HSPD1 (Heat Shock 60kDa Protein 1)
2014-10-01 Cappello Francesco , Conway de Macario Everly , Macario Alberto JL AffiliationIdentity
HGNC
LOCATION
2q33.1
IMAGE
LEGEND
Hsp60 and Hsp10 protein/gene/genomic data.
LOCUSID
ALIAS
CPN60,GROEL,HLD4,HSP-60,HSP60,HSP65,HuCHA60,SPG13
FUSION GENES
Abstract
The HSPD1 gene encodes a protein known as HSP60 or Hsp60, also commonly referred to as Cpn60. This protein is a molecular chaperone typically localized inside mitochondria where it forms a chaperoning machine with HSP10 (encoded by the HSPE1 gene), also called Cpn10, to assist protein folding inside the organelle. Hsp60 also occurs in the cytosol, plasma-cell membrane, intercellular space, and blood. Its functions in all these extramitochondrial locations are poorly understood. While the canonical functions of Hsp60 are considered to be cytoprotective, anti-stress and maintenance of protein homeostasis, other roles are currently being investigated. For example, Hsp60 participates in the pathogenesis of diseases in various ways in certain types of cancer, and chronic inflammatory and autoimmune pathological conditions. These are considered chaperonopathies by mistake, in which a normal chaperone (normal at least as far as it can be determined by current methods to study the structure of a molecule available only at extremely low concentrations and quantities) turns against the organism instead of protecting it, favouring the growth and dissemination of cancer cells, or the initiation-progression of inflammation, for instance. In addition, Hsp60 mutations cause at least two types of severe genetic chaperonopathies. All this knowledge is expanding nowadays clearly pointing to Hsp60 as a potential target for chaperonotherapy by replacement when it is defective or by inhibition when it is pathogenic.
DNA/RNA
The human hsp60 genes and pseudogenes: genomic data. Source: Mukherjee et al. BMC Evolutionary Biology 2010 10:64. PMID 20193073
Description
The human HSP60 gene (HSPD1) contains 12 exons and 11 introns and was predicted to span over approximately 13 kb of the genomic DNA. The first exon is non-coding region (Hansen et al., 2003; Mukherjee et al., 2010).
Transcription
Two transcript variants encoding the same protein have been identified for HSPD1 http://www.ncbi.nlm.nih.gov/gene/3329; Mukherjee et al., 2010).
Pseudogene
Twelve pseudogenes located on chromosome 3, 4, 5, 6, 8 and 12 have been associated with HSP60 (Mukherjee et al., 2010).
Proteins
The molecular anatomy of the human Hsp60: structural domains.
Left: The anatomy of the human Hsp60: structural domains. The cartoon represents a three-dimensional model of the human Hsp60 monomer showing its three structural domains: apical in green, intermediate in yellow and equatorial in red. Right: This picture presents the ATP and Mg+/K+ binding sites on Hsp60. Particularly it shows two highly conserved sequences: 52-DGVTVAKEI-60 (orange-brown), and 85-AGDGTTTATVL-95 (magenta) corresponding to the binding sites for Mg+/K+ (green and yellow spheres, respectively) and ATP/ADP (red). Source: Cappello et al., Expert Opin Ther Targets. 2014 ; 18 (2) : 185-208. PMID 24286280.
Description
The HSP60 consists of 573 amino acids corresponding to a molecular weight of 61.05 kDa (Mukherjee et al., 2010). The HSP60 protein are abundant proteins of eubacteria genomes and mitochondria in eukaryotes, and also occurs in other locations, such as the cellular cytosol, plasma-cell membrane, and extracellular space (including blood) in eukaryotic organisms.
