Thu . 19 Jun 2019

Heat shock protein

heat shock protein, heat shock protein 70
Heat shock proteins HSP are a family of proteins that are produced by cells in response to exposure to stressful conditions They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light, and during wound healing or tissue remodeling Many members of this group perform chaperone function by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress This increase in expression is transcriptionally regulated The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor HSF HSPs are found in virtually all living organisms, from bacteria to humans

Heat-shock proteins are named according to their molecular weight For example, Hsp60, Hsp70 and Hsp90 the most widely studied HSPs refer to families of heat shock proteins on the order of 60, 70, and 90 kilodaltons in size, respectively The small 8-kilodalton protein ubiquitin, which marks proteins for degradation, also has features of a heat shock protein A conserved protein binding domain of approximately 80 amino-acid alpha crystallins are known as small heat shock proteins sHSP

Contents

  • 1 Discovery
  • 2 Function
    • 21 Upregulation in stress
    • 22 Role as chaperone
    • 23 Management
    • 24 Cardiovascular
    • 25 Immunity
    • 26 Lens
  • 3 Clinical significance
  • 4 Applications
    • 41 Cancer vaccine adjuvant
    • 42 Anticancer therapeutics
    • 43 Agricultural
  • 5 Classification
  • 6 See also
  • 7 References
  • 8 External links

Discovery

It is known that rapid heat hardening can be elicited by a brief exposure of cells to sub-lethal high temperature, which in turn provides protection from subsequent and more severe temperature In 1962, Italian geneticist Ferruccio Ritossa reported that heat and the metabolic uncoupler 2,4-dinitrophenol induced a characteristic pattern of "puffing" in the chromosomes of Drosophila This discovery eventually led to the identification of the heat-shock proteins HSP or stress proteins whose expression this puffing represented Increased synthesis of selected proteins in Drosophila cells following stresses such as heat shock was first reported in 1974

Beginning in the mid-1960s, investigators recognized that many HSPs function as molecular chaperones and thus play a critical role in protein folding, intracellular trafficking of proteins, and coping with proteins denatured by heat and other stresses Since that time, the study of stress proteins has undergone explosive growth

Function

According to Marvin et al sHSPs independently express not only in heat shock response but also have developmental roles in embryonic or juvenile stages of mammals, teleost fish and some lower vertebral genomes hspb1 HSP27 is expressed during stress and during the development of embryo, somites, mid-hindbrain, heart and lens in zebrafish Expression of the hspb4 gene, which codes for alpha crystallin, increases considerably in the lens in response to heat shock

Upregulation in stress

Production of high levels of heat shock proteins can also be triggered by exposure to different kinds of environmental stress conditions, such as infection, inflammation, exercise, exposure of the cell to toxins ethanol, arsenic, trace metals, and ultraviolet light, among many others, starvation, hypoxia oxygen deprivation, nitrogen deficiency in plants, or water deprivation As a consequence, the heat shock proteins are also referred to as stress proteins and their upregulation is sometimes described more generally as part of the stress response

The mechanism by which heat-shock or other environmental stressors activates the heat shock factor has been determined in bacteria During heat stress, outer membrane proteins OMPs do not fold and cannot insert correctly into the outer membrane They accumulate in the periplasmic space These OMPs are detected by DegS, an inner membrane protease, that passes the signal through the membrane to the sigmaE transcription factor However, some studies suggest that an increase in damaged or abnormal proteins brings HSPs into action

Some bacterial heat shock proteins are upregulated via a mechanism involving RNA thermometers such as the FourU thermometer, ROSE element and the Hsp90 cis-regulatory element

Role as chaperone

Several heat shock proteins function as intra-cellular chaperones for other proteins They play an important role in protein–protein interactions such as folding and assisting in the establishment of proper protein conformation shape and prevention of unwanted protein aggregation By helping to stabilize partially unfolded proteins, HSPs aid in transporting proteins across membranes within the cell

Some members of the HSP family are expressed at low to moderate levels in all organisms because of their essential role in protein maintenance

Management

Heat-shock proteins also occur under non-stressful conditions, simply "monitoring" the cell's proteins Some examples of their role as "monitors" are that they carry old proteins to the cell's "recycling bin" proteasome and they help newly synthesised proteins fold properly

These activities are part of a cell's own repair system, called the "cellular stress response" or the "heat-shock response"

Cardiovascular

Heat shock proteins appear to serve a significant cardiovascular role Hsp90, hsp84, hsp70, hsp27, hsp20, and alpha B crystallin all have been reported as having roles in the cardiovasculature

Hsp90 binds both endothelial nitric oxide synthase and soluble guanylate cyclase, which in turn are involved in vascular relaxation

