ArticleOncogene2004
LMW-PTP is a positive regulator of tumor onset and growth.
Article in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed, 104 citations in OpenAlex.
- Structure-Based Design of Active-Site-Directed, Highly Potent, Selective, and Orally Bioavailable Low-Molecular-Weight Protein Tyrosine Phosphatase Inhibitors.Journal of medicinal chemistry · 2022Article
- A bacterial tyrosine phosphatase modulates cell proliferation through targeting RGCC.PLoS pathogens · 2021Article
- Low molecular weight protein tyrosine phosphatase as signaling hub of cancer hallmarks.Cellular and molecular life sciences : CMLS · 2021Review
- Protein Tyrosine Phosphatases: A new paradigm in an old signaling system?Advances in cancer research · 2021Review
- Review
- EPHA2 mutations with oncogenic characteristics in squamous cell lung cancer and malignant pleural mesothelioma.Oncogenesis · 2019Article
- Discovery of the Oncogenic Parp1, a Target of bcr-abl and a Potential Therapeutic, in mir-181a/PPFIA1 Signaling Pathway.Molecular therapy. Nucleic acids · 2019Article
- LMW-PTP targeting potentiates the effects of drugs used in chronic lymphocytic leukemia therapy.Cancer cell international · 2019Article
- Targeting LMW-PTP to sensitize melanoma cancer cells toward chemo- and radiotherapy.Cancer medicine · 2018Article
- Early quantitative profiling of differential retinal protein expression in lens-induced myopia in guinea pig using fluorescence difference two-dimensional gel electrophoresis.Molecular medicine reports · 2018Article
- Diabetes reversal by inhibition of the low-molecular-weight tyrosine phosphatase.Nature chemical biology · 2017Article
- Review
- Phosphoproteomic analysis of interacting tumor and endothelial cells identifies regulatory mechanisms of transendothelial migration.Science signaling · 2016Article
- Deletion of low molecular weight protein tyrosine phosphatase (Acp1) protects against stress-induced cardiomyopathy.The Journal of pathology · 2015Article
- Low molecular weight protein tyrosine phosphatase (LMWPTP) upregulation mediates malignant potential in colorectal cancer.Oncotarget · 2015Article
- Antitumor activity of irradiated riboflavin on human renal carcinoma cell line 786-O.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Article
- Protein tyrosine phosphatases as potential therapeutic targets.Acta pharmacologica Sinica · 2014Review
- The regulatory roles of phosphatases in cancer.Oncogene · 2014Review
- Eph receptor signaling and ephrins.Cold Spring Harbor perspectives in biology · 2013Review
- The role of low-molecular-weight protein tyrosine phosphatase (LMW-PTP ACP1) in oncogenesis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Low molecular weight protein tyrosine phosphatases (LMW-PTPs) are an enzyme family that plays a key role in cell proliferation control by dephosphorylating/inactivating both tyrosine kinase receptors (such as PDGF, insulin, and ephrin receptors) and docking proteins (such, as beta-catenin) endowed with both adhesion and transcriptional activity. Besides being a frequent event in human tumors, overexpression of LMW-PTP has been recently demonstrated to be sufficient to induce neoplastic transformation. We recently demonstrated that overexpression of LMW-PTP strongly potentiates the stability of cell-cell contacts at the adherens junction level, which powerfully suggests that LMW-PTP may also contribute to cancer invasivity. Focusing on mechanisms by which LMW-PTP is involved in cancer onset and progression, the emerging picture is that LMW-PTP strongly increases fibronectin-mediated cell adhesion and mobility but, paradoxically, decreases cell proliferation. Nevertheless, LMW-PTP-transfected NIH3T3 fibroblasts engrafted in nude mice induce the onset of larger fibrosarcomas, which are endowed with higher proliferation activity as compared to mock-transfected controls. Quite opposite effects have been obtained with engrafted fibroblasts transfected with a dominant-negative form of LMW-PTP. Notably, in sarcoma extracts, LMW-PTP overexpression greatly influences the ephrin A2 (EphA2) but not PDGF receptor or beta-catenin tyrosine phosphorylation. The high association of dephosphorylated EphA2 overexpression with most human cancers and our observation that cell growth stimulation by LMW-PTP overexpression is restricted to the in vivo model, strongly suggest that LMW-PTP oncogenic potential is mediated by its EphA2 tyrosine dephosphorylating activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.