HSP60 belongs to the chaperone subgroup called chaperonins, of which two varieties are known: chaperonins of Group I and chaperonins of Group II. The former include the human HSP60 typically present in the mitochondria (but also occurring in other locations as described above) and the bacterial GroEL. Chaperonins of Group II include the archaeal thermosome subunits and the cytosolic chaperonin CCT (Chaperonin-containing TCP-1). The human HSP60 and the bacterial GroEL form oligomers: seven monomers associate to form a ring and two rings associate end to end to build a large chaperoning machine of fourteen subunits, all identical. This tetradecamer is the HSP60 functional chaperoning complex that associates with Hsp60 and requires ATP and ATPase activity for the folding of substrates (Cappello et al., 2014).
HSP60 belongs to the chaperone subgroup called chaperonins, of which two varieties are known: chaperonins of Group I and chaperonins of Group II. The former include the human HSP60 typically present in the mitochondria (but also occurring in other locations as described above) and the bacterial GroEL. Chaperonins of Group II include the archaeal thermosome subunits and the cytosolic chaperonin CCT (Chaperonin-containing TCP-1). The human HSP60 and the bacterial GroEL form oligomers: seven monomers associate to form a ring and two rings associate end to end to build a large chaperoning machine of fourteen subunits, all identical. This tetradecamer is the HSP60 functional chaperoning complex that associates with Hsp60 and requires ATP and ATPase activity for the folding of substrates (Cappello et al., 2014).
Expression
HSP60 expression is virtually ubiquitous, since it can be found in cells of different tissues and organs, including immune system, epithelial tissue and other cells (Cappello et al., 2011a). However, sometimes its levels can be under the threshold of detectability by immunomorphology or immunoblotting. It can also be found in the blood (Shamaei-Tousi et al., 2007).
Hsp60 presence and localization in normal tissues.
Top: Normal human bronchial mucosa. Ciliated cells present Hsp60 positivity by immunohistochemistry (IHC) in the cytosol (red spots, see arrow for example). Bottom: Normal human colonic mucosa. Intestinal cells do not show any positivity for Hsp60 at IHC, since the protein is under the threshold of detectability. Modified from: Cappello et al., Methods Mol Biol. 2011 ; 787 : 245-254. PMID 21898240
Localisation
HSP60 subcellular localization is mainly in the mitochondria, but it also occurs in extra-mitochondrial sites such as the cytosol, cell surface, peroxisomes, and the endoplasmic reticulum (Soltys and Gupta, 1996; Soltys and Gupta, 1999; Gupta et al., 2008). Levels of extramitochondrial localization increase during inflammatory states (Rodolico et al., 2010; Tomasello et al., 2011; Cappello et al., 2011b) and tumorigenesis (Cappello et al., 2008; Cappello et al., 2011c; Campanella et al., 2012; Rappa et al., 2012).
Hsp60 localization localization in pathologic tissues.
Top: Epithelial cell of inflamed colonic mucosa (patient with ulcerative colitis) showing Hsp60 positivity (immunogold) in cytosol (arrows). Modfied from Tomasello et al., 2011). Bottom: Pulmonary mucoepidermoid carcinoma cell (H292) showing Hsp60 positivity (immunogold) in cytosol and at plasma-cell membrane level (arrows). Inset: a classical mitochondrial positivity for Hsp60.
Modified from Campanella et al., PLoS One. 2012 ; 7 (7) : e42008. PMID 22848686
Function
Assisting mitochondrial protein folding, unfolding, and degradation (Bukau and Horwich, 1998; Fink, 1999; Slavotinek and Biesecker, 2001; Thirumalai and Lorimer, 2001; Corrao et al., 2010). HSP60 also have anti-apoptosis and pro-apoptosis roles in different pathophysiologic conditions such as heart failure (Knowlton et al., 1998; Kirchhoff et al., 2002; Gupta and Knowlton, 2005; Lin et al, 2007; Kim et al., 2009) and cancer (Chandra et al., 2007; Campanella et al., 2008).
Hsp60 function.