Krief et al referred hspb7 cvHSP - cardiovascular Heat shock protein as cardiac heat shock protein Gata4 is an essential gene responsible for cardiac morphogenesis It also regulates the gene expression of hspb7 and hspb12 Gata4 depletion can result in reduced transcript levels of hspb7 and hspb12 and this could result in cardiac myopathies in zebrafish embryos as observed by Gabriel et al

hspb7 also acts in the downregulation of Kupffer vesicles which is responsible for regulation of left-right asymmetry of heart in zebrafish Along with hspb7, hspb12 is involved in cardiac laterality determination A kinase of the nitric oxide cell signalling pathway, protein kinase G, phosphorylates a small heat shock protein, hsp20 Hsp20 phosphorylation correlates well with smooth muscle relaxation and is one significant phosphoprotein involved in the process Hsp20 appears significant in development of the smooth muscle phenotype during development Hsp20 also serves a significant role in preventing platelet aggregation, cardiac myocyte function and prevention of apoptosis after ischemic injury, and skeletal muscle function and muscle insulin response

Hsp27 is a major phosphoprotein during women's contractions Hsp27 functions in small muscle migrations and appears to serve an integral role

Immunity

Extracellular and membrane bound heat-shock proteins, especially Hsp70 are involved in binding antigens and presenting them to the immune system

Lens

Alpha crystallin α4- crystallin or hspb4 is involved in the development of lens in Zebrafish as it is expressed in response to heat shock in the Zebrafish embryo in its developmental stages

Clinical significance

Heat shock factor 1 HSF1 is a transcription factor that is involved in the general maintenance and upregulation of Hsp70 protein expression Recently it was discovered that HSF1 is a powerful multifaceted modifier of carcinogenesis HSF1 knockout mice show significantly decreased incidence of skin tumor after topical application of DMBA 7,12-dimethylbenzanthracene, a mutagen Moreover, HSF1 inhibition by a potent RNA aptamer attenuates mitogenic MAPK signaling and induces cancer cell apoptosis

Applications

Cancer vaccine adjuvant

Given their role in antigen presentation, HSPs are useful as immunologic adjuvants in boosting the response to a vaccine Furthermore, some researchers speculate that HSPs may be involved in binding protein fragments from dead malignant cells and presenting them to the immune system Therefore, HSPs may be useful for increasing the effectiveness of cancer vaccines

Anticancer therapeutics

Intracellular heat shock proteins are highly expressed in cancerous cells and are essential to the survival of these cell types Hence small molecule inhibitors of HSPs, especially Hsp90 show promise as anticancer agents The potent Hsp90 inhibitor 17-AAG was in clinical trials for the treatment of several types of cancer, but for various reasons unrelated to efficacy did not go on to Phase 3 HSPgp96 also shows promise as an anticancer treatment and is currently in clinical trials against non-small cell lung cancer

Agricultural

Researchers are also investigating the role of HSPs in conferring stress tolerance to hybridized plants, hoping to address drought and poor soil conditions for farming Various HSPs were shown to be differentially expressed in the leaf and root of drought-tolerant and drought-sensitive sorghum varieties in response to drought

Classification

The principal heat-shock proteins that have chaperone activity belong to five conserved classes: HSP33, HSP60, HSP70, HSP90, HSP100, and the small heat-shock proteins sHSPs

Approximate molecular weight

kDa

Prokaryotic proteins Eukaryotic proteins Function
10 kDa GroES Hsp10
20–30 kDa GrpE The HspB group of Hsp Eleven members in mammals including Hsp27, HSPB6 or HspB1
40 kDa DnaJ Hsp40 Co-factor of Hsp70
60 kDa GroEL, 60kDa antigen Hsp60 Involved in protein folding after its post-translational import to the mitochondrion/chloroplast
70 kDa DnaK The HspA group of Hsp including Hsp71, Hsp70, Hsp72, Grp78 BiP, Hsx70 found only in primates Protein folding and unfolding, provides thermotolerance to cell on exposure to heat stress Also prevents protein folding during post-translational import into the mitochondria/chloroplast
90 kDa HtpG, C625 The HspC group of Hsp including Hsp90, Grp94 Maintenance of steroid receptors and transcription factors
100 kDa ClpB, ClpA, ClpX Hsp104, Hsp110 Tolerance of extreme temperature

Although the most important members of each family are tabulated here, it should be noted that some species may express additional chaperones, co-chaperones, and heat shock proteins not listed In addition, many of these proteins may have multiple splice variants Hsp90α and Hsp90β, for instance or conflicts of nomenclature Hsp72 is sometimes called Hsp70

See also

  • Biology portal
  • Molecular and cellular biology portal
  • Cellular stress response
  • Chaperone
  • Chaperonin
  • Co-chaperone
  • FourU thermometer
  • Hsp90 cis-regulatory element
  • ROSE element
  • HSF1

