ArticleTranslational cancer research2020
Metallothionein 1M (MT1M) inhibits lung adenocarcinoma cell viability, migration, and expression of cell mobility-related proteins through MDM2/p53/MT1M signaling.
Article in Translational cancer research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Harnessing the TAF1 Acetyltransferase for Targeted Acetylation of the Tumor Suppressor p53.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- ProstaMine: a bioinformatics tool for identifying subtype-specific co-alterations associated with aggressiveness in prostate cancer.Frontiers in pharmacology · 2024Article
- Risk prediction for dermatomyositis-associated hepatocellular carcinoma.BMC bioinformatics · 2023Article
- Dermatomyositis with intrahepatic cholangiocarcinoma: a case report and data mining based on machine learning.Frontiers in oncology · 2023Article
- Tumor cell cytoplasmic metallothionein expression associates with differential tumor immunogenicity and prognostic outcome in high-grade serous ovarian carcinoma.Frontiers in oncology · 2023Article
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Authors and funding
6 authors.
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Abstract
backgroundMetallothionein 1M (MT1M) functions to regulate cell proliferation and cancer metastasis. This study assessed the effects of MT1M overexpression and mouse double minute 2 homolog (MDM2) knockdown on the regulation of non-small cell lung cancer A549 cell viability, migration, and protein expression
methodsA549 cells were stably infected with lentivirus carrying MT1M cDNA or transiently transfected MDM2 siRNA and/or treated with the p53 inhibitor for the assessment of changes in cell viability, wound healing, Transwell migration, and qRT-PCR and Western blot assays. Luciferase reporter assay was performed to investigate p53 binding to the MT1M promoter.
resultsThe data showed that MT1M overexpression inhibited A549 cell viability and migration capacity
conclusionsIn conclusion, MDM2 can bind to and phosphorylate p53 protein to inactivate the protein, thereby reducing MT1M expression and leading to tumor cell proliferation and migration.
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