Hsp60 works in cooperation with Hsp10, its co-chaperonin, to assist protein folding of unfolded mitochondrial proteins by an ATP dependent mechanism. Modified from www.pdbj.org.
Homology
Up to now more than 150 homologues of HSP60 sequences with pair-wise similarity extending from 40-100% at the amino acid level. Among these homologues one can mention those from rat rat (Rattus norvegicus), pufferfish (Fugu rubripes), zebrafish (Danio rerio), the nematode Caenorhabditis elegans, mouse (Mus musculus), and Chlamydia trachomatis (Gupta, 1995). Moreover, Hsp60 presents a high structural homology with other human proteins, that may act as autoantigen, such as acetylcholine receptor, thyroglobulin, etc. (Jones et al., 1993). The high homology between Hsp60 of several bacterial species and the human protein led to postulate its involvement in molecular mimicry phenomena with pathogenic implications (Campanella et al., 2009; Cappello et al., 2009). Moreover, the high homology between human and bacterial Hsp60 and other human autoantigens led to postulate its role in the autoimmune manifestations of some autoimmune diseases, such as myasthenia gravis (Cappello et al., 2010; Marino Gammazza et al., 2012) and Hashimotos thyroiditis (Marino Gammazza et al., 2014).
Hsp60 homology and cross-reactivity.
Comparison between the structures of Chlamydia trachomatis (ct-) and human- (h-) Hsp60. Shown are the positions of the four epitopes with 100% homologies. Circle: apical domain; arrow: intermediate domain; arrowhead: equatorial domain. Source: Cappello et al., PLoS Pathog. 2009 ; 5 (8) :e1000552. PMID 19714222.
Mutations
Mutations that cripple Hsp60 and cause disease in humans.
Left: wild type Hsp60, with the amino acids V98 (yellow) and D29 (red) highlighted. Right: the mutants V98I, causing spastic paraplegia SPG13 (yellow), and D29G, causing MitCHAP-60 disease (red), are highlighted. These mutations appear to alter the molecular anatomy of Hsp60 to the point of making it functionally defective. Source: Cappello et al., Expert Opin Ther Targets. 2014 ; 18 (2) : 185-208. PMID 24286280
Germinal
Not known in Homo sapiens.
Somatic
Hereditary spastic paraplegia (SPG13) is associated with a mutation in the HSP60 gene: the amino acid 72 Valine is changed to Isoleucine (Hansen et al., 2002). MitCHAP-60 disease is associated with a mutation in the HSP60 gene: The amino acid 29 Aspartic acid is changed to Glycine (Magen et al., 2008).
General note:
HSP60 expression (mRNA) and levels (protein) were elevated, decreased or without changes in a number of cancers studied by independent groups with various techniques. For a review on this topic see: Czarnecka et al., 2006; Cappello et al., 2008; Rappa et al., 2012; Macario et al., 2013). Moreover, cancer cells, but not the normal counterparts release HSP60 via exosomes (Merendino et al., 2010; Campanella et al., 2012). Further studies on this topic are currently under way to better understand why Hsp60 levels change during carcinogenesis and what is the role of this protein in cancer progression
General note:
HSP60 expression (mRNA) and levels (protein) were elevated, decreased or without changes in a number of cancers studied by independent groups with various techniques. For a review on this topic see: Czarnecka et al., 2006; Cappello et al., 2008; Rappa et al., 2012; Macario et al., 2013). Moreover, cancer cells, but not the normal counterparts release HSP60 via exosomes (Merendino et al., 2010; Campanella et al., 2012). Further studies on this topic are currently under way to better understand why Hsp60 levels change during carcinogenesis and what is the role of this protein in cancer progression
Epigenetics
Not known in Homo sapiens.
Implicated in
Entity name
Autoimmune diseases
Note
First clinical trials using HSP60 (peptide 277) has been tested in type-2 diabetes.
