HCSGD entry for ZMPSTE24
1. General information
| Official gene symbol | ZMPSTE24 |
|---|---|
| Entrez ID | 10269 |
| Gene full name | zinc metallopeptidase STE24 |
| Other gene symbols | FACE-1 FACE1 HGPS PRO1 STE24 Ste24p |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0004222 | Metalloendopeptidase activity | IEA | molecular_function |
| GO:0005637 | Nuclear inner membrane | IEA | cellular_component |
| GO:0005789 | Endoplasmic reticulum membrane | IEA | cellular_component |
| GO:0006508 | Proteolysis | TAS | biological_process |
| GO:0006998 | Nuclear envelope organization | IEA | biological_process |
| GO:0008235 | Metalloexopeptidase activity | TAS | molecular_function |
| GO:0016021 | Integral component of membrane | IEA | cellular_component |
| GO:0030327 | Prenylated protein catabolic process | IEA | biological_process |
| GO:0046872 | Metal ion binding | IEA | molecular_function |
| GO:0071586 | CAAX-box protein processing | 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 |
|---|---|---|---|
| 0.0953594734 | 0.5765405532 | 0.6465627769 | 1.0000000000 |
- 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 | Up | 0.3621427687 |
| GSE13712_SHEAR | Up | 0.0051465905 |
| GSE13712_STATIC | Up | 0.0057132819 |
| GSE19018 | Down | -0.4004629569 |
| GSE19899_A1 | Up | 0.7637081701 |
| GSE19899_A2 | Up | 0.3021002936 |
| PubMed_21979375_A1 | Up | 0.3059962880 |
| PubMed_21979375_A2 | Up | 0.5048058305 |
| GSE35957 | Up | 0.0585431568 |
| GSE36640 | Up | 0.6027534749 |
| GSE54402 | Up | 0.0288325982 |
| GSE9593 | Up | 0.2870803295 |
| GSE43922 | Up | 0.5721102977 |
| GSE24585 | Down | -0.0842259322 |
| GSE37065 | Down | -0.0081192026 |
| GSE28863_A1 | Down | -0.4153086381 |
| GSE28863_A2 | Up | 0.2172277040 |
| GSE28863_A3 | Down | -0.7707610802 |
| GSE28863_A4 | Down | -0.2209004760 |
| GSE48662 | Down | -0.0731049647 |
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-98-5p | MIMAT0000096 | MIRT004942 | qRT-PCR | Functional MTI (Weak) | 17942906 |
| hsa-miR-124-3p | MIMAT0000422 | MIRT022576 | Microarray | Functional MTI (Weak) | 18668037 |
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- mirRecord
No target information from mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 13 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 27120622 | A Heterozygous ZMPSTE24 Mutation Associated with Severe Metabolic Syndrome, Ectopic Fat Accumulation, and Dilated Cardiomyopathy |
| 27120622 | ZMPSTE24 encodes the only metalloprotease, which transforms prelamin into mature lamin A |
| 27120622 | Up to now, mutations in ZMPSTE24 have been linked to Restrictive Dermopathy (RD), Progeria or Mandibulo-Acral Dysplasia (MAD) |
| 27120622 | We report here the phenotype of a patient referred for severe metabolic syndrome and cardiomyopathy, carrying a mutation in ZMPSTE24 |
| 27120622 | We show here that a central obesity without subcutaneous lipoatrophy is associated with a laminopathy due to a heterozygous missense mutation in ZMPSTE24 |
| 26724531 | LMNA mutations resulting in lipodystrophy and HIV protease inhibitors trigger vascular smooth muscle cell senescence and calcification: Role of ZMPSTE24 downregulation |
| 26724531 | The metalloprotease ZMPSTE24 is the key enzyme in prelamin A maturation |
| 26724531 | AIM: We studied whether altered expression of ZMPSTE24 could contribute to vascular cell dysfunction in response to LMNA mutations or PI treatments |
| 26724531 | METHODS: Protein expression of prelamin A and ZMPSTE24 were evaluated in patients' cells and in human cultured VSMCs |
| 26724531 | RESULTS: Fibroblasts from LMNA-mutated lipodystrophic patients (mutations R482W, D47Y or R133L) and peripheral blood mononuclear cells from PI-treated-HIV-infected patients expressed increased prelamin A and decreased ZMPSTE24, which was also observed in VSMCs overexpressing mutant LMNA or treated with PIs |
| 26724531 | ZMPSTE24 silencing in native VSMCs recapitulated the mutant LMNA- and PI-induced accumulation of farnesylated prelamin A, oxidative stress, inflammation, senescence and calcification |
| 26724531 | A negative regulator of ZMPSTE24, miRNA-141-3p, was enhanced in LMNA-mutated or PI-treated VSMCs |
| 26724531 | The farnesylation inhibitors pravastatin and FTI-277, or the antioxidant N-acetyl cysteine, partly restored ZMPSTE24 expression, and concomitantly decreased oxidative stress, inflammation, senescence, and calcification of PI-treated VSCMs |
| 26724531 | CONCLUSIONS: ZMPSTE24 downregulation is a major contributor in VSMC dysfunctions resulting from LMNA mutations or PI treatments that could translate in early atherosclerosis at the clinical level |
| 26029982 | The pro-senescence lamin A mutant contains a deletion in the sequence required for processing by the protease ZMPSTE24 leading to accumulation of farnesylated lamin A in the nuclear envelope |
