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Gene Symbol |
PRDX1 |
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Aliases |
MSP23, NKEF-A, NKEFA, PAG, PAGA, PAGB, PRX1, PRXI, TDPX2 |
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Entrez Gene ID |
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Gene Name |
Peroxiredoxin 1 |
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Chromosomal Location |
1p34.1 |
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HGNC ID |
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Summary |
This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Four transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jan 2011]
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e!Ensembl
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Gene Ontology (GO)
GO ID |
Ontology |
Function |
Evidence |
Reference |
GO:0001501 |
Biological process |
Skeletal system development |
TAS |
8089076 |
GO:0001895 |
Biological process |
Retina homeostasis |
HEP |
23580065 |
GO:0006979 |
Biological process |
Response to oxidative stress |
IBA |
21873635 |
GO:0019430 |
Biological process |
Removal of superoxide radicals |
IBA |
21873635 |
GO:0030101 |
Biological process |
Natural killer cell activation |
IDA |
8462106 |
GO:0042744 |
Biological process |
Hydrogen peroxide catabolic process |
IBA |
21873635 |
GO:0042744 |
Biological process |
Hydrogen peroxide catabolic process |
IDA |
11986303, 18606987 |
GO:0045321 |
Biological process |
Leukocyte activation |
IBA |
21873635 |
GO:0045454 |
Biological process |
Cell redox homeostasis |
IBA |
21873635 |
GO:0005615 |
Cellular component |
Extracellular space |
HDA |
22664934, 23580065 |
GO:0005634 |
Cellular component |
Nucleus |
HDA |
21630459 |
GO:0005634 |
Cellular component |
Nucleus |
IDA |
17603937 |
GO:0005737 |
Cellular component |
Cytoplasm |
IBA |
21873635 |
GO:0005737 |
Cellular component |
Cytoplasm |
IDA |
17603937 |
GO:0005829 |
Cellular component |
Cytosol |
IBA |
21873635 |
GO:0070062 |
Cellular component |
Extracellular exosome |
HDA |
19199708, 20458337, 23533145 |
GO:0003723 |
Molecular function |
RNA binding |
HDA |
22658674, 22681889 |
GO:0004601 |
Molecular function |
Peroxidase activity |
IDA |
11986303 |
GO:0005515 |
Molecular function |
Protein binding |
IPI |
15105503, 17909037, 18172504, 19369943, 21044950, 21969592, 23386615, 27607350 |
GO:0008379 |
Molecular function |
Thioredoxin peroxidase activity |
IBA |
21873635 |
GO:0008379 |
Molecular function |
Thioredoxin peroxidase activity |
IDA |
18606987 |
GO:0045296 |
Molecular function |
Cadherin binding |
HDA |
25468996 |
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Protein Information |
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Protein Name |
Peroxiredoxin-1, epididymis secretory sperm binding protein, natural killer cell-enhancing factor A, natural killer-enhancing factor A, proliferation-associated gene A, proliferation-associated gene protein, thioredoxin peroxidase 2, thioredoxin-dependent peroxide reductase 2 |
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Function |
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). |
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UniProt |
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PDB |
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Interactions |
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STRING |
MINT |
IntAct |
ENSP00000385834 |
P02787 |
P02787 |
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View interactions
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Associated Diseases
Disease group | Disease Name | References |
Endocrine System Diseases |
Methylmalonic acidemia with homocystinuria |
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PCOS |
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Neoplasms |
Lung Cancer |
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Liver Cancer |
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Esophagus Neoplasm |
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Respiratory Tract Diseases |
Pulmonary asbestosis |
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Pulmonary Fibrosis |
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References |
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Atiomo W, Khalid S, Parameshweran S, Houda M, Layfield R |
Department of Obstetrics and Gynaecology, School of Human Development, University of Nottingham, and Nottingham University Hospitals, Nottingham, UK. william.atiomo@nottingham.ac.uk |
BJOG. 2009 Jan;116(2):137-43. doi: 10.1111/j.1471-0528.2008.02041.x. |
