scholarly journals The Pathophysiological Role of Heat Shock Response in Autoimmunity: A Literature Review

Cells ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2626
Author(s):  
Ariadni Androvitsanea ◽  
Kostas Stylianou ◽  
Eleni Drosataki ◽  
Ioannis Petrakis
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Literature Review ◽  
Heat Shock Proteins ◽  
Immune Responses ◽  
Inhibitory Effects ◽  
Pathophysiological Role ◽  
Shock Response ◽  
Shock Proteins

Within the last two decades, there has been increasing evidence that heat-shock proteins can have a differential influence on the immune system. They can either provoke or ameliorate immune responses. This review focuses on outlining the stimulatory as well as the inhibitory effects of heat-shock proteins 27, 40, 70, 65, 60, and 90 in experimental and clinical autoimmune settings.

Physiological Functions of Heat Shock Proteins

2020 ◽  
Vol 21 (8) ◽  
pp. 751-760 ◽  
Author(s):  
Qiang Shan ◽  
Fengtao Ma ◽  
Jingya Wei ◽  
Hongyang Li ◽  
Hui Ma ◽  
...  
Keyword(s):  
Heart Disease ◽  
Heat Stress ◽  
Heat Shock ◽  
Cancer Therapy ◽  
Heat Shock Proteins ◽  
Immune Responses ◽  
Molecular Chaperones ◽  
General Medicine ◽  
Shock Proteins

Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities. HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance of cellular homeostasis. Heat shock factor (HSF) is activated in response to environmental stresses and binds to heat shock elements (HSEs), promoting HSP translation and thus the production of high levels of HSPs to prevent damage to the organism. Here, we summarize the role of molecular chaperones as anti-heat stress molecules and their involvement in immune responses and the modulation of apoptosis. In addition, we review the potential application of HSPs to cancer therapy, general medicine, and the treatment of heart disease.

Heat shock proteins regulating Toll-like receptors and the immune system could be a novel therapeutic target for melanoma

2020 ◽  
Vol 20 ◽  
Author(s):  
Navid Shomali ◽  
Leila Sadat Hatamnezhad ◽  
Saeed Tarzi ◽  
Rozita Tamjidifar ◽  
Huaxi Xu ◽  
...  
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Immune Responses ◽  
Early Stage ◽  
Toll Like Receptors ◽  
Cross Presentation ◽  
Extracellular Milieu ◽  
Skin Cancers ◽  
Shock Proteins

: Melanoma is a serious type of skin cancer, which develops in melanocyte cells. Although it is less common than some other skin cancers, it can be far more dangerous if not treated at an early stage because of its ability to spread rapidly to other organs. Heat shock proteins (HSP) are intracellular molecular chaperones of naive proteins, which are induced in response to stressful conditions. HSP is released into the extracellular milieu and binds to Toll-like receptors (TLRs) to regulate immune responses, such as cytokine and chemokine release. HSPs have the capacity to release and bind to tumor-specific antigens, with cross-presentation of major histocompatibility complex (MHC) class I antigens. TLRs are innate immune system receptors, involved in the melanoma growth pathway through HSP activation. Melanocytes express TLR4 and TLR9 to modulate immune responses. Many TLR ligands are considered as proper adjuvant candidates, as they can activate dendritic cells. Targeting some TLRs, such as TLR7 and TLR9, is an available option for treating melanoma. In this review, we aimed to determine the relationship between TLRs and HSP groups in melanoma.

scholarly journals Heat Shock Proteins: Connectors between Heart and Kidney

Cells ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1939
Author(s):  
Carolina Victória Cruz Junho ◽  
Carolina Amaral Bueno Azevedo ◽  
Regiane Stafim da Cunha ◽  
Ainhoa Rodriguez de Yurre ◽  
Emiliano Medei ◽  
...  
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Intracellular Signaling ◽  
Cardiorenal Syndrome ◽  
Redox Balance ◽  
Cellular Functions ◽  
Shock Proteins ◽  
Type 3

