ArticleOncotarget2014
Intracellular and extracellular domains of protein tyrosine phosphatase PTPRZ-B differentially regulate glioma cell growth and motility.
Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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
18 citing papers in PubMed, 40 citations in OpenAlex.
- Dysregulation of post-translational modifications in glioma: advances in pathological mechanisms and clinical targeting strategies.Journal of translational medicine · 2026Review
- Vaccine-induced T cell receptor T cell therapy targeting a glioblastoma stemness antigen.Nature communications · 2025Article
- Protein Tyrosine Phosphatase Receptor Zeta 1 as a Potential Target in Cancer Therapy and Diagnosis.International journal of molecular sciences · 2023Review
- Detection and genomic analysis of BRAF fusions in Juvenile Pilocytic Astrocytoma through the combination and integration of multi-omic data.BMC cancer · 2022Article
- The landscape of receptor-mediated precision cancer combination therapy via a single-cell perspective.Nature communications · 2022Article
- Macropinocytosis requires Gal-3 in a subset of patient-derived glioblastoma stem cells.Communications biology · 2021Article
- Discovering and interpreting transcriptomic drivers of imaging traits using neural networks.Bioinformatics (Oxford, England) · 2020Article
- Cell migration through three-dimensional confining pores: speed accelerations by deformation and recoil of the nucleus.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Article
- Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma.Cellular and molecular life sciences : CMLS · 2019Review
- Review
- Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases.Molecules (Basel, Switzerland) · 2018Review
- Humanized chondroitinase ABC sensitizes glioblastoma cells to temozolomide.The journal of gene medicine · 2017Article
- Glioma: experimental models and reality.Acta neuropathologica · 2017Review
- Glycoprotein non-metastaticmelanoma protein B promotes glioma motility and angiogenesis through the Wnt/β-catenin signaling pathway.Experimental biology and medicine (Maywood, N.J.) · 2016Article
- Comprehensive protein tyrosine phosphatase mRNA profiling identifies new regulators in the progression of glioma.Acta neuropathologica communications · 2016Article
- Small-molecule inhibition of PTPRZ reduces tumor growth in a rat model of glioblastoma.Scientific reports · 2016Article
- Chicoric acid binds to two sites and decreases the activity of the YopH bacterial virulence factor.Oncotarget · 2016Article
- Identification of a novel MET mutation in high-grade glioma resulting in an auto-active intracellular protein.Acta neuropathologica · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gliomas are primary brain tumors for which surgical resection and radiotherapy is difficult because of the diffuse infiltrative growth of the tumor into the brain parenchyma. For development of alternative, drug-based, therapies more insight in the molecular processes that steer this typical growth and morphodynamic behavior of glioma cells is needed. Protein tyrosine phosphatase PTPRZ-B is a transmembrane signaling molecule that is found to be strongly up-regulated in glioma specimens. We assessed the contribution of PTPRZ-B protein domains to tumor cell growth and migration, via lentiviral knock-down and over-expression using clinically relevant glioma xenografts and their derived cell models. PTPRZ-B knock-down resulted in reduced migration and proliferation of glioma cells in vitro and also inhibited tumor growth in vivo. Interestingly, expression of only the PTPRZ-B extracellular segment was sufficient to rescue the in vitro migratory phenotype that resulted from PTPRZ-B knock-down. In contrast, PTPRZ-B knock-down effects on proliferation could be reverted only after re-expression of PTPRZ-B variants that contained its C-terminal PDZ binding domain. Thus, distinct domains of PTPRZ-B are differentially required for migration and proliferation of glioma cells, respectively. PTPRZ-B signaling pathways therefore represent attractive therapeutic entry points to combat these tumors.
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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.