Abstract
BACKGROUND: The exact causes of polycystic ovary syndrome (PCOS) are uncertain, and treatment could be improved. Discovery-based approaches like 'proteomics' may result in faster insights into the causes of PCOS and improved treatment. OBJECTIVES: To identify the number and nature of proteomic biomarkers found in PCOS so far and to identify their diagnostic and therapeutic potential. SEARCH STRATEGY: All published studies on proteomic biomarkers in women with PCOS identified through the MEDLINE (1966-2008), EMBASE (1980-2008) and the ISI web of knowledge (v4.2) databases. SELECTION CRITERIA: The terms 'polycystic ovary syndrome' and 'proteomic', 'proteomics', 'proteomic biomarker' or 'proteomics biomarker' without any limits/restrictions were used. DATA COLLECTION AND ANALYSIS: Original data were abstracted where available and summarised on a separate Microsoft Excel (2007) database for analysis. MAIN RESULTS: Seventeen articles were identified, of which 6 original papers and 1 review article contained original data. Tissues investigated included serum, omental biopsies, ovarian biopsies, follicular fluid and T lymphocytes. Sample sizes ranged from 3 to 30 women. One hundred and forty-eight biomarkers were identified. The biomarkers were involved in many pathways, for example the regulation of fibrinolysis and thrombosis, insulin resistance, immunity/inflammation and the antioxidant pathway. Eleven groups of biomarkers appeared to be independently validated. The individual sensitivities for the diagnosis of PCOS were reported for 11 named biomarkers and ranged from 57 to 100%. AUTHOR'S CONCLUSIONS: Proteomic biomarker discovery in PCOS offers great potential. Current challenges include reproducibility and data analysis. The establishment of a PCOS-specific biomarker data bank and international consensus on the framework of systematic reviews in this field are required. |
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Galazis Nicolas, Docheva Nikolina, Nicolaides Kypros H, Atiomo William |
Division of Human Development, School of Clinical Sciences, University of Nottingham, Nottingham, United Kingdom. ngalazis@gmail.com |
PLoS One. 2013;8(1):e53801. doi: 10.1371/journal.pone.0053801. Epub 2013 Jan 29. |
Abstract
BACKGROUND: Preterm Birth (PTB) is a major cause of neonatal mortality and morbidity. Women with Polycystic Ovary Syndrome (PCOS) are at high risk of PTB. There is a need for research studies to investigate the mechanisms linking PCOS and PTB, to facilitate screening, and develop novel preventative strategies. OBJECTIVE: To list all the proteomic biomarkers of PTB and integrate this list with the PCOS biomarker database to identify commonly expressed biomarkers of the two conditions. SEARCH STRATEGY: A systematic review of PTB biomarkers and update of PCOS biomarker database. All eligible published studies on proteomic biomarkers for PTB and PCOS identified through various databases were evaluated. SELECTION CRITERIA: For the identification of the relevant studies, the following search terms were used: "proteomics", "proteomic", "preterm birth", "preterm labour", "proteomic biomarker" and "polycystic ovary syndrome". This search was restricted to humans only DATA COLLECTION AND ANALYSIS: A database on proteomic biomarkers for PTB was created while an already existing PCOS biomarker database was updated. The two databases were integrated and biomarkers that were co-expressed in both women with PCOS and PTB were identified and investigated. RESULTS: A panel of six proteomic biomarkers was similarly differentially expressed in women with PTB and women with PCOS compared to their respective controls (normal age-matched women in the case of PCOS studies and women with term pregnancy in the case of PTB studies). These biomarkers include Pyruvate kinase M1/M2, Vimentin, Fructose bisphosphonate aldolase A, Heat shock protein beta-1, Peroxiredoxin-1 and Transferrin. CONCLUSIONS: These proteomic biomarkers (Pyruvate kinase M1/M2, Vimentin, Fructose bisphosphonate aldolase A, Heat shock protein beta-1, Peroxiredoxin-1 and Transferrin) can be potentially used to better understand the pathophysiological mechanisms linking PCOS and PTB. This would help to identify subgroups of women with PCOS at risk of PTB and hence the potential of developing preventative strategies. |
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National Institute for Research in Reproductive Health, Jehangir Merwanji Street, Parel, Mumbai-400 012
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