context, and intracellular or extracellular location. Intracellular effects are often antiinflammatory with inhibition of nuclear factor-kappaB signaling. Extracellular effects can lead to inflammatory cytokine production or induction of regulatory immune cells and reduced inflammation.

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