Over the development of eukaryotic cells, intrinsic mechanisms have been developed in order to provide the ability to defend against aggressive agents. In this sense, a group of proteins plays a crucial role in controlling the production of several proteins, guaranteeing cell survival. The heat shock proteins (HSPs), are a family of proteins that have been linked to different cellular functions, being activated under conditions of cellular stress, not only imposed by thermal variation but also toxins, radiation, infectious agents, hypoxia, etc. Regarding pathological situations as seen in cardiorenal syndrome (CRS), HSPs have been shown to be important mediators involved in the control of gene transcription and intracellular signaling, in addition to be an important connector with the immune system. CRS is classified as acute or chronic and according to the first organ to suffer the injury, which can be the heart (CRS type 1 and type 2), kidneys (CRS type 3 and 4) or both (CRS type 5). In all types of CRS, the immune system, redox balance, mitochondrial dysfunction, and tissue remodeling have been the subject of numerous studies in the literature in order to elucidate mechanisms and propose new therapeutic strategies. In this sense, HSPs have been targeted by researchers as important connectors between kidney and heart. Thus, the present review has a focus to present the state of the art regarding the role of HSPs in the pathophysiology of cardiac and renal alterations, as well their role in the kidney–heart axis.

The Role of Heat Shock Proteins and Their Receptors in the Activation of the Immune System

2001 ◽  
Vol 382 (4) ◽  
Author(s):  
Harpreet Singh-Jasuja ◽  
Norbert Hilf ◽  
Danièle Arnold-Schild ◽  
Hansjörg Schild
Keyword(s):  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Activation of Heat Shock Genes Is Not Necessary for Protection by Heat Shock Transcription Factor 1 against Cell Death Due to a Single Exposure to High Temperatures

2003 ◽  
Vol 23 (16) ◽  
pp. 5882-5895 ◽  
Author(s):  
Sachiye Inouye ◽  
Kensaku Katsuki ◽  
Hanae Izu ◽  
Mitsuaki Fujimoto ◽  
Kazuma Sugahara ◽  
...  
Keyword(s):  
Cell Death ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Response ◽  
Single Exposure ◽  
Heat Shock Genes ◽  
Amino Terminal ◽  
Shock Response ◽  
Shock Proteins

ABSTRACT Heat shock response, which is characterized by the induction of a set of heat shock proteins, is essential for induced thermotolerance and is regulated by heat shock transcription factors (HSFs). Curiously, HSF1 is essential for heat shock response in mammals, whereas in avian HSF3, an avian-specific factor is required for the burst activation of heat shock genes. Amino acid sequences of chicken HSF1 are highly conserved with human HSF1, but those of HSF3 diverge significantly. Here, we demonstrated that chicken HSF1 lost the ability to activate heat shock genes through the amino-terminal domain containing an alanine-rich sequence and a DNA-binding domain. Surprisingly, chicken and human HSF1 but not HSF3 possess a novel function that protects against a single exposure to mild heat shock, which is not mediated through the activation of heat shock genes. Overexpression of HSF1 mutants that could not bind to DNA did not restore the susceptibility to cell death in HSF1-null cells, suggesting that the new protective role of HSF1 is mediated through regulation of unknown target genes other than heat shock genes. These results uncover a novel role of vertebrate HSF1, which has been masked underthe roles of heat shock proteins.

scholarly journals Role of Heat Shock Proteins in Protection from and Pathogenesis of Infectious Diseases

1999 ◽  
Vol 12 (1) ◽  
pp. 19-39 ◽  
Author(s):  
Ulrich Zügel ◽  
Stefan H. E. Kaufmann
Keyword(s):  
Immune Response ◽  
Immune System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Unfolding ◽  
Wide Distribution ◽  
Microbial Pathogens ◽  
Stressed Cells ◽  
Shock Proteins

SUMMARY Increased synthesis of heat shock proteins (hsp) occurs in prokaryotic and eukaryotic cells when they are exposed to stress. By increasing their hsp content, cells protect themselves from lethal assaults, primarily because hsp interfere with the uncontrolled protein unfolding that occurs under stress. However, hsp are not produced only by stressed cells; some hsp are synthesized constitutively and perform important housekeeping functions. Accordingly, hsp are involved in the assembly of molecules which play important roles in the immune system. It is not surprising that due to their wide distribution and their homology among different species, hsp represent target antigens of the immune response. Frequent confrontation of the immune system with conserved regions of hsp which are shared by various microbial pathogens can potentiate antimicrobial immunity. However, long-term confrontation of the immune system with hsp antigens which are similar in the host and invaders may convert the immune response against these host antigens and promote autoimmune disease. This review provides an overview of the role of hsp in immunity with a focus on infectious and autoimmune diseases.

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