The therapeutic potential of heat shock proteins in cardiomyopathies due to mutations in cardiac structural proteins

2010 ◽  
Vol 49 (6) ◽  
pp. 904-907 ◽  
Author(s):  
Jessica E. Rodríguez ◽  
Monte S. Willis
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Therapeutic Potential ◽  
Structural Proteins ◽  
Shock Proteins

scholarly journals The role and therapeutic potential of heat shock proteins in haemorrhagic stroke

2019 ◽  
Vol 23 (9) ◽  
pp. 5846-5858 ◽  
Author(s):  
Anwen Shao ◽  
Yunxiang Zhou ◽  
Yihan Yao ◽  
Wenhua Zhang ◽  
Jianmin Zhang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Therapeutic Potential ◽  
Haemorrhagic Stroke ◽  
Shock Proteins

Cytokine function of heat shock proteins

2004 ◽  
Vol 286 (4) ◽  
pp. C739-C744 ◽  
Author(s):  
Min-Fu Tsan ◽  
Baochong Gao
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Innate Immune System ◽  
Therapeutic Potential ◽  
Innate Immune ◽  
Heat Sensitivity ◽  
Receptor Complex ◽  
Shock Proteins ◽  
Antigen Presenting ◽  
Tlr4 Receptor

Extensive work in the last 10 years has suggested that heat shock proteins (HSPs) may be potent activators of the innate immune system. It has been reported that Hsp60, Hsp70, Hsp90, and gp96 are capable of inducing the production of proinflammatory cytokines by the monocyte-macrophage system and the activation and maturation of dendritic cells (antigen-presenting cells) in a manner similar to the effects of lipopolysaccharide (LPS) and bacterial lipoprotein, e.g., via CD14/Toll-like receptor2 (TLR2) and CD14/TLR4 receptor complex-mediated signal transduction pathways. However, recent evidence suggests that the reported cytokine effects of HSPs may be due to the contaminating LPS and LPS-associated molecules. The reasons for previous failure to recognize the contaminant(s) as being responsible for the reported HSP cytokine effects include failure to use highly purified, low-LPS preparations of HSPs; failure to recognize the heat sensitivity of LPS; and failure to consider contaminant(s) other than LPS. Thus it is essential that efforts should be directed to conclusively determine whether the reported HSP cytokine effects are due to HSPs or to contaminant(s) present in the HSP preparations before further exploring the implication and therapeutic potential of the putative cytokine function of HSPs.

scholarly journals Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection

2021 ◽  
Vol 22 (17) ◽  
pp. 9366
Author(s):  
Anna Lubkowska ◽  
Waldemar Pluta ◽  
Aleksandra Strońska ◽  
Alicja Lalko
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Viral Replication ◽  
Viral Infection ◽  
Viral Infections ◽  
Therapeutic Potential ◽  
Biological Significance ◽  
Hsp70 Family ◽  
The Stability ◽  
Shock Proteins

Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and bacteria. They are responsible for the correct protein folding, protection of the cell against stressors, presenting immune and inflammatory cytokines; furthermore, they are important factors in regulating cell differentiation, survival and death. Although the biological function of HSPs is to maintain cell homeostasis, some of them can be used by viruses both to fold their proteins and increase the chances of survival in unfavorable host conditions. Folding viral proteins as well as replicating many different viruses are carried out by, among others, proteins from the HSP70 and HSP90 families. In some cases, the HSP70 family proteins directly interact with viral polymerase to enhance viral replication or they can facilitate the formation of a viral replication complex and/or maintain the stability of complex proteins. It is known that HSP90 is important for the expression of viral genes at both the transcriptional and the translational levels. Both of these HSPs can form a complex with HSP90 and, consequently, facilitate the entry of the virus into the cell. Current studies have shown the biological significance of HSPs in the course of infection SARS-CoV-2. A comprehensive understanding of chaperone use during viral infection will provide new insight into viral replication mechanisms and therapeutic potential. The aim of this study is to describe the molecular basis of HSP70 and HSP90 participation in some viral infections and the potential use of these proteins in antiviral therapy.

Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves

1983 ◽  
Vol 3 (9) ◽  
pp. 1648-1655
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Structural Proteins ◽  
Lycopersicon Peruvianum ◽  
Electron Microscopic ◽  
Considerable Part ◽  
Heat Shock Granules ◽  
Simultaneous Synthesis ◽  
Shock Proteins

Biochemical and electron microscopic analyses of heat-shocked suspension cultures of Peruvian tomato (Lycopersicon peruvianum) revealed that a considerable part of the dominant small heat shock proteins (hsps) with an Mr of approximately 17,000 are structural proteins of newly forming granular aggregates in the cytoplasm (heat shock granules), whose formation strictly depends on heat shock conditions (37 to 40 degrees C) and the presence or simultaneous synthesis of hsps. However, under certain conditions, e.g., in preinduced cultures maintained at 25 degrees C, hsps also accumulate as soluble proteins without concomitant assembly of heat shock granules. Similar heat shock-induced cytoplasmic aggregates were also observed in other cell cultures and heat-shocked tomato leaves and corn coleoptiles.

scholarly journals The Functions and Therapeutic Potential of Heat Shock Proteins in Inflammatory Bowel Disease—An Update

2019 ◽  
Vol 20 (21) ◽  
pp. 5331 ◽  
Author(s):  
Abdullah Hoter ◽  
Hassan Y. Naim
Keyword(s):  
Inflammatory Bowel Disease ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Bowel Disease ◽  
Therapeutic Potential ◽  
Inflammatory Bowel ◽  
Targeted Inhibition ◽  
Shock Proteins ◽  
Lines Of Evidence

Inflammatory bowel disease (IBD) is a multifactorial human intestinal disease that arises from numerous, yet incompletely defined, factors. Two main forms, Crohn’s disease (CD) and ulcerative colitis (UC), lead to a chronic pathological form. Heat shock proteins (HSPs) are stress-responsive molecules involved in various pathophysiological processes. Several lines of evidence link the expression of HSPs to the development and prognosis of IBD. HSP90, HSP70 and HSP60 have been reported to contribute to IBD in different aspects. Moreover, induction and/or targeted inhibition of specific HSPs have been suggested to ameliorate the disease consequences. In the present review, we shed the light on the role of HSPs in IBD and their targeting to prevent further disease progression.

Diagnostic, Prognostic and Therapeutic Potential of Heat Shock Proteins in Schistosomiasis and Bladder Cancer: A Review

2020 ◽  
Vol 18 ◽  
Author(s):  
Ndibonani Kebonang Qokoyi ◽  
Priscilla Masamba ◽  
Geraldene Munsamy ◽  
Abidemi Paul Kappo
Keyword(s):  
Bladder Cancer ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Therapeutic Potential ◽  
Treatment Options ◽  
Sub Saharan Africa ◽  
Cancer Of The Bladder ◽  
Sub Saharan ◽  
Shock Proteins ◽  
Parasitic Worms

Abstract:: Schistosomiasis is a waterborne tropical disease caused by infection with parasitic worms of the Schistosoma genus. This causes significant morbidity in the Middle East, South America, Southeast Asia and, mostly, in sub-Saharan Africa. For over 30 decades, this disease has been on a gradual rise, claiming thousands of lives and disfiguring its sufferers. Currently, over 280 000 mortalities per annum are attributed to this disease, with about 207 million reported cases of infection worldwide. In addition to these overwhelming statistics, infection caused by S. haematobium has been reported to predispose its sufferers to cancer of the bladder. Bladder cancer is regarded as the most common type of cancer in the urinary system, with relatively high incidence, progression and mortality rates despite the efforts put into providing optimal treatment for the disease. Despite the diagnostic and treatment options already put into place, there is still a growing need to develop alternative strategies to combat these diseases. The high expression levels of a group of molecular chaperones, known as heat shock proteins, can be used as biomarkers of infection and can consequently play a role in the development of alternative treatment methods.

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