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Could Small Heat Shock Protein HSP27 Be a First-Line Target for Preventing Protein Aggregation in Parkinson’S Disease?
International Journal of Molecular Sciences Review Could Small Heat Shock Protein HSP27 Be a First-Line Target for Preventing Protein Aggregation in Parkinson’s Disease? Javier Navarro-Zaragoza 1,2 , Lorena Cuenca-Bermejo 2,3 , Pilar Almela 1,2,* , María-Luisa Laorden 1,2 and María-Trinidad Herrero 2,3,* 1 Department of Pharmacology, School of Medicine, University of Murcia, Campus Mare Nostrum, 30100 Murcia, Spain; [email protected] (J.N.-Z.); [email protected] (M.-L.L.) 2 Institute of Biomedical Research of Murcia (IMIB), Campus de Ciencias de la Salud, 30120 Murcia, Spain 3 Clinical & Experimental Neuroscience (NICE), Institute for Aging Research, School of Medicine, University of Murcia, Campus Mare Nostrum, 30100 Murcia, Spain; [email protected] * Correspondence: [email protected] (P.A.); [email protected] (M.-T.H.); Tel.: +34-868889358 (P.A.); +34-868883954 (M.-T.H.) Abstract: Small heat shock proteins (HSPs), such as HSP27, are ubiquitously expressed molecular chaperones and are essential for cellular homeostasis. The major functions of HSP27 include chaper- oning misfolded or unfolded polypeptides and protecting cells from toxic stress. Dysregulation of stress proteins is associated with many human diseases including neurodegenerative diseases, such as Parkinson’s disease (PD). PD is characterized by the presence of aggregates of α-synuclein in the central and peripheral nervous system, which induces the degeneration of dopaminergic neurons in the substantia nigra pars compacta (SNpc) and in the autonomic nervous system. Autonomic dys- function is an important non-motor phenotype of PD, which includes cardiovascular dysregulation, Citation: Navarro-Zaragoza, J.; among others. Nowadays, the therapies for PD focus on dopamine (DA) replacement. -
Identification and Characterization of Three Heat Shock Protein 90
G C A T T A C G G C A T genes Article Identification and Characterization of Three Heat Shock Protein 90 (Hsp90) Homologs in the Brown Planthopper Xuan Chen 1,2, Ze-Dong Li 1, Yi-Ting Dai 1, Ming-Xing Jiang 1,* and Chuan-Xi Zhang 1,2,* 1 State Key Laboratory of Rice Biology and Ministry of Agriculture Key Laboratory of Agricultural Entomology, Institute of Insect Science, Zhejiang University, Hangzhou 310058, China; [email protected] (X.C.); [email protected] (Z.-D.L.); [email protected] (Y.-T.D.) 2 State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-Products, Key Laboratory of Biotechnology in Plant Protection of MOA of China and Zhejiang Province, Institute of Plant Virology, Ningbo University, Ningbo 315211, China * Correspondence: [email protected] (M.-X.J.); [email protected] (C.-X.Z.) Received: 9 August 2020; Accepted: 10 September 2020; Published: 12 September 2020 Abstract: Hsp90 (heat shock protein 90) chaperone machinery is considered to be a key regulator of proteostasis under both physiological and stress growth conditions in eukaryotic cells. The high conservation of both the sequence and function of Hsp90 allows for the utilization of various species to explore new phenotypes and mechanisms. In this study, three Hsp90 homologs were identified in the brown planthopper (BPH), Nilaparvata lugens: cytosolic NlHsp90, endoplasmic reticulum (ER) NlGRP94 and mitochondrial NlTRAP1. Sequence analysis and phylogenetic construction showed that these proteins belonged to distinct classes consistent with the predicted localization and suggested an evolutionary relationship between NlTRAP1 and bacterial HtpG (high-temperature protein G). -
Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection After Brain Injury
