Atlas of Genetics and Cytogenetics in Oncology and Haematology


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HSPB1 (Heat-Shock 27 kDa Protein 1)

Identity

Other namesHSP27
HSP28
Hsp25
CMT2F
HMN2B
SRP27
HS.76067
DKFZp586P1322
HGNC (Hugo) HSPB1
LocusID (NCBI) 3315
Location 7q11.23
Location_base_pair Starts at 75931875 and ends at 75933614 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Genes flanking HSPB1 in centromere to telomere direction:
- MDH2 (mitochondrial malate dehydrogenase precursor)
- FLJ37078 (hypothetical protein LOC222183)
- HSPB1
- YWHAG (tyrosine 3-monooxygenase/tryptophan)
- SRCRB40 (scavenger receptor cysteine-rich domain-containing group B protein precursor)

DNA/RNA

Description The DNA sequence (1.69 Kb) contains 3 exons.
Transcription The transcript is 847 bp.
Pseudogene Two pseudogenes have been identified:
- a processed retropseudogene lacking promoter elements on Xp11.23 (Hickey et al., 1996);
- a 5'-truncated semiprocessed retropseudogene on 9q13-9q21 (Kappe et al., 2003).

Protein

Note HspB1 belongs to the ubiquitous family of small heat shock proteins (sHsps). sHsps are characterized by low molecular mass (12-30 kDa), a conserved C-terminal "a-crystallin" domain and oligomeric structure. sHsps bind denatured proteins and facilitate their refolding by the ATP-dependent molecular chaperones of the Hsp70 family (Haslbeck et al., 2005; Sun and MacRae, 2005).
 