Disease
HSP60 has been implicated in T cell activation and cause inflammatory reaction. It has been involved in the pathogenesis of a number of autoimmune diseases and inflammatory conditions such as type-1 diabetes, juvenile chronic arthritis, atherosclerosis, Crohn disease, rheumatoid arthritis, systemic lupus erythematosus, Sjogren syndrome, Hashimoto thyroiditis, and myasthenia gravis (Campanella et al., 2009; Cappello et al., 2009; Cappello et al., 2010; Marino Gammazza et al., 2012; Marino Gammazza et al., 2014).
Entity name
Colon cancer
Note
For a review on Hsp60 in colon cancer, see Cappello et al., 2011c.
Disease
Hsp60 expression and levels were increased in colon cancer of various grades and stages compared to controls (Cappello et al., 2005a). This has been confirmed by other independent groups (Mori et al., 2005; He et al., 2007).
Prognosis
Hsp60 has been described as a potential serum marker for colorectal cancer (Hamelin et al., 2011).
Oncogenesis
Hsp60 levels increase gradually through the carcinogenic steps (i.e., normal-to-dysplasia-to-carcinoma sequence) and Hsp60 is a good marker to distinguish dysplastic from normal cells (Cappello et al., 2003a).
Entity name
Lung cancer.
Note
The four major histological types of carcinoma of the lung are: squamous cell carcinoma (SCC), adenocarcinoma (AD), small cell carcinoma (SCLC), and large cell carcinoma (LCC). In some cases there can be a combination of histological patterns (Husain and Kumar, 2005).
Disease
Hsp60 levels were decreased in adenocarcinoma and adenosquamous carcinoma compared to controls (Cappello et al., 2005b; Cappello et al., 2006a). However, this has not been confirmed by another independent group (Xu et al., 2011) that in a series of lung adenocarcinomas found increased levels of Hsp60 compared to controls. The authors postulated that the possible reason to explain this contrasting data may be two: different TNM stages and different part of the tumor biopsied (e.g., central versus periphery).
Prognosis
Hsp60 levels were significantly correlated with TNM stage of the tumor and Eastern Cooperative Oncology Group performance status (Xu et al., 2011). Multivariate statistical analysis showed that patient age, pathological T stage, N stage, and Hsp60 expression were independent prognostic indicators with regard to disease-free survival (Xu et al., 2011).
Oncogenesis
Hsp60 levels decrease gradually through carcinogenetic steps of lung (i.e., normal-to-dysplasia-to-carcinoma sequence) (Cappello et al., 2005b; Cappello et al., 2006a).
Entity name
Prostate cancer
Note
Prostate cancer is preceded by the so called prostate intraneoplastic lesion or PIN, a dysplastic (pretumoral) lesion. Prostatic hyperplasia is not considered a preneoplastic condition (Bostwick and Chen, 2012). Gleason score is an index of malignancy: the higher it is, the worse is the prognosis (Egevad et al., 2012). Prostate specific antigen (PSA) is a serum marker used for prostate cancer diagnosis and follow-up (Loeb et al., 2014).
Disease
Many studies have shown that Hsp60 levels are increased in prostate cancer, using immunohistochemistry (Cornford et al., 2000; Cappello et al., 2003b; Johansson et al., 2006), and proteomics (Skyortsov et al., 2011). HSP60 was significantly increased in both early and advanced prostate cancers when compared with non-neoplastic prostatic epithelium (Cornford et al., 2000). In non-malignant prostate, HSP60-staining is localized in the glandular compartment, particularly basal epithelial cells. In prostate cancer, most epithelial cells showed moderate to strong staining without apparent correlation between staining intensity and Gleason grade (Johansson et al., 2006).
Prognosis
Recurrence-free survival in patients with strong HSP60 staining was shorter than in those with weak levels (Glaessgen et al., 2008). In another study, the levels of HSP60 were significantly increased in tumors with high Gleason score. HSP60 expression was also significantly associated with initial serum PSA levels and with the presence of lymph node metastasis (Castilla et al., 2010).
