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 Beneficial Regulation of Elastase Activity and Expression of Tissue Inhibitors of Matrixmetalloproteinases, Fibrillin, Transforming Growth Factor-β, and Heat Shock Proteins by P. leucotomos in Nonirradiated or Ultraviolet-Radiated Epidermal Keratinocytes

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Neena Philips ◽  
Salvador Gonzalez
Keyword(s):  
Growth Factor ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Transforming Growth Factor ◽  
Epidermal Keratinocytes ◽  
Elastase Activity ◽  
Tissue Inhibitors ◽  
Cellular Expression ◽  
Ecm Proteins ◽  
Shock Proteins

There is loss of the structural integrity of the extracellular matrix (ECM) with intrinsic aging as well as photoaging, largely due to reactive oxygen species (ROS). The structural ECM proteins include the microfibrils that are composed of fibrillin. The structural ECM proteins are primarily degraded by the matrixmetalloproteinases (MMPs) and elastase enzymes. The MMPs are inhibited by the tissue inhibitors of MMPs (TIMPs). A primary regulator of the ECM proteins is transforming growth factor-β (TGF-β), and the chaperone proteins important for its formation are the heat shock proteins (HSP). P. leucotomos extract beneficially regulates of MMPs, TIMPs, and TGF-β in nonirradiated or ultraviolet (UV) radiated fibroblasts and melanoma cells. The hypothesis of this research was that the antioxidant activity or chemistry of P. leucotomos extract would also directly inhibit elastase activity, stimulate the cellular expression of TIMPs, fibrillins, and TGF-β, and regulate HSPs in nonirradiated and UVA or UVB radiated epidermal keratinocytes. P. leucotomos directly inhibited elastase activity, stimulated the cellular expression of TIMPs, fibrillins, and TGF-β, and differentially regulated HSPs in nonirradiated and UVA or UVB radiated epidermal keratinocytes. We infer that the P. leucotomos extract strengthens the ECM and is effective in the prevention or treatment of intrinsic and photoaging of skin.

scholarly journals Synergistic Effects of Toxic Elements on Heat Shock Proteins

2014 ◽  
Vol 2014 ◽  
pp. 1-17 ◽  
Author(s):  
Khalid Mahmood ◽  
Saima Jadoon ◽  
Qaisar Mahmood ◽  
Muhammad Irshad ◽  
Jamshaid Hussain
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Toxic Elements ◽  
Current Knowledge ◽  
Synergistic Effects ◽  
Expression Patterns ◽  
Expression Levels ◽  
Functional Capabilities ◽  
Shock Proteins ◽  
Diverse Groups

Heat shock proteins show remarkable variations in their expression levels under a variety of toxic conditions. A research span expanded over five decades has revealed their molecular characterization, gene regulation, expression patterns, vast similarity in diverse groups, and broad range of functional capabilities. Their functions include protection and tolerance against cytotoxic conditions through their molecular chaperoning activity, maintaining cytoskeleton stability, and assisting in cell signaling. However, their role as biomarkers for monitoring the environmental risk assessment is controversial due to a number of conflicting, validating, and nonvalidating reports. The current knowledge regarding the interpretation of HSPs expression levels has been discussed in the present review. The candidature of heat shock proteins as biomarkers of toxicity is thus far unreliable due to synergistic effects of toxicants and other environmental factors. The adoption of heat shock proteins as “suit of biomarkers in a set of organisms” requires further investigation.

scholarly journals Heat Shock Proteins in Oxidative Stress and Ischemia/Reperfusion Injury and Benefits from Physical Exercises: A Review to the Current Knowledge

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Jakub Szyller ◽  
Iwona Bil-Lula
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Current Knowledge ◽  
Ischemia Reperfusion ◽  
Physical Exercises ◽  
Shock Proteins

Heat shock proteins (HSPs) are molecular chaperones produced in response to oxidative stress (OS). These proteins are involved in the folding of newly synthesized proteins and refolding of damaged or misfolded proteins. Recent studies have been focused on the regulatory role of HSPs in OS and ischemia/reperfusion injury (I/R) where reactive oxygen species (ROS) play a major role. ROS perform many functions, including cell signaling. Unfortunately, they are also the cause of pathological processes leading to various diseases. Biological pathways such as p38 MAPK, HSP70 and Akt/GSK-3β/eNOS, HSP70, JAK2/STAT3 or PI3K/Akt/HSP70, and HSF1/Nrf2-Keap1 are considered in the relationship between HSP and OS. New pathophysiological mechanisms involving ROS are being discovered and described the protein network of HSP interactions. Understanding of the mechanisms involved, e.g., in I/R, is important to the development of treatment methods. HSPs are multifunctional proteins because they closely interact with the antioxidant and the nitric oxide generation systems, such as HSP70/HSP90/NOS. A deficiency or excess of antioxidants modulates the activation of HSF and subsequent HSP biosynthesis. It is well known that HSPs are involved in the regulation of several redox processes and play an important role in protein-protein interactions. The latest research focuses on determining the role of HSPs in OS, their antioxidant activity, and the possibility of using HSPs in the treatment of I/R consequences. Physical exercises are important in patients with cardiovascular diseases, as they affect the expression of HSPs and the development of OS.

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.