cells Review Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury Jong Youl Kim 1, Sumit Barua 1, Mei Ying Huang 1,2, Joohyun Park 1,2, Midori A. Yenari 3,* and Jong Eun Lee 1,2,* 1 Department of Anatomy, Yonsei University College of Medicine, Seoul 03722, Korea; [email protected] (J.Y.K.); [email protected] (S.B.); [email protected] (M.Y.H.); [email protected] (J.P.) 2 BK21 Plus Project for Medical Science and Brain Research Institute, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu, Seoul 03722, Korea 3 Department of Neurology, University of California, San Francisco & the San Francisco Veterans Affairs Medical Center, Neurology (127) VAMC 4150 Clement St., San Francisco, CA 94121, USA * Correspondence: [email protected] (M.A.Y.); [email protected] (J.E.L.); Tel.: +1-415-750-2011 (M.A.Y.); +82-2-2228-1646 (ext. 1659) (J.E.L.); Fax: +1-415-750-2273 (M.A.Y.); +82-2-365-0700 (J.E.L.) Received: 17 July 2020; Accepted: 26 August 2020; Published: 2 September 2020 Abstract: The 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions. Its chaperone properties can assist in protein folding and prevent protein aggregation following several of these insults. Although its neuroprotective properties have been largely attributed to its chaperone functions, HSP70 may interact directly with proteins involved in cell death and inflammatory pathways following injury. -
REVIEW Heat Shock Proteins – Modulators of Apoptosis in Tumour
Leukemia (2000) 14, 1161–1173 2000 Macmillan Publishers Ltd All rights reserved 0887-6924/00 $15.00 www.nature.com/leu REVIEW Heat shock proteins – modulators of apoptosis in tumour cells EM Creagh, D Sheehan and TG Cotter Tumour Biology Laboratory, Department of Biochemistry, University College Cork, Lee Maltings, Prospect Row, Cork, Ireland Apoptosis is a genetically programmed, physiological method ditions, when the stress level eliminates the capacity for regu- of cell destruction. A variety of genes are now recognised as lated activation of the apoptotic cascade, the cells undergo positive or negative regulators of this process. Expression of inducible heat shock proteins (hsp) is known to correlate with necrosis. At lower levels, injured cells activate their own increased resistance to apoptosis induced by a range of apoptotic programme. However, if the level of stress is low diverse cytotoxic agents and has been implicated in chemo- enough, cells attempt to survive and activate a stress response therapeutic resistance of tumours and carcinogenesis. Inten- system (Figure 1). This response involves a shut-down of all sive research on apoptosis over the past number of years has cellular protein synthesis apart from a rapid induction of heat provided significant insights into the mechanisms and molecu- shock proteins, which results in a transient state of thermotol- lar events that occur during this process. The modulatory 8 effects of hsps on apoptosis are well documented, however, erance. Once the stress element is removed, these cells func- the mechanisms of hsp-mediated protection against apoptosis tion normally and the levels of hsps drop back to basal levels remain to be fully defined, although several hypotheses have with time. -
Anti-Heat Shock Protein 27 (HSP27) Developed in Rabbit, Igg Fraction of Antiserum
Anti-Heat Shock Protein 27 (HSP27) Developed in Rabbit, IgG Fraction of Antiserum Product Number P 1498 REH FXO31656 Product Description Anti-Heat Shock Protein 27 (HSP27) is developed in by various cytokines, growth factors, hormones and rabbit using as immunogen a synthetic peptide chemicals. HSP27 shows a rapid phosphorylation, corresponding to amino acids 186-205 located at following exposure to stress stimuli.4,5 It is the C-terminus of human HSP27, conjugated to phosphorylated on multiple serine residues by KLH. This sequence is highly homologous in rat MAPKAP kinase 2/3 in the p38 MAPK stress- HSP27 (85% identity) and to a lesser extent in sensitive signaling pathway.4-7 HSP27 acts as an mouse HSP27/25 (65% identity). Whole antiserum actin-cap binding protein and can inhibit actin is fractionated and then further purified by ion- polymerization, thus modulating actin dynamics exchange chromatography to provide the IgG during stress. This function is regulated by fraction of antiserum that is essentially free of other phosphorylation and the oligomerization state of rabbit serum proteins. HSP27.7,8 HSP27 has also been shown to protect against apoptotic cell death triggered by a variety of Anti- Heat Shock Protein 27 (HSP27) recognizes stimuli including hyperthermia, oxidative stress, Fas HSP27 (27 kDa). Applications include the detection ligand and cytotoxic drugs.9,10 Recent findings of HSP27 by immunoblotting and indicate that HSP27 interferes specifically with the immunofluorescence. Staining of HSP27 in mitochondrial pathway of caspase-induced cell immunoblotting is specifically inhibited with the death,11,12 by acting as a negative regulator of HSP27 immunizing peptide (human, amino acids cytochrome c-dependent activation of caspase-3.13 186-205). -
