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.

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 Clinical and Therapeutic Significance of Various Heat Shock Proteins

2021 ◽  
Vol 11 (4) ◽  
Author(s):  
Mallu Maheswara Reddy ◽  
Kotikalapudi Sree Rama Chandra Karthik ◽  
Vemparala Renuka ◽  
Agaarapu Chandana ◽  
Golamari Siva Reddy
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Experimental Studies ◽  
Therapeutic Benefit ◽  
Membrane Domains ◽  
Diagnosis And Prognosis ◽  
Clinical Biomarkers ◽  
Clinical Biomarker ◽  
Shock Proteins

The purpose of this study was to explore the different roles of heat shock proteins especially in immunity and infections. Heat shock proteins were discovered 56 years ago, and much of the work has focused on the role of these proteins that play in protecting cells from stress. Heat shock proteins are highly conserved class of proteins present in all species from bacteria to humans. Several experimental studies have been successful in pointing to the role of heat shock protein as a clinical biomarker and therapeutic target in a variety of diseases. It will also highlight features of HSP family, and will discuss future implications of HSPs in the diagnosis and prognosis of clinical and therapeutic significance. The development of membrane-interacting drugs that modify specific membrane domains, modulating heat shock response, may also be of significant therapeutic benefit. These proteins function as molecular chaperones, assisting in the refolding of misfolded proteins or their elimination if they become irreversibly damaged. Proteomic studies have identified several different HSPs in various disease types that may be clinical biomarkers or molecular targets for various therapies.

scholarly journals Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96.

1995 ◽  
Vol 182 (3) ◽  
pp. 885-889 ◽  
Author(s):  
D Arnold ◽  
S Faath ◽  
H Rammensee ◽  
H Schild
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Tumor Cells ◽  
Mhc Class I ◽  
Donor Cell ◽  
Class I ◽  
Heat Shock Protein Gp96 ◽  
Shock Proteins

Vaccination of mice with heat shock proteins isolated from tumor cells induces immunity to subsequent challenge with those tumor cells the heat shock protein was isolated from but not with other tumor cells (Udono, H., and P.K. Srivastava. 1994. J. Immunol. 152:5398-5403). The specificity of this immune response is caused by tumor-derived peptides bound to the heat shock proteins (Udono., H., and P.K. Srivastava. 1993. J. Exp. Med. 178:1391-1396). Our experiments show that a single immunization with the heat shock protein gp96 isolated from beta-galactosidase (beta-gal) expressing P815 cells (of DBA/2 origin) induces cytotoxic T lymphocytes (CTLs) specific for beta-gal, in addition to minor H antigens expressed by these cells. CTLs can be induced in mice that are major histocompatibility complex (MHC) identical to the gp96 donor cells (H-2d) as well as in mice with a different MHC (H-2b). Thus gp96 is able to induce "cross priming" (Matzinger, P., and M.J. Bevan. 1977. Cell. Immunol. 33:92-100), indicating that gp96-associated peptides are not limited to the MHC class I ligands of the gp96 donor cell. Our data confirm the notion that samples of all cellular antigens presentable by MHC class I molecules are represented by peptides associated with gp96 molecules of that cell, even if the fitting MHC molecule is not expressed. In addition, we extend previous reports on the in vivo immunogenicity of peptides associated gp96 molecules to two new groups of antigens, minor H antigens, and proteins expressed in the cytosol.

Progesterone enhances target gene transcription by receptor free of heat shock proteins hsp90, hsp56, and hsp70

1991 ◽  
Vol 11 (10) ◽  
pp. 4998-5004
Author(s):  
M K Bagchi ◽  
S Y Tsai ◽  
M J Tsai ◽  
B W O'Malley
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Transcriptional Activation ◽  
Target Gene ◽  
Steroid Hormone ◽  
Receptor Activation ◽  
Target Cells ◽  
Dependent Manner ◽  
Shock Proteins

Steroid receptors regulate transcription of target genes in vivo and in vitro in a steroid hormone-dependent manner. Unoccupied progesterone receptor exists in the low-salt homogenates of target cells as a functionally inactive 8 to 10S complex with several nonreceptor components such as two molecules of 90-kDa heat shock protein (hsp90), a 70-kDa heat shock protein (hsp70), and a 56-kDa heat shock protein (hsp56). Ligand-induced dissociation of receptor-associated proteins such as hsp90 has been proposed as the mechanism of receptor activation. Nevertheless, it has not been established whether, beyond release of heat shock proteins, the steroidal ligand plays a role in modulating receptor activity. To examine whether the release of these nonreceptor proteins from receptor complex results in a constitutively active receptor, we isolated an unliganded receptor form essentially free of hsp90, hsp70, and hsp56. Using a recently developed steroid hormone-responsive cell-free transcription system, we demonstrate for the first time that the dissociation of heat shock proteins is not sufficient to generate a functionally active receptor. This purified receptor still requires hormone for high-affinity binding to a progesterone response element and for efficient transcriptional activation of a target gene. When an antiprogestin, Ru486, is bound to the receptor, it fails to promote efficient transcription. We propose that in the cell, in addition to the release of receptor-associated inhibitory proteins, a distinct hormone-mediated activation event must precede efficient gene activation.

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