HCSGD entry for LMNA
1. General information
| Official gene symbol | LMNA |
|---|---|
| Entrez ID | 4000 |
| Gene full name | lamin A/C |
| Other gene symbols | CDCD1 CDDC CMD1A CMT2B1 EMD2 FPL FPLD FPLD2 HGPS IDC LDP1 LFP LGMD1B LMN1 LMNC LMNL1 PRO1 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000278 | Mitotic cell cycle | TAS | biological_process |
| GO:0005198 | Structural molecule activity | IEA TAS | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005634 | Nucleus | IDA | cellular_component |
| GO:0005635 | Nuclear envelope | IDA TAS | cellular_component |
| GO:0005638 | Lamin filament | IEA TAS | cellular_component |
| GO:0005652 | Nuclear lamina | TAS | cellular_component |
| GO:0005654 | Nucleoplasm | TAS | cellular_component |
| GO:0005737 | Cytoplasm | IDA | cellular_component |
| GO:0005829 | Cytosol | TAS | cellular_component |
| GO:0005882 | Intermediate filament | IEA TAS | cellular_component |
| GO:0006915 | Apoptotic process | TAS | biological_process |
| GO:0006921 | Cellular component disassembly involved in execution phase of apoptosis | TAS | biological_process |
| GO:0006987 | Activation of signaling protein activity involved in unfolded protein response | TAS | biological_process |
| GO:0007077 | Mitotic nuclear envelope disassembly | TAS | biological_process |
| GO:0007084 | Mitotic nuclear envelope reassembly | TAS | biological_process |
| GO:0007517 | Muscle organ development | IMP | biological_process |
| GO:0016607 | Nuclear speck | IEA | cellular_component |
| GO:0030334 | Regulation of cell migration | ISS | biological_process |
| GO:0030951 | Establishment or maintenance of microtubule cytoskeleton polarity | ISS | biological_process |
| GO:0030968 | Endoplasmic reticulum unfolded protein response | TAS | biological_process |
| GO:0034504 | Protein localization to nucleus | ISS | biological_process |
| GO:0035105 | Sterol regulatory element binding protein import into nucleus | IEA | biological_process |
| GO:0044267 | Cellular protein metabolic process | TAS | biological_process |
| GO:0048471 | Perinuclear region of cytoplasm | IDA | cellular_component |
| GO:0055015 | Ventricular cardiac muscle cell development | IEA | biological_process |
| GO:0071456 | Cellular response to hypoxia | IEP | biological_process |
| GO:0090201 | Negative regulation of release of cytochrome c from mitochondria | IEA | biological_process |
| GO:0090343 | Positive regulation of cell aging | IDA | biological_process |
| GO:2001237 | Negative regulation of extrinsic apoptotic signaling pathway | IEA | biological_process |
Entries Per Page
Displaying Page of
4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.9704349569 | 0.0229793511 | 0.9999902473 | 0.2916697203 |
- 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 | -0.0744243217 |
| GSE13712_SHEAR | Down | -0.3644191276 |
| GSE13712_STATIC | Up | 0.1117099012 |
| GSE19018 | Up | 0.1420852840 |
| GSE19899_A1 | Down | -0.9024964559 |
| GSE19899_A2 | Down | -0.5570023617 |
| PubMed_21979375_A1 | Down | -0.8709994819 |
| PubMed_21979375_A2 | Down | -0.7531589497 |
| GSE35957 | Down | -0.1959483554 |
| GSE36640 | Down | -0.1507263828 |
| GSE54402 | Down | -0.4147448649 |
| GSE9593 | Up | 0.0869903339 |
| GSE43922 | Down | -0.8725183741 |
| GSE24585 | Up | 0.2809795614 |
| GSE37065 | Down | -0.2425670893 |
| GSE28863_A1 | Up | 0.0259289969 |
| GSE28863_A2 | Up | 0.3312481978 |
| GSE28863_A3 | Down | -0.2463049515 |
| GSE28863_A4 | Down | -0.1252410961 |
| GSE48662 | Down | -0.2819315103 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-340-5p | MIMAT0004692 | MIRT019532 | Sequencing | Functional MTI (Weak) | 20371350 |
| hsa-miR-9-5p | MIMAT0000441 | MIRT021388 | Microarray | Functional MTI (Weak) | 17612493 |
| hsa-miR-124-3p | MIMAT0000422 | MIRT022394 | Proteomics;Microarray | Non-Functional MTI (Weak) | 18668037 |
| hsa-miR-296-3p | MIMAT0004679 | MIRT038445 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-615-3p | MIMAT0003283 | MIRT040169 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-let-7e-5p | MIMAT0000066 | MIRT051592 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-let-7a-5p | MIMAT0000062 | MIRT052409 | CLASH | Functional MTI (Weak) | 23622248 |
Entries Per Page
Displaying Page of
- mirRecord
No target information from mirRecord
- mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 27 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 28033363 | 7 years due to myocardial infarction or stroke, is caused by mutations in the LMNA gene |