  Fig.1. HspB1 contains an N-terminal hydrophobic domain with a WDFP motif and an alpha-crystallin domain at residues Glu87-Pro168. The arrows indicate phosphorylation sites at serines 15, 78 and 82.
Description HspB1 is a protein of 205 amino acids (22783 Da), which can be phosphorylated at serines 15, 78 and 82 by mitogen- activated protein kinases associated protein kinases (MAPKAP kinase 2, MAPKAP kinase 3). Various signals modulate HspB1 phosphorylation: growth factors, tumor necrosis factor, differentiating agents, heat and oxidative stress (Arrigo et al., 2007). HspB1 forms oligomers up to 1000 kDa, which are dynamic structures. Phosphorylation results in a decrease size of the oligomers (Kato et al., 1994; Rogalla et al., 1999). Dissociation of the oligomers is required for recognition of protein substrates (Shashidharamurthy et al., 2005). It has been reported that HspB1 forms heterooligomers with other sHsps: alphaB-crystallin (HspB5) and Hsp20 (HspB6) (Zantema et al., 1992; Sugiyama et al., 2000; Bukach et al., 2009).
Expression Ubiquitous, produced constutively at high levels in heart and skeletal muscles (Sugiyama et al., 2000); overexpressed in response to a wide variety of physiological and environmental insults; produced at high levels in many tumors (Garrido et al., 2006). Increased expression of HspB1 in response to the aggregation of proteins specific for conformational diseases have been reported by several authors (Outeiro et al., 2006; Vleminckx et al., 2002).
Localisation Cytosol, nucleus. HspB1 has been identified as a component of the nuclear speckles, structures implied in RNA processing (Bryantsev et al., 2007).
HspB1 interacts with actin, intermediat filaments and microtubules (Landry and Huot, 1995; Mounier and Arrigo, 2002; Lee et al., 2005; Hino et al., 2000; Jonak et al., 2002). During ischemia in muscles, HspB1 is translocated from the cytosol to myofibryls (Golenhoffen et al., 2004).
HspB1 accumulates in protein aggregates associated with conformational diseases: Parkinson's disease (Outeiro et al., 2006; Zourlidou et al., 2004), Alexander disease (Iwaki et al., 1993), Alzheimer's disease (Wilhelmus et al., 2006).
HspB1 was also detected as a surface membrane protein in some cancer cell types (Shin et al., 2003).
Function HspB1 acts as an ATP-independent molecular chaperone and prevents irreversible aggregation of bound substrates in vitro (Jakob et al., 1993).
HspB1 is involved in the remodeling of cytoskeleton during embryogenesis and protection of the cytoskeleton in cells exposed to various stresses, particularly in the skeletal and cardiac muscles (Mounier and Arrigo, 2002; Sugiyama et al., 2000; Golenhofen et al., 2004; Salinthone et al., 2008). HspB1 phosphorylated by p38 MAP kinase is necessary for migration of vascular smooth muscle cells, neutrophils, fibroblasts and breast epithelial cells (Salinthone et al., 2008).
HspB1 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes (Cuesta et al., 2000).
HspB1 interacts with different proteins of the programmed cell death machinery and thereby blocks apoptosis at distinct key points. It has been demonstrated that HspB1 sequesters cytochrome C and thus, prevents assembly of the apoptosome (Bruey et al., 2000a; Concannon et al., 2001). The release of Smac/Diablo from mitochondria is also blocked by HspB1 (Chauhan et al., 2003). In addition, HspB1 inhibits activation of procaspase-3 by caspase 9 (Garrido et al., 1999; Concannon et al., 2001). HspB1 prevents translocation of pro-apoptotic Bid to mitochondria by stabilization of actin microfilaments (Paul et al., 2002). Havasi et al. (2008) demonstrated that HspB1 inhibits activation of pro-apoptotic Bax protein via a phosphatidylinositol 3-kinase-dependent mechanism. In the extrinsic pathway (receptor-mediated cell death) HspB1 prevents interaction of DAXX (death domain associated protein) with Fas death receptor and protein kinase Ask1 in caspase-independent pathway (Charette et al., 2000). It has been reported by Rane et al. (2003) that HspB1 controls apoptosis by binding cytoprotective protein kinase B (Akt). Anti-oxidant properties of HspB1 play an important function in the regulation of apoptosis. HspB1 maintain glutathione in its reduced form and decrease the amount of reactive oxygen species (ROS) produced in cells exposed to oxidative stress or tumor necrosis factor TNFalpha (Arrigo et al., 2007). HspB1 may indirectly affect apoptosis by promoting degradation of death regulatory proteins by ubiquitin-proteasome pathway. Under stress conditions HspB1 stimulates ubiquitination of I-kappaBalpha, an inhibitor of the anti-apoptotic transcription factor NF-kappaB, and p27Kip1, a cyclin-dependent kinase inhibitor. The HspB1- mediated proteolysis of p27Kip1 facilitates progression from Go/G1 to S-phase of the cell cycle (Parcellier et al., 2006).
In cancer cells HspB1 participates in oncogenesis and resistance to chemotherapy (see below). It has also been reported that expression of recombinant HspB1 at elevated levels leads to protection of human mammary epithelial cells from doxorubicin. The protection is associated with suppression of the doxorubicin-induced senescence, where HspB1 inhibits p53-mediated induction of p21 (O'Callaghan-Sunol et al., 2007). However, Venkatakrishnan and co-workers (2008) demonstrated that HspB1 causes p21 upregulation and G2/M phase cell cycle arrest in doxorubicin-treated fibroblasts.
Homology HspB1 shares homology trough the conserved alpha-crystallin domain with other members of the sHsps family. Eleven human sHsps have been identified so far: HspB1 (Hsp27) HspB2, HspB3, alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), Hsp20 (HspB6), cvHsp (HspB7), HspB8 (H11), HspB9, HspB10 (ODF1) and Hsp16.2 (Kappe et al., 2003; Bellyei et al., 2007).

