HSPD1 (Heat Shock 60kDa Protein 1)

2014-10-01 Cappello Francesco , Conway de Macario Everly , Macario Alberto JL Affiliation

Identity

HGNC

HSPD1

LOCATION

2q33.1

IMAGE

LEGEND

Hsp60 and Hsp10 protein/gene/genomic data.

LOCUSID

3329

ALIAS

CPN60,GROEL,HLD4,HSP-60,HSP60,HSP65,HuCHA60,SPG13

FUSION GENES

Show Gene Fusions

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).

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

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

Gene ID	Transcript ID	Uniprot
ENSG00000144381	ENST00000345042	P10809
ENSG00000144381	ENST00000345042	A0A024R3X4
ENSG00000144381	ENST00000388968	P10809
ENSG00000144381	ENST00000388968	A0A024R3X4
ENSG00000144381	ENST00000418022	C9J0S9
ENSG00000144381	ENST00000426480	C9JL25
ENSG00000144381	ENST00000428204	C9JCQ4
ENSG00000144381	ENST00000430176	E7ESH4
ENSG00000144381	ENST00000439605	C9JL19
ENSG00000144381	ENST00000440114	F8WBB1
ENSG00000144381	ENST00000452200	E7EXB4

Expression (GTEx)

100

200

300

400

500

600

700

Adipose - Subcutaneous

Adipose - Visceral

Adrenal Gland

Artery - Aorta

Artery - Tibial

Bladder

Brain - Amygdala

Brain - Anterior cingulate cortex

Brain - Caudate

Brain - Cerebellar Hemisphere

Brain - Cerebellum

Brain - Cortex

Brain - Frontal Cortex

Brain - Hippocampus

Brain - Hypothalamus

Brain - Nucleus accumbens

Brain - Putamen

Brain - Spinal cord

Brain - Substantia nigra

Breast - Mammary Tissue

Cells - Cultured fibroblasts

Cells - EBV - transformed lymphocytes

Cervix - Ectocervix

Cervix - Endocervix

Colon - Sigmoid

Colon - Transverse

Esophagus - Gastroesophageal Junction

Esophagus - Mucosa

Esophagus - Muscularis

Fallopian Tube

Heart - Atrial Appendage

Heart - Left Ventricle

Kidney - Cortex

Kidney - Medulla

Liver

Lung

Minor Salivary Gland

Muscle - Skeletal

Nerve - Tibial

Ovary

Pancreas

Pituitary

Prostate

Skin - Not Sun Exposed

Skin - Sun Exposed

Small Intestine - Terminal Ileum

Spleen

Stomach

Testis

Thyroid

Uterus

Vagina

Whole Blood

Pathways

Pathway	Source	External ID
Type I diabetes mellitus	KEGG	ko04940
Type I diabetes mellitus	KEGG	hsa04940
RNA degradation	KEGG	ko03018
RNA degradation	KEGG	hsa03018
Tuberculosis	KEGG	ko05152
Tuberculosis	KEGG	hsa05152
Legionellosis	KEGG	ko05134
Legionellosis	KEGG	hsa05134
Metabolism of proteins	REACTOME	R-HSA-392499
Mitochondrial protein import	REACTOME	R-HSA-1268020
Gene Expression	REACTOME	R-HSA-74160
Generic Transcription Pathway	REACTOME	R-HSA-212436
Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors	REACTOME	R-HSA-8864260
TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation	REACTOME	R-HSA-8869496

Protein levels (Protein atlas)

Not detected

Low

Medium

High

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