HCSGD entry for LONP1
1. General information
| Official gene symbol | LONP1 |
|---|---|
| Entrez ID | 9361 |
| Gene full name | lon peptidase 1, mitochondrial |
| Other gene symbols | LON LONP LonHS PIM1 PRSS15 hLON |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
This gene isn't in Literature mining network.
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000002 | Mitochondrial genome maintenance | NAS | biological_process |
| GO:0001666 | Response to hypoxia | IEA IEP | biological_process |
| GO:0003697 | Single-stranded DNA binding | IBA IEA | molecular_function |
| GO:0003727 | Single-stranded RNA binding | IDA | molecular_function |
| GO:0004176 | ATP-dependent peptidase activity | IDA IEA | molecular_function |
| GO:0004252 | Serine-type endopeptidase activity | IBA IEA | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005524 | ATP binding | IDA IEA | molecular_function |
| GO:0005737 | Cytoplasm | IDA | cellular_component |
| GO:0005739 | Mitochondrion | IDA | cellular_component |
| GO:0005759 | Mitochondrial matrix | IEA IMP | cellular_component |
| GO:0006508 | Proteolysis | IEA | biological_process |
| GO:0006515 | Misfolded or incompletely synthesized protein catabolic process | IBA IEA | biological_process |
| GO:0007005 | Mitochondrion organization | IEA IMP | biological_process |
| GO:0007568 | Aging | IEA | biological_process |
| GO:0009725 | Response to hormone | IEA | biological_process |
| GO:0010044 | Response to aluminum ion | IEA | biological_process |
| GO:0030163 | Protein catabolic process | IEA | biological_process |
| GO:0032042 | Mitochondrial DNA metabolic process | NAS | biological_process |
| GO:0034599 | Cellular response to oxidative stress | IC IDA IEA | biological_process |
| GO:0042645 | Mitochondrial nucleoid | IDA | cellular_component |
| GO:0043531 | ADP binding | IDA | molecular_function |
| GO:0043565 | Sequence-specific DNA binding | IDA IEA | molecular_function |
| GO:0051131 | Chaperone-mediated protein complex assembly | IEA | biological_process |
| GO:0051260 | Protein homooligomerization | IDA | biological_process |
| GO:0051603 | Proteolysis involved in cellular protein catabolic process | IDA | biological_process |
| GO:0051880 | G-quadruplex DNA binding | IDA | molecular_function |
| GO:0070182 | DNA polymerase binding | IPI | molecular_function |
| GO:0070361 | Mitochondrial light strand promoter anti-sense binding | IDA IEA | molecular_function |
| GO:0070362 | Mitochondrial heavy strand promoter anti-sense binding | IDA | molecular_function |
| GO:0070363 | Mitochondrial light strand promoter sense binding | IDA | molecular_function |
| GO:0070364 | Mitochondrial heavy strand promoter sense binding | IDA | molecular_function |
| GO:0070407 | Oxidation-dependent protein catabolic process | IEA IMP | biological_process |
| GO:0090296 | Regulation of mitochondrial DNA replication | IEA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.8602511303 | 0.0134472322 | 0.9999902473 | 0.2291952104 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Down | -0.1986278644 |
| GSE13712_SHEAR | Down | -0.0980642118 |
| GSE13712_STATIC | Up | 0.0212797138 |
| GSE19018 | Down | -0.0065029286 |
| GSE19899_A1 | Down | -1.1968697424 |
| GSE19899_A2 | Down | -1.6542768576 |
| PubMed_21979375_A1 | Up | 0.0493854147 |
| PubMed_21979375_A2 | Down | -1.0523849259 |
| GSE35957 | Down | -0.8455283192 |
| GSE36640 | Down | -0.9370668052 |
| GSE54402 | Up | 0.1055216495 |
| GSE9593 | Up | 0.0510780735 |
| GSE43922 | Down | -0.4666033863 |
| GSE24585 | Down | -0.5964974957 |
| GSE37065 | Down | -0.4072708887 |
| GSE28863_A1 | Up | 0.0903487987 |
| GSE28863_A2 | Up | 0.1382066396 |
| GSE28863_A3 | Up | 0.4180069725 |
| GSE28863_A4 | Up | 0.0191792870 |
| GSE48662 | Up | 0.6503621427 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-26b-5p | MIMAT0000083 | MIRT029135 | Microarray | Functional MTI (Weak) | 19088304 |
| hsa-miR-20a-3p | MIMAT0004493 | MIRT038977 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-16-5p | MIMAT0000069 | MIRT051178 | CLASH | Functional MTI (Weak) | 23622248 |
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- mirRecord
MicroRNA name | mirBase ID | Target site number | MiRNA mature ID | Test method inter | MiRNA regulation site | Reporter target site | Pubmed ID |
|---|---|---|---|---|---|---|---|
| hsa-miR-1 | MIMAT0000416 | NA | hsa-miR-1 | {Western blot} | {overexpression by miRNA precursor transfection} | 18818206 |
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6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 7 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 26461412 | What Goes Wrong with Lon in Ageing |
| 26461412 | We have shown previously that the product of the human lon gene, the Lon protease, selectively degrades oxidized mitochondrial proteins, thus preventing their aggregation and cross-linking |
| 26461412 | Lon induction, by pre-treatment with low-level stress, protects against oxidative protein damage, diminished mitochondrial function, and loss of cell proliferation, induced by toxic levels of hydrogen peroxide |