| 24584199 | Here, we investigated the effects of prelamin A on HP1alpha homeostasis, subcellular distribution, phosphorylation, and their contribution to accelerated senescence in mouse embryonic fibroblasts (MEFs) derived from Zmpste24(-/-) mice |
| 24584199 | Although prelamin A interacted with HP1alpha in a manner similar to lamin A, HP1alpha associated with the nuclease-resistant nuclear matrix fraction was remarkably increased in Zmpste24(-/-) MEFs compared with that in wild-type littermate controls |
| 24584199 | However, the peak of HP1alpha phosphorylation was significantly compromised and appeared until 2 h, which is correlated with the delayed maximal formation of gamma-H2AX foci in Zmpste24(-/-) MEFs |
| 24584199 | Furthermore, knocking down HP1alpha by siRNA alleviated the delayed DNA damage response and accelerated senescence in Zmpste24(-/-) MEFs, evidenced by the rescue of the delayed gamma-H2AX foci formation, downregulation of p16, and reduction of senescence-associated beta-galactosidase activity |
| 24155329 | We show that prelamin A is accumulated in fibroblasts from centenarians owing to downregulation of its specific endoprotease ZMPSTE24, whereas other nuclear envelope constituents are mostly unaffected and cells do not enter senescence |
| 24101728 | MicroRNA-141-3p plays a role in human mesenchymal stem cell aging by directly targeting ZMPSTE24 |
| 24101728 | We show for the first time that ZMPSTE24, which is involved in the post-translational maturation of lamin A, is largely responsible for the prelamin A accumulation related to cellular senescence in hMSCs |
| 24101728 | Direct binding of miR-141-3p to the 3'UTR of ZMPSTE24 transcripts was confirmed using a 3'UTR-luciferase reporter assay |
| 24101728 | We also found that miR-141-3p, which is overexpressed during senescence as a result of epigenetic regulation, is able to decrease ZMPSTE24 expression levels, and leads to an upregulation of prelamin A in hMSCs |
| 22555846 | IS upregulated prelamin A, a hallmark of vascular smooth muscle cell senescence, and downregulated FACE1/Zempste24 protein expression in HASMCs, and N-acetylcysteine suppressed these effects |
| 22555846 | Taken together, IS accelerates vascular smooth muscle cell senescence with upregulation of p53, p21, and prelamin A and downregulation of FACE1 through oxidative stress |
| 22297442 | Importantly, rapamycin treatment does not affect lamin C protein levels, but increases the relative expression of the prelamin A endoprotease ZMPSTE24 |
| 21746928 | The premature aging phenotype of Hutchinson Gilford progeria syndrome is largely recapitulated in mice deficient for the lamin A-processing enzyme, Zmpste24 |
| 21746928 | We have previously reported that Zmpste24 deficiency results in genomic instability and early cellular senescence due to the delayed recruitment of repair proteins to sites of DNA damage |
| 21746928 | Here, we further investigate the molecular mechanism underlying delayed DNA damage response and identify a histone acetylation defect in Zmpste24(-/-) mice |
| 21746928 | The life span of Zmpste24(-/-) mice was also extended with the supplementation of a histone deacetylase inhibitor, sodium butyrate, to drinking water |
| 20819672 | Candidate genes including LMNA, ZMPSTE24, PPAR G, INSR and WRN were sequenced to screen for DNA variants |
| 20458013 | BACKGROUND: Hutchinson-Gilford progeria syndrome is a rare inherited disorder of premature aging caused by mutations in LMNA or Zmpste24 that disrupt nuclear lamin A processing, leading to the accumulation of prelamin A |
| 20458013 | Prelamin A accumulation correlated with downregulation of the lamin A processing enzyme Zmpste24/FACE1, and FACE1 mRNA and protein levels were reduced in response to oxidative stress |
| 20458013 | Small interfering RNA knockdown of FACE1 reiterated the prelamin A-induced nuclear morphology defects characteristic of aged VSMCs, and overexpression of prelamin A accelerated VSMC senescence |
| 19015945 | The use of Face-1/Zmpste24-deficient mice allowed us to demonstrate that accumulation of farnesylated prelamin A causes severe abnormalities of the nuclear envelope, hyper-activation of p53 signalling, cellular senescence, stem cell dysfunction and the development of a progeroid phenotype |
| 19015945 | Using Face-1/Zmpste24-deficient mice as model, we found that a combination of statins and aminobisphosphonates inhibits both types of modifications of prelamin A and progerin, improves the ageing-like symptoms of these mice and extends substantially their longevity, opening a new therapeutic possibility for human progeroid syndromes associated with nuclear-envelope defects |
| 18363904 | In contrast to the accelerated aging defects observed in HGPS cells, the progeroid phenotype resulting from increased expression of wild-type lamin A can be rescued by overexpression of ZMPSTE24, the metalloproteinase responsible for the removal of the farnesylated carboxyl terminal region of lamin A |
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