Regulation of Antimicrobial Pathways by Endogenous Heat Shock Proteins in Gastrointestinal Disorders
Review Regulation of Antimicrobial Pathways by Endogenous Heat Shock Proteins in Gastrointestinal Disorders Emma Finlayson-Trick 1 , Jessica Connors 2, Andrew Stadnyk 1,2 and Johan Van Limbergen 1,2,* 1 Department of Microbiology & Immunology, Dalhousie University, 5850 College Street, Room 7-C, Halifax, NS B3H 4R2, Canada; emma.fi[email protected] (E.F.-T.); [email protected] (A.S.) 2 Division of Pediatric Gastroenterology and Nutrition, Department of Pediatrics, Dalhousie University, IWK Health Centre, 5850/5980 University Avenue, Halifax, NS B3K 6R8, Canada; [email protected] * Correspondence: [email protected]; Tel.: +902-470-8746; Fax: +902-470-7249 Received: 31 August 2018; Accepted: 26 September 2018; Published: 28 September 2018 Abstract: Heat shock proteins (HSPs) are essential mediators of cellular homeostasis by maintaining protein functionality and stability, and activating appropriate immune cells. HSP activity is influenced by a variety of factors including diet, microbial stimuli, environment and host immunity. The overexpression and down-regulation of HSPs is associated with various disease phenotypes, including the inflammatory bowel diseases (IBD) such as Crohn’s disease (CD). While the precise etiology of CD remains unclear, many of the putative triggers also influence HSP activity. The development of different CD phenotypes therefore may be a result of the disease-modifying behavior of the environmentally-regulated HSPs. Understanding the role of bacterial and endogenous HSPs in host homeostasis and disease will help elucidate the complex interplay of factors. Furthermore, discerning the function of HSPs in CD may lead to therapeutic developments that better reflect and respond to the gut environment. -
Lipopolysaccharide Heat Shock Protein 60
Heat Shock Protein 60: Specific Binding of Lipopolysaccharide Christiane Habich, Karina Kempe, Ruurd van der Zee, Robert Rümenapf, Hidehiko Akiyama, Hubert Kolb and This information is current as Volker Burkart of September 28, 2021. J Immunol 2005; 174:1298-1305; ; doi: 10.4049/jimmunol.174.3.1298 http://www.jimmunol.org/content/174/3/1298 Downloaded from References This article cites 50 articles, 20 of which you can access for free at: http://www.jimmunol.org/content/174/3/1298.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 28, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2005 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Heat Shock Protein 60: Specific Binding of Lipopolysaccharide1 Christiane Habich,2* Karina Kempe,* Ruurd van der Zee,† Robert Ru¨menapf,* Hidehiko Akiyama,* Hubert Kolb,* and Volker Burkart* Human heat shock protein 60 (HSP60) has been shown to bind to the surface of innate immune cells and to elicit a proinflam- matory response. -
The Role of Heat Shock Proteins in Regulating Receptor Signal Transduction