Mutations

 
  Fig2. Distribution of HSPB1 mutations in dHMN II and CMT2F patients.
dHMN: distal hereditary motor neuropathy, CMT: Charcot-Marie-Tooth type 2F disease, AD: autosomal dominant, AR: autosomal recessive.
Germinal Mutations in the HSPB1 gene were found to cause distal hereditary motor neuropathy type II (dHMN II) or Charcot-Marie-Tooth disease type 2F (CMT2F). Five of the mutations are located in the alpha-crystallin domain (see figure 2).
Dierick and co-workers (2007) identified a HSPB1 promoter variant (c.-217T>C) in an ALS patient, which drastically impaired the HSPB1 heat shock response.
Somatic Not known.

Implicated in

Entity Various cancers
Disease Increased levels of HspB1 have been detected in breast cancer, ovarian cancer, osteosarcomas, endometrial cancer and leukemias (Garrido et al., 2006; Ciocca and Calderwood, 2005). It was also reported that the pattern of HspB1 phosphorylation in tumor cells is different from that observed in nontransformed cells (Sarto et al., 2004; Tremolada et al., 2005).
Prognosis Overexpression of HspB1 correlates with poor prognosis in gastric, liver, prostate carcinoma and osteosarcomas (Glaessgen et al., 2008; Romani et al., 2007; Ciocca and Calderwood., 2005).
Increased IbpB1 expression is associated with a favorable prognosis in schistosomiasis-associated bladder carcinoma (El-Meghawry El-Kenawy et al., 2008), neuroblastoma (Zanini et al., 2007) and non-small cell lung carcinoma (Malusecka et al., 2008).
Patients with reduced HspB1 expression have poorer survival rates in oral squamous cell carcinoma (Lo Muzio et al., 2004) and ovarian carcinoma (Geisler et al., 2004).
Lower lymphocyte HspB1 level is associated with an increased risk of lung cancer (Wang et al., 2008).
Cytogenetics Not reported.
Hybrid/Mutated Gene Not known.
Abnormal Protein Not known.
Oncogenesis HspB1 is involved in oncogenesis and resistance to various anti-cancer therapies due to its cytoprotective activities. It is suggested that HspB1 plays a crucial function during metastasis formation (Zhao et al., 2007).
Strategies combining chemo- or radiotherapy with down-regulation of HspB1 have been proposed as effective anti-cancer treatments. The HspB1 knockdown by using small interfering RNA (siRNA) increases sensitivity of human epithelial cells to geldanamycin (McCollum et al., 2006) and pancreatic cancer cells to gemcitabine (Mori-Iwamoto et al., 2007). Blocking HspB1 by antisense RNA restores apoptosis induced by drugs in multiple myeloma cells (Chauhan et al., 2003) and human bladder cancer cells (Kamada et al., 2007). Various cancer cells transfected with antisense Hsp27 cDNA exhibits increased sensitivity to gamma-irradiation (Aloy et al., 2008). Down regulation of HspB1 by interferon C enhances drug sensitivity in oral squamous cell carcinoma (Yonekura et al., 2003). Kim et al. (2007) has demonstrated that a heptapeptide derived from protein kinase C delta (PKC delta)-V5 region sequesters HspB1 and sensitizes human cancer cells to irradiation and cisplatine.
  
Entity Charcot-Marie-Tooth type IIF disease (CMT-IIF) / distal hereditary motor neuropathy (dHMN)
Note A number of mutations in HspB1 has been identified that are associated with dHMNII or CMT2F (table of figure 2). The exact pathogenic mechanism of the HspB1 mutations is not yet understood. Expression of the mutant HspB1 (P182S) results in the formation of insoluble aggregates, affects assembly of neurofilament network and axonal transport in cortical neurons (Ackerley et al., 2006; Evgrafov et al., 2004; Zhai et al., 2007).
Disease CMT disease and dHMN belong to a clinically heterogeneous group of disorders characterized by progressive weakness and distal limb muscle atrophy due to nerve degeneration. The neuropathy of CMT affects both motor and sensory nerves. The phenotype of dHMN II resembles CMT2F, but sensory abnormalities are absent in dHMNII.
  