Oncogenesis
HSP60 levels increase gradually through carcinogenic steps (from PIN to carcinoma) of prostate (Cappello et al., 2003b).
Entity name
Exocervical cancer
Note
Exocervical cancer is preceded by the so called squamous intraepithelial lesion or SIL, a dysplastic (pretumoral) lesion (Garrett and McCann, 2013). SIL, as well as exocervical cancer, have been related to infection by Human Papilloma Virus (HPV) (Garrett and McCann, 2013).
Disease
Hsp60 levels are increased in exocervical cancer, as shown by immunohistochemistry (Cappello et al., 2002-2003; Castle et al., 2005).
Oncogenesis
HSP60 levels increase gradually through carcinogenic steps (from SIL to carcinoma) of exocervix (Cappello et al., 2002-2003).
Entity name
Vesical cancer
Disease
HSP60 levels are decreased in vesical cancers such as bladder carcinoma (Lebret et al., 2003; Cappello et al., 2006b).
Prognosis
HSP60 is considered a useful marker for patients with superficial bladder carcinoma for predicting disease progression: lower levels correlate with worse outcome of local treatments. Particularly, HSP60 levels are considered useful prognostic marker to identify patients for whom local treatment would be insufficient (Lebret et al., 2003). Hsp60 levels may predict response to neoadjuvant chemoradiotherapy in invasive or high-risk superficial bladder cancer (Urushibara et al., 2007).
Article Bibliography
| Pubmed ID | Last Year | Title | Authors |
|---|---|---|---|
| 22212075 | 2012 | Precursors of prostate cancer. | Bostwick DG et al |
| 9476895 | 1998 | The Hsp70 and Hsp60 chaperone machines. | Bukau B et al |
| 22848686 | 2012 | The odyssey of Hsp60 from tumor cells to other destinations includes plasma membrane-associated stages and Golgi and exosomal protein-trafficking modalities. | Campanella C et al |
| 24286280 | 2014 | Hsp60 chaperonopathies and chaperonotherapy: targets and agents. | Cappello F et al |
| 20708221 | 2010 | Immunohistochemical expression of Hsp60 correlates with tumor progression and hormone resistance in prostate cancer. | Castilla C et al |
| 16112431 | 2005 | Immunohistochemical evaluation of heat shock proteins in normal and preinvasive lesions of the cervix. | Castle PE et al |
| 11156417 | 2000 | Heat shock protein expression independently predicts clinical outcome in prostate cancer. | Cornford PA et al |
| 19913561 | 2010 | Human Hsp10 and Early Pregnancy Factor (EPF) and their relationship and involvement in cancer and immunity: current knowledge and perspectives. | Corrao S et al |
| 16861898 | 2006 | Mitochondrial chaperones in cancer: from molecular biology to clinical diagnostics. | Czarnecka AM et al |
| 22458905 | 2012 | Implications of the International Society of Urological Pathology modified Gleason grading system. | Egevad L et al |
| 10221986 | 1999 | Chaperone-mediated protein folding. | Fink AL et al |
| 22258649 | 2012 | The molecular anatomy of human Hsp60 and its similarity with that of bacterial orthologs and acetylcholine receptor reveal a potential pathogenetic role of anti-chaperonin immunity in myasthenia gravis. | Gammazza AM et al |
| 23337842 | 2013 | Abnormal cytology in 2012: management of atypical squamous cells, low-grade intraepithelial neoplasia, and high-grade intraepithelial neoplasia. | Garrett LA et al |
| 19132982 | 2008 | Heat shock proteins 27, 60 and 70 as prognostic markers of prostate cancer. | Glaessgen A et al |
| 18575266 | 2008 | Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10. | Gupta RS et al |