| 26461412 | Blocking Lon induction, with lon siRNA, also blocks this induced protection |
| 26461412 | In senescent cells, and in older primary cells, however, Lon activity declines, and adaptational responses become sluggish or even ineffectual |
| 26461412 | Studies in Drosophila melanogaster flies and in mice now suggest that declining Lon activity and declining responsiveness to stress, may contribute to the ageing process, and to various age-associated diseases |
| 26461412 | We propose that Lon is a generalized stress-protective enzyme whose decline may contribute to the increased levels of protein damage and mitochondrial dysfunction observed in ageing and various age-related diseases |
| 26363553 | Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer |
| 26363553 | Lon protease is a nuclear DNA-encoded mitochondrial enzyme highly conserved throughout evolution, involved in the degradation of damaged and oxidized proteins of the mitochondrial matrix, in the correct folding of proteins imported in mitochondria, and in the maintenance of mitochondrial DNA |
| 26363553 | Lon expression is induced by various stimuli, including hypoxia and reactive oxygen species, and provides protection against cell stress |
| 26363553 | Lon down-regulation is associated with ageing and with cell senescence, while up-regulation is observed in tumour cells, and is correlated with a more aggressive phenotype of cancer |
| 26363553 | Lon up-regulation contributes to metabolic reprogramming observed in cancer, favours the switch from a respiratory to a glycolytic metabolism, helping cancer cell survival in the tumour microenvironment, and contributes to epithelial to mesenchymal transition |
| 26363553 | Silencing of Lon, or pharmacological inhibition of its activity, causes cell death in various cancer cells |
| 26363553 | Thus, Lon can be included in the growing class of proteins that are not responsible for oncogenic transformation, but that are essential for survival and proliferation of cancer cells, and that can be considered as a new target for development of anticancer drugs |
| 24024159 | Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging |
| 24024159 | The Lon Protease is a key enzyme in the degradation of oxidized proteins within the mitochondrial matrix |
| 24024159 | Under conditions of acute stress Lon is highly inducible, possibly with the oxidant acting as the signal inducer, thereby providing increased protection |
| 24024159 | It seems that under chronic stress conditions, however, Lon levels actually decline |
| 24024159 | Lon levels also decline with age and with senescence, and senescent cells even lose the ability to induce Lon during acute stress |
| 24024159 | We propose that the regulation of Lon is biphasic, in that it is up-regulated during transient stress and down-regulated during chronic stress and aging, and we suggest that the loss of Lon responsiveness may be a significant factor in aging, and in age-related diseases |
| 21868393 | Oxidative damage to mitochondrial proteins is thought to contribute to the aging process, but the Lon protease normally degrades such proteins |
| 21868393 | In early-passage WI-38 human lung fibroblasts, Lon expression is rapidly induced during H(2)O(2) stress, which prevents the accumulation of oxidized proteins and protects cell viability |
| 21868393 | In contrast, middle passage cells exhibit only sluggish induction of Lon expression in oxidative stress, and oxidized proteins initially accumulate |
| 21868393 | Late-passage, or senescent, cells have low basal levels of Lon and high levels of accumulated oxidized proteins; in response to oxidative stress, they fail to induce Lon expression and exhibit continually increasing accumulation of oxidized proteins |
| 21868393 | These senescent changes are similar to the effects of Lon silencing in young cells |
| 21868393 | We suggest that loss of Lon stress inducibility is part of a pattern of diminishing stress adaptability that predisposes cells to senescence |
| 20528770 | In contrast, up-regulation of Nuak2 (NUAK family, SNF1-like kinase 2) and down-regulation of Lonp2 (Lon peptidase 2), Foxo3a (forkhead box O3a), Sod1 (copper/zinc superoxide dismutase) and Sesn1 (sestrin 1) in the kidneys of recuperated offspring suggest that protein homoeostasis and resistance to oxidative stress are compromised, leading to accelerated cellular senescence in these shorter-lived mice |
| 20094032 | Misfolded proteins deposited at the cell poles lead to selective re-localization of the DnaK/DnaJ/ClpB disaggregating chaperones, but not of GroEL and Lon to these sites |
| 18446870 | Irreversibly oxidized proteins are targeted to degradation by mitochondrial matrix proteolytic systems such as the Lon protease |
| 18446870 | The ATP-stimulated Lon protease is believed to play a crucial role in the degradation of oxidized proteins within the mitochondria and age-related declines in the activity and/or expression of this proteolytic system have been previously reported |
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