Entity Conformational disorders
Disease One of the characteristics of neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), amylotrophic lateral sclerosis (ALS) and Huntington disease is the formation of protein aggregates. HspB1 and other molecular chaperones are often detected as components of these aggregates.
Cerebral deposits of intracellular neurofibrylllary tangles and extracellular aggregates of amyloid beta peptide (Abeta) are the pathological hallmarks of Alzheimer's disease. Intracellular Lewy bodies associated with Parkinson's disease contain alpha-synuclein. In Huntington's disease (HD), a proteolytic fragment of the huntingtin protein that contains an expanded polyglutamine tract (polyQ), misfolds and forms aggregates. Rosenthal fibers of Alexander disease are cytoplasmic inclusions within astrocytes, which contain glial fibrillary acidic protein (GFAP) (Iwaki et al., 1993; Der Perng et al., 2006).
Numerous studies indicate that molecular chaperones associated with intra- and extracellular protein deposits, affects their production and toxicity.
It has been reported that HspB1 inhibits assembly of Abeta fibryls in vitro and reduces cerebrovascular toxicity of Abeta (Wilhelmus et al., 2006). HspB1 also inhibits GFAP polymerization (Der Perng et al., 2006) and toxicity induced by overexpression of alpha-synuclein or polyQ in neuronal cells (Outeiro et al., 2006; Zourlidou et al., 2004; Wyttenbach et al., 2002). It is proposed that the sequestering of HspB1 by Rosenthal fibers diminishes its function as an anti-apoptotic factor which in turn results in astrocytes degeneration (Mignot et al., 2004). Similarly, association of HspB1 with mutated Cu/Zn superoxide dismutase 1 (SOD1) may induce apoptosis (Okado-Matsumoto and Fridovich, 2002). Missense mutations in the gene coding for SOD1 cause familial cases of amyotrophic lateral sclerosis (ALS) characterized by the death of large motor neurons in the cerebral cortex and spinal cord (Rakhit and Chakrabartty, 2006).
  
Entity Williams syndrome
Note Stock et al. (2003) used FISH to map the HspB1 gene and they found that the band 7q11.23 also contains the site of the deletion associated with Williams sydrome (WS). The HSPB1 gene was deleted in three out of six WS patients examined in this study.
Disease Williams syndrome (WS, also known as Williams- Beuren syndrome, WBS) is a rare neurodevelopmental disorder characterized by multiple anomalies including: typical facial dysmorphisms (elfin face), congenital heart defects, infantile hypercalcemia, mental retardation and growth deficiency.
  

