ArticleHistochemistry and cell biology2009
Protein phosphatase 1A (PPM1A) is involved in human cytotrophoblast cell invasion and migration.
Article in Histochemistry and cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Article
- Transcriptome Analysis, Machine Learning, and Experimental Identification of CDK7 Affecting the Progression of Pregnancy-induced Hypertension by Influencing Macrophage Polarization.Current molecular medicine · 2026Article
- A comprehensive overview of PPM1A: From structure to disease.Experimental biology and medicine (Maywood, N.J.) · 2022Review
- A novel group of genes that cause endocrine resistance in breast cancer identified by dynamic gene expression analysis.Oncotarget · 2022Article
- MicroRNA-487a-3p inhibits the growth and invasiveness of oral squamous cell carcinoma by targeting PPM1A.Bioengineered · 2021Article
- Cardiolipin, the Mitochondrial Signature Lipid: Implication in Cancer.International journal of molecular sciences · 2020Review
- Effect of miR-135b inhibitor on biological characteristics of osteosarcoma cells through up-regulating PPM1A.International journal of clinical and experimental pathology · 2019Article
- The phosphatase PPM1A inhibits triple negative breast cancer growth by blocking cell cycle progression.NPJ breast cancer · 2019Article
- Expression and potential mechanism of metabolism-related genes and CRLS1 in non-small cell lung cancer.Oncology letters · 2018Article
- Loss of PPM1A expression enhances invasion and the epithelial-to-mesenchymal transition in bladder cancer by activating the TGF-β/Smad signaling pathway.Oncotarget · 2014Article
- Article
- The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatases.British journal of pharmacology · 2012Review
- Delayed re-epithelialization in Ppm1a gene-deficient mice is mediated by enhanced activation of Smad2.The Journal of biological chemistry · 2011Article
- Increased c-Jun N-terminal kinase activation in human endometriotic endothelial cells.Histochemistry and cell biology · 2011Article
- Extending the knowledge in histochemistry and cell biology.Histochemistry and cell biology · 2010Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trophoblast invasion is crucial for embryo implantation and placentation. Excessive trophoblast invasion leads to hydatidiform moles and choriocarcinoma. PPM1A is a phosphatase which dephosphorylates and inactivates a broad range of substrates, including TGF-beta, MAP kinases, p38 and JNK kinase cascades, and is involved in tumor suppression. The objective of this study was to investigate the expression of PPM1A in normal and malignant human placenta and its role in trophoblast invasion, which shares many similarities with invasion of tumor cells. By Western blotting and immunocytochemistry, significantly higher expression of PPM1A in human placental villi at term was found as compared with that during the first trimester. Furthermore, the expression level of PPM1A protein in hydatidiform moles was lower compared with that during normal pregnancy. We further investigated the function of PPM1A in extravillous trophoblast cell line HTR8/SVneo. Transwell migration and Matrigel invasion assays demonstrated that PPM1A siRNA significantly promoted the motility and invasiveness of the cells. Gelatin zymography showed that knockdown of PPM1A with siRNA elevated the expression of pro-matrix metalloproteinase pro-(MMP)-9, but down-regulated tissue inhibitors of metalloproteinases (TIMP)-2. The present data indicate that PPM1A plays a critical role in the regulation of normal placentation by inhibiting trophoblast migration and invasion.
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