Heat Shock Proteins and Cardiovascular Pathophysiology

2001 ◽  
Vol 81 (4) ◽  
pp. 1461-1497 ◽  
Author(s):  
Luc H. E. H. Snoeckx ◽  
Richard N. Cornelussen ◽  
Frans A. Van Nieuwenhoven ◽  
Robert S. Reneman ◽  
Ger J. Van der Vusse
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cardiovascular System ◽  
Defense Mechanism ◽  
Physiological Role ◽  
Eukaryotic Cell ◽  
Cellular Protein ◽  
Cell Organelles ◽  
Physiological Processes ◽  
Shock Proteins

In the eukaryotic cell an intrinsic mechanism is present providing the ability to defend itself against external stressors from various sources. This defense mechanism probably evolved from the presence of a group of chaperones, playing a crucial role in governing proper protein assembly, folding, and transport. Upregulation of the synthesis of a number of these proteins upon environmental stress establishes a unique defense system to maintain cellular protein homeostasis and to ensure survival of the cell. In the cardiovascular system this enhanced protein synthesis leads to a transient but powerful increase in tolerance to such endangering situations as ischemia, hypoxia, oxidative injury, and endotoxemia. These so-called heat shock proteins interfere with several physiological processes within several cell organelles and, for proper functioning, are translocated to different compartments following stress-induced synthesis. In this review we describe the physiological role of heat shock proteins and discuss their protective potential against various stress agents in the cardiovascular system.

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

scholarly journals Epigenetic Alterations of Heat Shock Proteins (HSPs) in Cancer

2019 ◽  
Vol 20 (19) ◽  
pp. 4758 ◽  
Author(s):  
Hyun Ban ◽  
Tae-Su Han ◽  
Keun Hur ◽  
Hyun-Soo Cho
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Cytotoxic Agents ◽  
Epigenetic Alterations ◽  
Regulatory Processes ◽  
Physiological Processes ◽  
Epigenetic Modifiers ◽  
Epigenetic Machinery ◽  
Shock Proteins

Heat shock proteins (HSPs) are associated with various physiological processes (protein refolding and degradation) involved in the responses to cellular stress, such as cytotoxic agents, high temperature, and hypoxia. HSPs are overexpressed in cancer cells and play roles in their apoptosis, invasion, proliferation, angiogenesis, and metastasis. The regulation or translational modification of HSPs is recognized as a therapeutic target for the development of anticancer drugs. Among the regulatory processes associated with HSP expression, the epigenetic machinery (miRNAs, histone modification, and DNA methylation) has key functions in cancer. Moreover, various epigenetic modifiers of HSP expression have also been reported as therapeutic targets and diagnostic markers of cancer. Thus, in this review, we describe the epigenetic alterations of HSP expression in cancer cells and suggest that HSPs be clinically applied as diagnostic and therapeutic markers in cancer therapy via controlled epigenetic modifiers.

scholarly journals Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes

2019 ◽  
Vol 24 (6) ◽  
pp. 1027-1044 ◽  
Author(s):  
Dorota Scieglinska ◽  
Zdzisław Krawczyk ◽  
Damian Robert Sojka ◽  
Agnieszka Gogler-Pigłowska
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Current Knowledge ◽  
Skin Layer ◽  
Keratinocyte Differentiation ◽  
Epidermal Keratinocytes ◽  
Physiological Processes ◽  
Open Questions ◽  
Stratified Squamous Epithelium ◽  
Shock Proteins

AbstractHeat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.

scholarly journals Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates

2021 ◽  
Vol 8 ◽  
Author(s):  
Bruno Fauvet ◽  
Andrija Finka ◽  
Marie-Pierre Castanié-Cornet ◽  
Anne-Marie Cirinesi ◽  
Pierre Genevaux ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Wild Type ◽  
Triple Mutant ◽  
Respiratory Enzymes ◽  
Physiological Processes ◽  
Knockout Mutants ◽  
Shock Proteins ◽  
Control Protein

In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains poorly characterized. To uncover physiological processes that depend on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild-type (WT) Escherichia coli and from knockout mutants ΔdnaKdnaJ (ΔKJ), ΔhtpG (ΔG), and ΔdnaKdnaJΔhtpG (ΔKJG). Whereas the ΔG mutant showed no detectable proteomic differences with wild-type, ΔKJ expressed more chaperones, proteases and ribosomes and expressed dramatically less metabolic and respiratory enzymes. Unexpectedly, we found that the triple mutant ΔKJG showed higher levels of metabolic and respiratory enzymes than ΔKJ, suggesting that bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70–Hsp40 substrates. Further in vivo experiments suggest that such Hsp90-mediated degradation possibly occurs through the HslUV protease.

The Role of Heat Shock Proteins in the Mechanisms of Neurodegeneration and Neuroprotection in Primary Glaucoma: Literature Review

2021 ◽  
pp. 122-131
Author(s):  
N. S. Lutsenko ◽  
T. V. Nedilka
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Neurodegenerative Diseases ◽  
Retinal Ganglion Cells ◽  
Defense Mechanism ◽  
Ganglion Cells ◽  
The Body ◽  
Retinal Ganglion ◽  
Shock Proteins

Heat shock proteins (HSP) are important components of the defense mechanism that increases the survival of body cells in adverse conditions due to antiapoptotic and cytoprotective effects. Since their discovery, numerous studies and experimental models have proved the role of HSPs as a key link in the processes of both repair and coagulation of proteins, as well as in the protection of cells from oxidative stress. The potential for pharmacological induction of HSPs in the human body makes them an attractive therapeutic target for many neurodegenerative diseases. This review examines the role of HSPs, especially fraction 70, in the mechanisms of neuroprotection of retinal ganglion cells in primary open-angle glaucoma being one of the common neurodegenerative diseases that can lead to complete loss of visual functions. A number of studies have shown the protective effect of HSP70 on retinal ganglion cells in animals with artificially induced glaucoma. But in the course of experiments on animal models, it was also proved that direct immunization with HSP through intravitreal injections induced pressure-independent degeneration of retinal ganglion cells. This indicates the need for indirect stimulation of HSP70 in order to activate their neuroprotective properties. To date, there are insufficient data on the circulation of HSP70 in the body of a person with glaucoma. These data indicate the prospects for further study of the role of HSP70 in glaucoma degeneration and elucidation of the ways of their mediated induction. Keywords: heat shock protein, HSP70, glaucoma, ganglion cells, retina, neuroprotection.

scholarly journals The Role ofα-Synuclein and LRRK2 in Tau Phosphorylation

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Fumitaka Kawakami ◽  
Takafumi Ichikawa
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Experimental Evidence ◽  
Physiological Role ◽  
Tau Phosphorylation ◽  
Therapeutic Strategies ◽  
Tau Pathology ◽  
Shock Proteins ◽  
Considerable Body

There is now a considerable body of experimental evidence that Parkinson’s disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role ofα-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition ofα-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

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