External links

Nomenclature
HGNC (Hugo)HSPB1   5246
Cards
AtlasHSPB1ID40880ch7q11
Entrez_Gene (NCBI)HSPB1  3315  heat shock 27kDa protein 1
GeneCards (Weizmann)HSPB1
Ensembl (Hinxton)ENSG00000106211 [Gene_View]  chr7:75931875-75933614 [Contig_View]  HSPB1 [Vega]
ICGC DataPortalENSG00000106211
cBioPortalHSPB1
AceView (NCBI)HSPB1
Genatlas (Paris)HSPB1
WikiGenes3315
SOURCE (Princeton)NM_001540
Genomic and cartography
GoldenPath (UCSC)HSPB1  -  7q11.23   chr7:75931875-75933614 +  7q11.23   [Description]    (hg19-Feb_2009)
EnsemblHSPB1 - 7q11.23 [CytoView]
Mapping of homologs : NCBIHSPB1 [Mapview]
OMIM602195   606595   608634   
Gene and transcription
Genbank (Entrez)AB020027 AK296890 AK311446 AK311894 AL050380
RefSeq transcript (Entrez)NM_001540
RefSeq genomic (Entrez)AC_000139 NC_000007 NC_018918 NG_008995 NT_007933 NW_001839047 NW_004929332
Consensus coding sequences : CCDS (NCBI)HSPB1
Cluster EST : UnigeneHs.520973 [ NCBI ]
CGAP (NCI)Hs.520973
Alternative Splicing : Fast-db (Paris)GSHG0027465
Alternative Splicing GalleryENSG00000106211
Gene ExpressionHSPB1 [ NCBI-GEO ]     HSPB1 [ SEEK ]   HSPB1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP04792 (Uniprot)
NextProtP04792  [Medical]
With graphics : InterProP04792
Splice isoforms : SwissVarP04792 (Swissvar)
Domaine pattern : Prosite (Expaxy)HSP20 (PS01031)   
Domains : Interpro (EBI)a-crystallin/Hsp20_dom [organisation]   Alpha-crystallin/HSP [organisation]   HSP20-like_chaperone [organisation]  
Related proteins : CluSTrP04792
Domain families : Pfam (Sanger)HSP20 (PF00011)   
Domain families : Pfam (NCBI)pfam00011   
DMDM Disease mutations3315
Blocks (Seattle)P04792
PDB (SRS)3Q9P    3Q9Q    4MJH   
PDB (PDBSum)3Q9P    3Q9Q    4MJH   
PDB (IMB)3Q9P    3Q9Q    4MJH   
PDB (RSDB)3Q9P    3Q9Q    4MJH   
Human Protein AtlasENSG00000106211 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasP04792
HPRD09076
IPIIPI00025512   IPI00909453   IPI00924436   
Protein Interaction databases
DIP (DOE-UCLA)P04792
IntAct (EBI)P04792
FunCoupENSG00000106211
BioGRIDHSPB1
InParanoidP04792
Interologous Interaction database P04792
IntegromeDBHSPB1
STRING (EMBL)HSPB1
Ontologies - Pathways
Ontology : AmiGOproteasome complex  retina homeostasis  protein kinase C binding  protein binding  extracellular space  nucleus  cytoplasm  cytoplasm  spindle  cytosol  cytoskeleton  plasma membrane  regulation of translational initiation  negative regulation of protein kinase activity  cellular component movement  response to unfolded protein  cell death  protein kinase C inhibitor activity  response to virus  gene expression  RNA metabolic process  mRNA metabolic process  protein kinase binding  Z disc  positive regulation of interleukin-1 beta production  intracellular signal transduction  cellular response to vascular endothelial growth factor stimulus  positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway  positive regulation of tumor necrosis factor biosynthetic process  identical protein binding  negative regulation of apoptotic process  regulation of I-kappaB kinase/NF-kappaB signaling  ubiquitin binding  positive regulation of blood vessel endothelial cell migration  poly(A) RNA binding  positive regulation of angiogenesis  extracellular vesicular exosome  negative regulation of protein serine/threonine kinase activity  negative regulation of protein serine/threonine kinase activity  negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  positive regulation of endothelial cell chemotaxis  
Ontology : EGO-EBIproteasome complex  retina homeostasis  protein kinase C binding  protein binding  extracellular space  nucleus  cytoplasm  cytoplasm  spindle  cytosol  cytoskeleton  plasma membrane  regulation of translational initiation  negative regulation of protein kinase activity  cellular component movement  response to unfolded protein  cell death  protein kinase C inhibitor activity  response to virus  gene expression  RNA metabolic process  mRNA metabolic process  protein kinase binding  Z disc  positive regulation of interleukin-1 beta production  intracellular signal transduction  cellular response to vascular endothelial growth factor stimulus  positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway  positive regulation of tumor necrosis factor biosynthetic process  identical protein binding  negative regulation of apoptotic process  regulation of I-kappaB kinase/NF-kappaB signaling  ubiquitin binding  positive regulation of blood vessel endothelial cell migration  poly(A) RNA binding  positive regulation of angiogenesis  extracellular vesicular exosome  negative regulation of protein serine/threonine kinase activity  negative regulation of protein serine/threonine kinase activity  negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  positive regulation of endothelial cell chemotaxis  
Pathways : BIOCARTAStress Induction of HSP Regulation [Genes]    Downregulated of MTA-3 in ER-negative Breast Tumors [Genes]    p38 MAPK Signaling Pathway [Genes]   
Pathways : KEGGMAPK signaling pathway    VEGF signaling pathway    Amoebiasis    Epstein-Barr virus infection   
Protein Interaction DatabaseHSPB1
Wikipedia pathwaysHSPB1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)HSPB1
snp3D : Map Gene to Disease3315
SNP (GeneSNP Utah)HSPB1
SNP : HGBaseHSPB1
Genetic variants : HAPMAPHSPB1
Exome VariantHSPB1
1000_GenomesHSPB1 
ICGC programENSG00000106211 
Somatic Mutations in Cancer : COSMICHSPB1 
CONAN: Copy Number AnalysisHSPB1 
Mutations and Diseases : HGMDHSPB1
Mutations and Diseases : intOGenHSPB1
Genomic VariantsHSPB1  HSPB1 [DGVbeta]
dbVarHSPB1
ClinVarHSPB1
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM602195    606595    608634   
MedgenHSPB1
GENETestsHSPB1
Disease Genetic AssociationHSPB1
Huge Navigator HSPB1 [HugePedia]  HSPB1 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneHSPB1
Homology/Alignments : Family Browser (UCSC)HSPB1
Phylogenetic Trees/Animal Genes : TreeFamHSPB1
Chemical/Protein Interactions : CTD3315
Chemical/Pharm GKB GenePA29511
Clinical trialHSPB1
Cancer Resource (Charite)ENSG00000106211
Other databases
Probes
Litterature
PubMed352 Pubmed reference(s) in Entrez
CoreMineHSPB1
iHOPHSPB1
OncoSearchHSPB1