Molecular Pharmacology Fast Forward. Published on January 22, 2019 as DOI: 10.1124/mol.118.114652 This article has not been copyedited and formatted. The final version may differ from this version. MOL # 114652 The Role of Heat Shock Proteins in Regulating Receptor Signal Transduction John M. Streicher, Ph.D. Department of Pharmacology, College of Medicine, University of Arizona, Tucson AZ USA Downloaded from molpharm.aspetjournals.org at ASPET Journals on October 2, 2021 1 Molecular Pharmacology Fast Forward. Published on January 22, 2019 as DOI: 10.1124/mol.118.114652 This article has not been copyedited and formatted. The final version may differ from this version. MOL # 114652 Running Title: Heat Shock Protein Regulation of Receptor Signaling Corresponding Author: Dr. John M. Streicher, Department of Pharmacology, College of Medicine, University of Arizona, Box 245050, LSN563, 1501 N. Campbell Ave., Tucson AZ 85724. Phone: (520)-626-7495. Email: [email protected] Text Pages: 28 Downloaded from Tables: 1 Figures: 1 References: 113 molpharm.aspetjournals.org Abstract: 233 Introduction: 348 Main Text: 3,427 at ASPET Journals on October 2, 2021 Abbreviations: alpha-GDP Dissociation Inhibitor (alpha-GDI); Central Nervous System (CNS); Cyclic Adenosine Monophosphate (cAMP); Cyclin Dependent Kinase (CDK); Extracellular Signal-Regulated Kinase (ERK); Focal Adhesion Kinase (FAK); G Protein-Coupled Receptor (GPCR); G Protein-Coupled Receptor Kinase (GRK); Glycogen Synthase Kinase-3 (GSK-3); Guanosine Di/Triphosphate (GDP/GTP); Heat Shock Factor-1 (HSF-1); Heat shock protein (Hsp); c-Jun N-Terminal Kinase (JNK); Mitogen Activated Protein Kinase (MAPK); MAPK/ERK Kinase (MEK); Protein Kinase A (PKA); Protein Kinase C (PKC); Stress-Induced Phosphoprotein-1 (STIP1); Vascular Endothelial Growth Factor Receptor (VEGFR) 2 Molecular Pharmacology Fast Forward. -
Description of Strongly Heat-Inducible Heat Shock Protein 70 Transcripts
www.nature.com/scientificreports OPEN Description of strongly heat- inducible heat shock protein 70 transcripts from Baikal endemic Received: 6 February 2019 Accepted: 30 May 2019 amphipods Published: xx xx xxxx Polina Drozdova 1, Daria Bedulina 1,2, Ekaterina Madyarova1,2, Lorena Rivarola- Duarte3,4,12, Stephan Schreiber 5, Peter F. Stadler 3,4,6,7,8,9,10, Till Luckenbach11 & Maxim Timofeyev 1,2 Heat shock proteins/cognates 70 are chaperones essential for proper protein folding. This protein family comprises inducible members (Hsp70s) with expression triggered by the increased concentration of misfolded proteins due to protein-destabilizing conditions, as well as constitutively expressed cognate members (Hsc70s). Previous works on non-model amphipod species Eulimnogammarus verrucosus and Eulimnogammarus cyaneus, both endemic to Lake Baikal in Eastern Siberia, have only revealed a constitutively expressed form, expression of which was moderately further induced by protein- destabilizing conditions. Here we describe heat-inducible hsp70s in these species. Contrary to the common approach of using sequence similarity with hsp/hsc70 of a wide spectrum of organisms and some characteristic features, such as absence of introns within genes and presence of heat shock elements in their promoter areas, the present study is based on next-generation sequencing for the studied or related species followed by diferential expression analysis, quantitative PCR validation and detailed investigation of the predicted polypeptide sequences. This approach allowed us to describe a novel type of hsp70 transcripts that overexpress in response to heat shock. Moreover, we propose diagnostic sequence features of this Hsp70 type for amphipods. Phylogenetic comparisons with diferent types of Hsp/Hsc70s allowed us to suggest that the hsp/hsc70 gene family in Amphipoda diversifed into cognate and heat-inducible paralogs independently from other crustaceans. -
Heat Shock Proteins in Thermotolerance and Other Cellular Processes1
[CANCER RESEARCH 47, 5249-5255, October 15, 1987) Perspectivesin CancerResearch Heat Shock Proteins in Thermotolerance and Other Cellular Processes1 Stephen W. Carper,2 John J. Duffy, and Eugene W. Gerner Department of Radiation Oncology and Cancer Center, The University of Arizona Health Sciences Center, Tucson, Arizona S5724 Heat shock proteins are a unique set of highly conserved erentially synthesized (for recent reviews, see Refs. 7-13). The proteins induced by heat and other stresses. Their role in expression of hsps and the amino acid sequence of several hsps cellular responses to stress is currently unclear, due in part to are highly conserved throughout evolution, implying that they a variety of experimental findings that are apparently contra may have some