| 15784164 | 2005 | HSP60, Bax, apoptosis and the heart. | Gupta S et al |
| 21973086 | 2011 | Identification and verification of heat shock protein 60 as a potential serum marker for colorectal cancer. | Hamelin C et al |
| 12483302 | 2003 | Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. | Hansen JJ et al |
| 11898127 | 2002 | Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. | Hansen JJ et al |
| 21136683 | 2007 | Proteomics-based identification of HSP60 as a tumor-associated antigen in colorectal cancer. | He Y et al |
| 16705742 | 2006 | Proteomic comparison of prostate cancer cell lines LNCaP-FGC and LNCaP-r reveals heatshock protein 60 as a marker for prostate malignancy. | Johansson B et al |
| 8466626 | 1993 | Sequence homologies between hsp60 and autoantigens. | Jones DB et al |
| 19875724 | 2009 | Extracellular heat shock protein 60, cardiac myocytes, and apoptosis. | Kim SC et al |
| 12070120 | 2002 | Cytosolic heat shock protein 60, apoptosis, and myocardial injury. | Kirchhoff SR et al |
| 9602430 | 1998 | Differential expression of heat shock proteins in normal and failing human hearts. | Knowlton AA et al |
| 12942564 | 2003 | Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma. | Lebret T et al |
| 17675567 | 2007 | HSP60 in heart failure: abnormal distribution and role in cardiac myocyte apoptosis. | Lin L et al |
| 25457014 | 2015 | Active surveillance for prostate cancer: a systematic review of clinicopathologic variables and biomarkers for risk stratification. | Loeb S et al |
| 18571143 | 2008 | Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. | Magen D et al |
| 24057177 | 2014 | Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes point to the chaperonin as an immunopathogenic factor in Hashimoto's thyroiditis. | Marino Gammazza A et al |
| 20169074 | 2010 | Hsp60 is actively secreted by human tumor cells. | Merendino AM et al |
| 16308103 | 2005 | Differential expression of Janus kinase 3 (JAK3), matrix metalloproteinase 13 (MMP13), heat shock protein 60 (HSP60), and mouse double minute 2 (MDM2) in human colorectal cancer progression using human cancer cDNA microarrays. | Mori D et al |
| 20193073 | 2010 | Chaperonin genes on the rise: new divergent classes and intense duplication in human and other vertebrate genomes. | Mukherjee K et al |
| 23225410 | 2012 | HSP-molecular chaperones in cancer biogenesis and tumor therapy: an overview. | Rappa F et al |
| 20390473 | 2010 | Hsp60 and Hsp10 increase in colon mucosa of Crohn’s disease and ulcerative colitis. | Rodolico V et al |
| 18229457 | 2007 | Plasma heat shock protein 60 and cardiovascular disease risk: the role of psychosocial, genetic, and biological factors. | Shamaei-Tousi A et al |
| 20977276 | 2011 | Proteomics profiling of microdissected low- and high-grade prostate tumors identifies Lamin A as a discriminatory biomarker. | Skvortsov S et al |
| 11525836 | 2001 | Unfolding the role of chaperones and chaperonins in human disease. | Slavotinek AM et al |
| 10322429 | 1999 | Mitochondrial-matrix proteins at unexpected locations: are they exported? | Soltys BJ et al |
| 11340060 | 2001 | Chaperonin-mediated protein folding. | Thirumalai D et al |
| 21441812 | 2011 | Changes in immunohistochemical levels and subcellular localization after therapy and correlation and colocalization with CD68 suggest a pathogenetic role of Hsp60 in ulcerative colitis. | Tomasello G et al |
| 17095522 | 2007 | HSP60 may predict good pathological response to neoadjuvant chemoradiotherapy in bladder cancer. | Urushibara M et al |