| 28033363 | The LMNA mutation results in the deletion of 50 amino acids from the carboxy-terminal region of prelamin A, producing the truncated, farnesylated protein progerin |
| 27374873 | Hutchinson-Gilford Progeria Syndrome: A premature aging disease caused by LMNA gene mutations |
| 27374873 | Products of the LMNA gene, primarily lamin A and C, are key components of the nuclear lamina, a proteinaceous meshwork that underlies the inner nuclear membrane and is essential for proper nuclear architecture |
| 27374873 | In humans, hundreds of mutations in the LMNA gene have been identified and correlated with over a dozen degenerative disorders, referred to as laminopathies |
| 27120622 | Reduced prelamin A expression by siRNA targeted toward LMNA transcripts resulted in decreased nuclear anomalies |
| 26724531 | LMNA mutations resulting in lipodystrophy and HIV protease inhibitors trigger vascular smooth muscle cell senescence and calcification: Role of ZMPSTE24 downregulation |
| 26724531 | BACKGROUND: Some LMNA mutations responsible for lipodystrophies, and some HIV-protease inhibitors (PIs) induce accumulation of farnesylated prelamin A and premature senescence in some cell types |
| 26724531 | Patients with LMNA mutations or under PI-based therapy suffer from early atherosclerosis |
| 26724531 | AIM: We studied whether altered expression of ZMPSTE24 could contribute to vascular cell dysfunction in response to LMNA mutations or PI treatments |
| 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 | 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 |
| 26354777 | Depletion of LMNB1 or LMNA/C was sufficient to recapitulate some OIS features, including cell cycle exit and downregulation of NE proteins |
| 25961132 | These structures are also dependent on association of lamin A/C, a canonical component of the nucleoskeleton that is mutated in myriad human diseases, including human segmental progeroid syndromes |
| 25961132 | Since ITLs are associated with telomere stability and require functional lamin A/C, our study suggests a mechanistic link between cellular aging (replicative senescence induced by telomere shortening) and organismal aging (modeled by Hutchinson Gilford Progeria Syndrome) |
| 24603298 | The LMNA gene codes for lamin-A and lamin-C proteins, which are structural components of the nuclear lamina |
| 23849162 | BACKGROUND: Laminopathies, due to mutations in LMNA, encoding A type-lamins, can lead to premature ageing and/or lipodystrophic syndromes, showing that these diseases could have close physiopathological relationships |
| 23846499 | Lipodystrophy-linked LMNA p |
| 23846499 | OBJECTIVE: Some mutations in LMNA, encoding A-type lamins, are responsible for Dunnigan-type-familial partial lipodystrophy (FPLD2), with altered fat distribution and metabolism |
| 23846499 | The high prevalence of early and severe cardiovascular outcomes in these patients suggests that, in addition to metabolic risk factors, FPLD2-associated LMNA mutations could have a direct role on the vascular wall cells |
| 23846499 | APPROACH AND RESULTS: We analyzed the cardiovascular phenotype of 19 FPLD2 patients aged >30 years with LMNA p |
| 23846499 | CONCLUSIONS: LMNA p |
| 22895095 | Mutations in the LMNA gene are associated with a spectrum of human dystrophic diseases termed the "nuclear laminopathies |
| 22789011 | Additionally, human invasive ductal carcinoma (IDC) tissue arrays were used to confirm the hPTTG1/CXCR2/p21 axis established in vitro |
| 22541428 | Like HGPS cells, Lmna(-/-) and LmnaDelta9 fibroblasts have typically misshapen nuclei |
| 22541428 | Unexpectedly, Lmna(-/-) or LmnaDelta9 mice that are also deficient for the inner nuclear membrane protein Sun1 show markedly reduced tissue pathologies and enhanced longevity |
| 22470345 | Based on its senescence-dependent involvement in alternative splicing, we postulate that SRSF1 is a key marker of EC senescence, regulating the expression of alternative isoforms of target genes such as endoglin (ENG), vascular endothelial growth factor A (VEGFA), tissue factor (T3), or lamin A (LMNA) that integrate in a common molecular senescence program |
| 22340368 | Human longevity and common variations in the LMNA gene: a meta-analysis |
| 22340368 | 4 kb of the LMNA gene on a sample of long-lived individuals (LLI) (US Caucasians with age >/= 95 years, N=873) and genetically matched younger controls (N=443) |