universally important function(s). It is com dictory. The purpose of this review is to evaluate the evidence monly accepted that the function of the hsps is either to protect regarding the role of lisps-' in cellular responses to stress and to cells against subsequent heat stress or to enhance the ability of speculate on other possible physiological functions of these cells to recover from the toxic effects of heat or other stresses. unique proteins. This Perspectives article evaluates current evidence regarding Over the past 10 years, hyperthermia has gained increasing this possible role of hsps and considers alternate effects of hsps acceptance as a mode of cancer treatment, especially when used on cellular physiological responses. in combination with radiotherapy (1). In 1985, the United States Food and Drug Administration formally recognized hy perthermia therapy, generally meaning the elevation of tumor Operational Definitions of hsps and Thermotolerance temperatures to 40-45°C, as an effective form of treatment for certain types of cancer. -
Dietary Nutrients and Bioactive Substances Modulate Heat Shock Protein (HSP) Expression: a Review
nutrients Review Dietary Nutrients and Bioactive Substances Modulate Heat Shock Protein (HSP) Expression: A Review Carolina Soares Moura 1,* ID , Pablo Christiano Barboza Lollo 2, Priscila Neder Morato 2 and Jaime Amaya-Farfan 1 ID 1 Protein Resources Laboratory, Food and Nutrition Department, Faculty of Food Engineering, University of Campinas (UNICAMP), Campinas 13083-862 São Paulo, Brazil; [email protected] 2 School of Health Sciences, Federal University of Grande Dourados, Dourados 79825-070, Mato Grosso do Sul, Brazil; [email protected] (P.C.B.L.); [email protected] (P.N.M.) * Correspondence: [email protected]; Tel.: +55-19-998418305 Received: 10 April 2018; Accepted: 23 May 2018; Published: 28 May 2018 Abstract: Interest in the heat shock proteins (HSPs), as a natural physiological toolkit of living organisms, has ranged from their chaperone function in nascent proteins to the remedial role following cell stress. As part of the defence system, HSPs guarantee cell tolerance against a variety of stressors, including exercise, oxidative stress, hyper and hypothermia, hyper and hypoxia and improper diets. For the past couple of decades, research on functional foods has revealed a number of substances likely to trigger cell protection through mechanisms that involve the induction of HSP expression. This review will summarize the occurrence of the most easily inducible HSPs and describe the effects of dietary proteins, peptides, amino acids, probiotics, high-fat diets and other food-derived substances reported to induce HSP response in animals and humans studies. Future research may clarify the mechanisms and explore the usefulness of this natural alternative of defense and the modulating mechanism of each substance. -
Heat Shock Proteins: Connectors Between Heart and Kidney
cells Review Heat Shock Proteins: Connectors between Heart and Kidney Carolina Victória Cruz Junho 1, Carolina Amaral Bueno Azevedo 2, Regiane Stafim da Cunha 2, Ainhoa Rodriguez de Yurre 3 , Emiliano Medei 3,4,5 , Andréa Emilia Marques Stinghen 2 and Marcela Sorelli Carneiro-Ramos 1,* 1 Center of Natural and Human Sciences (CCNH), Laboratory of Cardiovascular Immunology, Federal University of ABC, Santo André 09210-580, Brazil; [email protected] 2 Experimental Nephrology Laboratory, Basic Pathology Department, Universidade Federal do Paraná, Curitiba 81531-980, Brazil; [email protected] (C.A.B.A.); [email protected] (R.S.d.C.); [email protected] (A.E.M.S.) 3 Laboratory of Cardioimmunology, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro 21941-902, Brazil; [email protected] (A.R.d.Y.); [email protected] (E.M.) 4 D’Or Institute for Research and Education, Rio de Janeiro 21941-902, Brazil 5 National Center for Structural Biology and Bioimaging, Federal University of Rio de Janeiro, Rio de Janeiro 22281-100, Brazil * Correspondence: [email protected]; Tel.: +55-11-4996-8390 or +55-11-97501-2772 Abstract: 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.