Bibliography

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PMID 11444529
 
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PMID 11784858
 
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PMID 12430713
 
Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin.
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PMID 11978772
 
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Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function.
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Histochem Cell Biol. 2004 Nov;122(5):415-25. Epub 2004 Oct 12.
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HSP 27 as possible prognostic factor in patients with oral squamous cell carcinoma.
Lo Muzio L, Leonardi R, Mariggio MA, Mignogna MD, Rubini C, Vinella A, Pannone G, Giannetti L, Serpico R, Testa NF, De Rosa G, Staibano S.
Histol Histopathol. 2004 Jan;19(1):119-28.
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Alexander disease: putative mechanisms of an astrocytic encephalopathy.
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Cell Mol Life Sci. 2004 Feb;61(3):369-85. (REVIEW)
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Expression of heat shock protein 27 in human renal cell carcinoma.
Sarto C, Valsecchi C, Magni F, Tremolada L, Arizzi C, Cordani N, Casellato S, Doro G, Favini P, Perego RA, Raimondo F, Ferrero S, Mocarelli P, Galli-Kienle M.
Proteomics. 2004 Aug;4(8):2252-60.
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HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells.
Zourlidou A, Payne Smith MD, Latchman DS.
J Neurochem. 2004 Mar;88(6):1439-48.
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Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications.
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Cell Stress Chaperones. 2005 Summer;10(2):86-103.
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Nat Struct Mol Biol. 2005 Oct;12(10):842-6.
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Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium.
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Exp Mol Med. 2005 Oct 31;37(5):427-35.
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FEBS J. 2005 Jun;272(11):2613-27.
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Mutation analysis of the small heat shock protein 27 gene in chinese patients with Charcot-Marie-Tooth disease.
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Arch Neurol. 2005 Aug;62(8):1201-7.
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Characterization of heat shock protein 27 phosphorylation sites in renal cell carcinoma.
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Proteomics. 2005 Feb;5(3):788-95.
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A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes.
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Hum Mol Genet. 2006 Jan 15;15(2):347-54. Epub 2005 Dec 20.
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The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27.
Der Perng M, Su M, Wen SF, Li R, Gibbon T, Prescott AR, Brenner M, Quinlan RA.
Am J Hum Genet. 2006 Aug;79(2):197-213. Epub 2006 Jun 12.
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Cell Cycle. 2006 Nov;5(22):2592-601. Epub 2006 Nov 15.
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Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism.
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Cancer Res. 2006 Nov 15;66(22):10967-75.
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Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation.
Outeiro TF, Klucken J, Strathearn KE, Liu F, Nguyen P, Rochet JC, Hyman BT, McLean PJ.
Biochem Biophys Res Commun. 2006 Dec 22;351(3):631-8. Epub 2006 Oct 26.
PMID 17081499
 
HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells.
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FASEB J. 2006 Jun;20(8):1179-81. Epub 2006 Apr 26.
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Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.
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Biochim Biophys Acta. 2006 Nov-Dec;1762(11-12):1025-37. Epub 2006 May 22.
PMID 16814528
 
Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains.
Wilhelmus MM, Otte-Holler I, Wesseling P, de Waal RM, Boelens WC, Verbeek MM.
Neuropathol Appl Neurobiol. 2006 Apr;32(2):119-30.
PMID 16599941
 
Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets.
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FEBS Lett. 2007 Jul 31;581(19):3665-74. Epub 2007 Apr 24. (REVIEW)
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Inhibition of cell death by a novel 16.2 kD heat shock protein predominantly via Hsp90 mediated lipid rafts stabilization and Akt activation pathway.
Bellyei S, Szigeti A, Boronkai A, Pozsgai E, Gomori E, Melegh B, Janaky T, Bognar Z, Hocsak E, Sumegi B, Gallyas F Jr.
Apoptosis. 2007 Jan;12(1):97-112.
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Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells.
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Biochem J. 2007 Nov 1;407(3):407-17.
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Genetic variant in the HSPB1 promoter region impairs the HSP27 stress response.
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Hum Mutat. 2007 Aug;28(8):830.
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Hsp27 knockdown using nucleotide-based therapies inhibit tumor growth and enhance chemotherapy in human bladder cancer cells.
Kamada M, So A, Muramaki M, Rocchi P, Beraldi E, Gleave M.
Mol Cancer Ther. 2007 Jan;6(1):299-308. Epub 2007 Jan 11.
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Inhibition of heat shock protein 27-mediated resistance to DNA damaging agents by a novel PKC delta-V5 heptapeptide.
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Cancer Res. 2007 Jul 1;67(13):6333-41.
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Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine.
Mori-Iwamoto S, Kuramitsu Y, Ryozawa S, Mikuria K, Fujimoto M, Maehara S, Maehara Y, Okita K, Nakamura K, Sakaida I.
Int J Oncol. 2007 Dec;31(6):1345-50.
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Hsp27 modulates p53 signaling and suppresses cellular senescence.
O'Callaghan-Sunol C, Gabai VL, Sherman MY.
Cancer Res. 2007 Dec 15;67(24):11779-88.
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The expression of HSP27 is associated with poor clinical outcome in intrahepatic cholangiocarcinoma.
Romani AA, Crafa P, Desenzani S, Graiani G, Lagrasta C, Sianesi M, Soliani P, Borghetti AF.
BMC Cancer. 2007 Dec 21;7:232.
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Disruption of neurofilament network with aggregation of light neurofilament protein: a common pathway leading to motor neuron degeneration due to Charcot-Marie-Tooth disease-linked mutations in NFL and HSPB1.
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Hum Mol Genet. 2007 Dec 15;16(24):3103-16. Epub 2007 Sep 19.
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Differential proteomic analysis of human colorectal carcinoma cell lines metastasis-associated proteins.
Zhao L, Liu L, Wang S, Zhang YF, Yu L, Ding YQ.
J Cancer Res Clin Oncol. 2007 Oct;133(10):771-82. Epub 2007 May 15.
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Protective role of Hsp27 protein against gamma radiation-induced apoptosis and radiosensitization effects of Hsp27 gene silencing in different human tumor cells.
Aloy MT, Hadchity E, Bionda C, Diaz-Latoud C, Claude L, Rousson R, Arrigo AP, Rodriguez-Lafrasse C.
Int J Radiat Oncol Biol Phys. 2008 Feb 1;70(2):543-53. Epub 2007 Nov 5.
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Distal hereditary motor neuropathy in Korean patients with a small heat shock protein 27 mutation.
Chung KW, Kim SB, Cho SY, Hwang SJ, Park SW, Kang SH, Kim J, Yoo JH, Choi BO.
Exp Mol Med. 2008 Jun 30;40(3):304-12.
PMID 18587268
 