| 22340368 | These results suggest that LMNA variants may play a role in human lifespan |
| 22297442 | Knowledge of the mechanism underlying prelamin A turnover is critical for the development of clinically effective protein inhibitors that can avoid accumulation to toxic levels without impairing lamin A/C expression, which is essential for normal biological functions |
| 21535365 | The expression of E2F target genes, normally required for cell cycle progression, was downregulated after lamin A/C depletion but restored after the inactivation of p53 |
| 21208065 | Phenotypic changes in nuclear structure and heterochromatin, resulting from increased progerin production following overuse of a cryptic splice site in the LMNA gene have profound effects on cell cycle progression and DNA repair mechanisms |
| 20819672 | Candidate genes including LMNA, ZMPSTE24, PPAR G, INSR and WRN were sequenced to screen for DNA variants |
| 20819672 | The mRNA and protein expression levels of LMNA were examined in primary fibroblasts |
| 20819672 | Nuclear abnormalities including nuclear blebs, mislocalization of lamin A/C were evident in the patient fibroblasts |
| 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 |
| 20069564 | This nuclear arrangement was influenced by deficiency of the histone methyltransferase SUV39h, LMNA deficiency, and the histone deacetylase inhibitor Trichostatin A (TSA) |
| 20069564 | This association was increased by SUV39h deficiency and decreased by LMNA deficiency |
| 20021393 | In both syndromes, alterations in specific genes have been identified, with mutations in the WRN and LMNA genes respectively being the most closely associated with each syndrome |
| 19589617 | R545C mutation in the LMNA gene |
| 19589617 | R545C) in the carboxy-terminal domain of the lamin A/C gene |
| 19589617 | The organization of both lamin A/C and its inner nuclear membrane partner emerin are altered, eventually showing a honeycomb pattern upon immunofluorescence microscopy |
| 19589617 | Altogether, these data suggest that the LMNA mutation p |
| 19172989 | The LMNA gene encodes two major proteins of the inner nuclear lamina, lamins A and C, but not much is known about their expression levels |
| 17612587 | Lipodystrophic syndromes associated with mutations in LMNA, encoding A-type lamins, and with HIV antiretroviral treatments share several clinical characteristics |
| 17612587 | Nuclear alterations and prelamin A accumulation have been reported in fibroblasts from patients with LMNA mutations and adipocytes exposed to protease inhibitors (PI) |
| 17612587 | As genetically altered lamin A maturation also results in premature ageing syndromes with lipodystrophy, we studied prelamin A expression and senescence markers in cultured human fibroblasts bearing six different LMNA mutations or treated with PIs |
| 17612587 | As compared to control cells, fibroblasts with LMNA mutations or treated with PIs had nuclear shape abnormalities and reduced proliferative activity that worsened with increasing cellular passages |
| 17612587 | Adipose tissue samples from patients with LMNA mutations or treated with PIs also showed retention of prelamin A, overexpression of the cell cycle checkpoint inhibitor p16 and altered mitochondrial markers |
| 17612587 | Thus, both LMNA mutations and PI treatment result in accumulation of farnesylated prelamin A and oxidative stress that trigger premature cellular senescence |
| 17415412 | Finally, we showed that EWS interacts with lamin A/C and that loss of EWS results in a reduced lamin A/C expression |
| 17415412 | Furthermore, we demonstrate a novel role of EWS in cellular senescence, possibly through its interaction and modulation of lamin A/C |
| 17274801 | The most extreme cases of apoptosis occur in cells derived from diseases with mutations in the tail region of the LMNA gene, such as Dunningan-type familial partial lipodystrophy and mandibuloacral dysplasia, and this correlates with a significant level of micronucleation in these cells |
| 16816143 | The family of laminopathies is a fast-growing group of diseases caused by abnormalities in the structure or processing of the lamin A/C (LMNA) gene |
| 16816143 | This review gives an overview of current knowledge on lamin structure and function and all known diseases associated with LMNA abnormalities |
Entries Per Page
Displaying Page of