| 25027488 | 2014 | The role of heat shock proteins in atherosclerosis. | Wick G et al |
| 21671464 | 2011 | Heat shock protein-60 expression was significantly correlated with the prognosis of lung adenocarcinoma. | Xu X et al |
Other Information
Locus ID:
NCBI: 3329
MIM: 118190
HGNC: 5261
Ensembl: ENSG00000144381
Variants:
dbSNP: 3329
ClinVar: 3329
TCGA: ENSG00000144381
COSMIC: HSPD1
RNA/Proteins
Expression (GTEx)
Pathways
Protein levels (Protein atlas)
References
| Pubmed ID | Year | Title | Citations |
|---|---|---|---|
| 37694354 | 2024 | Potential association of HSPD1 with dysregulations in ribosome biogenesis and immune cell infiltration in lung adenocarcinoma: An integrated bioinformatic approach. | 1 |
| 38663552 | 2024 | Knockdown of heat shock protein family D member 1 (HSPD1) in lung cancer cell altered secretome profile and cancer-associated fibroblast induction. | 1 |
| 37694354 | 2024 | Potential association of HSPD1 with dysregulations in ribosome biogenesis and immune cell infiltration in lung adenocarcinoma: An integrated bioinformatic approach. | 1 |
| 38663552 | 2024 | Knockdown of heat shock protein family D member 1 (HSPD1) in lung cancer cell altered secretome profile and cancer-associated fibroblast induction. | 1 |
| 36520371 | 2023 | Reactivity to neural tissue epitopes, aquaporin 4 and heat shock protein 60 is associated with activated immune-inflammatory pathways and the onset of delirium following hip fracture surgery. | 0 |
| 36625202 | 2023 | Ectopic CH60 mediates HAPLN1-induced cell survival signaling in multiple myeloma. | 2 |
| 36692509 | 2023 | Chaperonin counteracts diet-induced non-alcoholic fatty liver disease by aiding sirtuin 3 in the control of fatty acid oxidation. | 2 |
| 36852893 | 2023 | Human Mitochondrial Protein HSPD1 Binds to and Regulates the Repair of Deoxyinosine in DNA. | 1 |
| 36889194 | 2023 | Cuproptosis-related gene PDHX and heat stress-related HSPD1 as potential key drivers associated with cell stemness, aberrant metabolism and immunosuppression in esophageal carcinoma. | 1 |
| 37087461 | 2023 | Knockdown of heat shock protein family D member 1 (HSPD1) promotes proliferation and migration of ovarian cancer cells via disrupting the stability of mitochondrial 3-oxoacyl-ACP synthase (OXSM). | 4 |
| 36520371 | 2023 | Reactivity to neural tissue epitopes, aquaporin 4 and heat shock protein 60 is associated with activated immune-inflammatory pathways and the onset of delirium following hip fracture surgery. | 0 |
| 36625202 | 2023 | Ectopic CH60 mediates HAPLN1-induced cell survival signaling in multiple myeloma. | 2 |
| 36692509 | 2023 | Chaperonin counteracts diet-induced non-alcoholic fatty liver disease by aiding sirtuin 3 in the control of fatty acid oxidation. | 2 |
| 36852893 | 2023 | Human Mitochondrial Protein HSPD1 Binds to and Regulates the Repair of Deoxyinosine in DNA. | 1 |
| 36889194 | 2023 | Cuproptosis-related gene PDHX and heat stress-related HSPD1 as potential key drivers associated with cell stemness, aberrant metabolism and immunosuppression in esophageal carcinoma. | 1 |
Citation
Cappello Francesco ; Conway de Macario Everly ; Macario Alberto JL
HSPD1 (Heat Shock 60kDa Protein 1)
Atlas Genet Cytogenet Oncol Haematol. 2014-10-01
Online version: http://atlasgeneticsoncology.org/gene/40888/hspd1
Historical Card
2007-02-01 HSPD1 (Heat Shock 60kDa Protein 1) by Ahmad Faried,Leri S Faried Affiliation
Department of General Surgical Science (Surgery I), Graduate School of Medicine, Gunma University, Maebashi, Japan