Heat shock protein expression independently predicts survival outcome in schistosomiasis-associated urinary bladder cancer.
El-Meghawry El-Kenawy A, El-Kott AF, Hasan MS.
Int J Biol Markers. 2008 Oct-Dec;23(4):214-8.
PMID 19199268
 
Heat shock proteins 27, 60 and 70 as prognostic markers of prostate cancer.
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APMIS. 2008 Oct;116(10):888-95.
PMID 19132982
 
Hsp27 inhibits Bax activation and apoptosis via a phosphatidylinositol 3-kinase-dependent mechanism.
Havasi A, Li Z, Wang Z, Martin JL, Botla V, Ruchalski K, Schwartz JH, Borkan SC.
J Biol Chem. 2008 May 2;283(18):12305-13. Epub 2008 Feb 25.
PMID 18299320
 
Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2.
Houlden H, Laura M, Wavrant-De Vrieze F, Blake J, Wood N, Reilly MM.
Neurology. 2008 Nov 18;71(21):1660-8. Epub 2008 Oct 1.
PMID 18832141
 
Stress proteins HSP27 and HSP70i predict survival in non-small cell lung carcinoma.
Malusecka E, Krzyzowska-Gruca S, Gawrychowski J, Fiszer-Kierzkowska A, Kolosza Z, Krawczyk Z.
Anticancer Res. 2008 Jan-Feb;28(1B):501-6.
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Small heat shock proteins in smooth muscle.
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Pharmacol Ther. 2008 Jul;119(1):44-54. Epub 2008 May 16.
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HSP27 regulates p53 transcriptional activity in doxorubicin-treated fibroblasts and cardiac H9c2 cells: p21 upregulation and G2/M phase cell cycle arrest.
Venkatakrishnan CD, Dunsmore K, Wong H, Roy S, Sen CK, Wani A, Zweier JL, Ilangovan G.
Am J Physiol Heart Circ Physiol. 2008 Apr;294(4):H1736-44. Epub 2008 Feb 8.
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Proteomic identification of heat shock protein 27 as a differentiation and prognostic marker in neuroblastoma but not in Ewing's sarcoma.
Zanini C, Pulera F, Carta F, Giribaldi G, Mandili G, Maule MM, Forni M, Turrini F.
Virchows Arch. 2008 Feb;452(2):157-67. Epub 2007 Dec 8.
PMID 18066588
 
Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20).
Bukach OV, Glukhova AE, Seit-Nebi AS, Gusev NB.
Biochim Biophys Acta. 2009 Mar;1794(3):486-95. Epub 2008 Dec 3.
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A clinical phenotype of distal hereditary motor neuronopathy type II with a novel HSPB1 mutation.
Ikeda Y, Abe A, Ishida C, Takahashi K, Hayasaka K, Yamada M.
J Neurol Sci. 2009 Feb 15;277(1-2):9-12. Epub 2008 Oct 25.
PMID 18952241
 
The level of Hsp27 in lymphocytes is negatively associated with a higher risk of lung cancer.
Wang F, Feng M, Xu P, Xiao H, Niu P, Yang X, Bai Y, Peng Y, Yao P, Tan H, Tanguay RM, Wu T.
Cell Stress Chaperones. 2009 May;14(3):245-251. Epub 2008 Sep 18.
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Contributor(s)

Written03-2009Ewa Laskowska, Dorota Kuczyńska-Wiśnik, Ewelina Matuszewska
Department of Biochemistry, University of Gdańsk, Kładki 24, 80-952 Gdańsk, Poland

Citation

This paper should be referenced as such :
Laskowska, E ; Kuczyska-Wiik, D ; Matuszewska, E
HSPB1 (Heat-Shock 27 kDa Protein 1)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(2):-.
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