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.

scholarly journals Molecular Chaperone Dysfunction in Neurodegenerative Diseases and Effects of Curcumin

2014 ◽  
Vol 2014 ◽  
pp. 1-14 ◽  
Author(s):  
Panchanan Maiti ◽  
Jayeeta Manna ◽  
Shobi Veleri ◽  
Sally Frautschy
Keyword(s):  
Natural Products ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Neurodegenerative Diseases ◽  
Protein Misfolding ◽  
Current Knowledge ◽  
Aggregate Size ◽  
Peptide Sequence ◽  
Treatment Regimens ◽  
Shock Proteins

The intra- and extracellular accumulation of misfolded and aggregated amyloid proteins is a common feature in several neurodegenerative diseases, which is thought to play a major role in disease severity and progression. The principal machineries maintaining proteostasis are the ubiquitin proteasomal and lysosomal autophagy systems, where heat shock proteins play a crucial role. Many protein aggregates are degraded by the lysosomes, depending on aggregate size, peptide sequence, and degree of misfolding, while others are selectively tagged for removal by heat shock proteins and degraded by either the proteasome or phagosomes. These systems are compromised in different neurodegenerative diseases. Therefore, developing novel targets and classes of therapeutic drugs, which can reduce aggregates and maintain proteostasis in the brains of neurodegenerative models, is vital. Natural products that can modulate heat shock proteins/proteosomal pathway are considered promising for treating neurodegenerative diseases. Here we discuss the current knowledge on the role of HSPs in protein misfolding diseases and knowledge gained from animal models of Alzheimer’s disease, tauopathies, and Huntington’s diseases. Further, we discuss the emerging treatment regimens for these diseases using natural products, like curcumin, which can augment expression or function of heat shock proteins in the cell.

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.

scholarly journals Heat Shock Proteins and Neurodegenerative Disorders

2008 ◽  
Vol 8 ◽  
pp. 270-274 ◽  
Author(s):  
Eliza Ting-Li Soo ◽  
Yee-Kong Ng ◽  
Boon-Huat Bay ◽  
George Wai-Cheong Yip
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Neurodegenerative Disorders ◽  
Current Knowledge ◽  
Cellular Damage ◽  
Protective Function ◽  
Cellular Processes ◽  
Evolutionarily Conserved ◽  
Shock Proteins ◽  
Stressful Stimulus

Heat shock proteins (HSPs) are evolutionarily conserved molecules and play important roles in fundamental cellular processes. They serve as molecular chaperones and hence provide a protective function in ensuring cell survival and repair of cellular damage after a stressful stimulus. This paper summarizes the current knowledge about the different roles of HSPs in aging and disease, focusing on the neurodegenerative disorders of Alzheimer's disease, Parkinson's disease, Huntington's disease, and prion disease.

Oral Microbial Heat-shock Proteins and Their Potential Contributions to Infections

2003 ◽  
Vol 14 (6) ◽  
pp. 399-412 ◽  
Author(s):  
Florence Goulhen ◽  
Daniel Grenier ◽  
Denis Mayrand
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Current Knowledge ◽  
Main Role ◽  
Oral Diseases ◽  
Human Pathogens ◽  
Tissue Destruction ◽  
Pathogenic Potential ◽  
Shock Proteins ◽  
Micro Organisms

The oral cavity is a complex ecosystem in which several hundred microbial species normally cohabit harmoniously. However, under certain special conditions, the growth of some micro-organisms with a pathogenic potential is promoted, leading to infections such as dental caries, periodontal disease, and stomatitis. The physiology and pathogenic properties of micro-organisms are influenced by modifications in environmental conditions that lead to the synthesis of specific proteins known as the heat-shock proteins (HSPs). HSPs are families of highly conserved proteins whose main role is to allow micro-organisms to survive under stress conditions. HSPs act as molecular chaperones in the assembly and folding of proteins, and as proteases when damaged or toxic proteins have to be degraded. Several pathological functions have been associated with these proteins. Many HSPs of oral micro-organisms, particularly periodontopathogens, have been identified, and some of their properties—including location, cytotoxicity, and amino acid sequence homology with other HSPs—have been reported. Since these proteins are immunodominant antigens in many human pathogens, studies have recently focused on the potential contributions of HSPs to oral diseases. The cytotoxicity of some bacterial HSPs may contribute to tissue destruction, whereas the presence of common epitopes in host proteins and microbial HSPs may lead to autoimmune responses. Here, we review the current knowledge regarding HSPs produced by oral micro-organisms and discuss their possible contributions to the pathogenesis of oral infections.

scholarly journals Behcet’s disease: from heat shock proteins to infections

2014 ◽  
Vol 8 (2) ◽  
pp. 139-155 ◽  
Author(s):  
Fatemeh Dabbagh ◽  
Afshin Borhani Haghighi ◽  
Younes Ghasemi
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Behçet’S Disease ◽  
Behcet’S Disease ◽  
Behçet's Disease ◽  
Current Knowledge ◽  
Unknown Etiology ◽  
Microbial Infection ◽  
Behcet's Disease ◽  
Shock Proteins

AbstractBackground: Behcet’s disease (BD) is a chronic, inflammatory multisystemic condition of unknown etiology. Although the cause of BD is not clear, it is believed to be the result of an autoimmune process triggered by an infectious or environmental agent (possibly local to a geographic region) in a genetically predisposed individual.Objective: To detail current knowledge of the role of microorganisms in the pathogenesis of BD and review the infectious etiology of this disease.Methods: The review based on publication in SCOPUS, Science direct, and PubMed.Results: A microbial infection has been implicated in the development of the disease to explain the strong inflammatory reactions observed, the activation of monocytes and macrophages, and the induction of proinflammatory cytokines and chemokines detected. Common factors linking some of the possible pathogenetic agents are extrinsically induced tissue stress or heat shock proteins, which react with host tissues and elicit significant T-helper type 1 cell responses.Conclusion: Based on collected data, we conclude that the microorganisms discussed seem to participate and, at least in part, act as triggers during the course of BD. By clarifying the microbial associations of BD and finding its etiology, particularly the causative antigens leading to BD, it would be easier to suggest more effective treatment and preventive strategies for this disease.

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