References

  1. ^ Ritossa F 1962 "A new puffing pattern induced by temperature shock and DNP in drosophila" Experientia 18 12: 571–573 doi:101007/BF02172188 ISSN 0014-4754 Retrieved 2014-04-27 
  2. ^ Matz JM, Blake MJ, Tatelman HM, Lavoi KP, Holbrook NJ July 1995 "Characterization and regulation of cold-induced heat shock protein expression in mouse brown adipose tissue" The American Journal of Physiology 269 1 Pt 2: R38–47 PMID 7631901 
  3. ^ Cao Y, Ohwatari N, Matsumoto T, Kosaka M, Ohtsuru A, Yamashita S August 1999 "TGF-beta1 mediates 70-kDa heat shock protein induction due to ultraviolet irradiation in human skin fibroblasts" Pflügers Archiv 438 3: 239–44 doi:101007/s004240050905 PMID 10398851 
  4. ^ Laplante AF, Moulin V, Auger FA, Landry J, Li H, Morrow G, Tanguay RM, Germain L November 1998 "Expression of heat shock proteins in mouse skin during wound healing" The Journal of Histochemistry and Cytochemistry 46 11: 1291–301 doi:101177/002215549804601109 PMID 9774628 
  5. ^ De Maio A January 1999 "Heat shock proteins: facts, thoughts, and dreams" Shock 11 1: 1–12 doi:101097/00024382-199901000-00001 PMID 9921710 
  6. ^ Wu C 1995 "Heat shock transcription factors: structure and regulation" Annual Review of Cell and Developmental Biology 11: 441–69 doi:101146/annurevcb11110195002301 PMID 8689565 
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  8. ^ Raboy B, Sharon G, Parag HA, Shochat Y, Kulka RG 1991 "Effect of stress on protein degradation: role of the ubiquitin system" Acta Biologica Hungarica 42 1–3: 3–20 PMID 1668897 
  9. ^ a b Lahvic, Jamie L; Ji, Yongchang; Marin, Paloma; Zuflacht, Jonah P; Springel, Mark W; Wosen, Jonathan E; Davis, Leigh; Hutson, Lara D; Amack, Jeffrey D 2013-12-15 "Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish" Developmental Biology 384 2: 166–180 doi:101016/jydbio201310009 ISSN 1095-564X PMC 3924900  PMID 24140541 
  10. ^ Ritossa F 1962 "A new puffing pattern induced by temperature shock and DNP in drosophila" Cellular and Molecular Life Sciences CMLS 18 12: 571–573 doi:101007/BF02172188 
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  12. ^ a b Schlesinger MJ July 1990 "Heat shock proteins" The Journal of Biological Chemistry 265 21: 12111–4 PMID 2197269 
  13. ^ a b Marvin, Martha; O'Rourke, Devon; Kurihara, Tomoki; Juliano, Courtney E; Harrison, Krista L; Hutson, Lara D February 2008 "Developmental expression patterns of the zebrafish small heat shock proteins" Developmental Dynamics: An Official Publication of the American Association of Anatomists 237 2: 454–463 doi:101002/dvdy21414 ISSN 1058-8388 PMID 18161059 
  14. ^ Santoro MG January 2000 "Heat shock factors and the control of the stress response" Biochemical Pharmacology 59 1: 55–63 doi:101016/S0006-29529900299-3 PMID 10605935 
  15. ^ Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT April 2003 "OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain" Cell 113 1: 61–71 doi:101016/S0092-86740300203-4 PMID 12679035 
  16. ^ Narberhaus F 2010 "Translational control of bacterial heat shock and virulence genes by temperature-sensing mRNAs" RNA Biology 7 1: 84–9 doi:104161/rna7110501 PMID 20009504 
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  20. ^ Antonova G, Lichtenbeld H, Xia T, Chatterjee A, Dimitropoulou C, Catravas JD 2007 "Functional significance of hsp90 complexes with NOS and sGC in endothelial cells" Clinical Hemorheology and Microcirculation 37 1–2: 19–35 PMID 17641392 Archived from the original on 2013-01-28 
  21. ^ Rosenfeld, Gabriel E; Mercer, Emily J; Mason, Christopher E; Evans, Todd 2013-09-15 "Small heat shock proteins Hspb7 and Hspb12 regulate early steps of cardiac morphogenesis" Developmental Biology 381 2: 389–400 doi:101016/jydbio201306025 ISSN 1095-564X PMC 3777613  PMID 23850773 
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  23. ^ Fan GC, Ren X, Qian J, Yuan Q, Nicolaou P, Wang Y, Jones WK, Chu G, Kranias EG April 2005 "Novel cardioprotective role of a small heat-shock protein, Hsp20, against ischemia/reperfusion injury" Circulation 111 14: 1792–9 doi:101161/01CIR000016085141872C6 PMID 15809372 
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  31. ^ Wall Street Journal article on company and FDA
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External links

  • Heat-Shock Proteins at the US National Library of Medicine Medical Subject Headings MeSH

heat shock protein, heat shock protein 60, heat shock protein 70, heat shock protein 90, heat shock protein and cancer, heat shock protein benefits, heat shock protein hot bath temperature, heat shock protein ppt, heat shock protein sauna, heat shock protein supplement


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Heat shock protein


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