ArticleCancer research2009
Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration.
Article in Cancer research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07438860 (Fluorescence-Guided Imaging of Brain Tumors), which is not on this map. Cited by 49 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Fluorescence-Guided Imaging of Brain Tumors: A Safety Study Using SBK2- ICG in a Phase 1 Clinical Trial
Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.
- Systematic review of protein biomarkers of invasive behavior in glioblastoma.Molecular neurobiology · 2014Pooled it
- Dimensional memory in glioblastoma mechanics: Traction force analysis of cells cultured in 2D versus 3D collagen environments.Bioactive materials · 2026Article
- A novel binding pocket in the D2 domain of protein tyrosine phosphatase mu (PTPmu) guides AI screen to identify small molecules that modulate tumour cell adhesion, growth and migration.Journal of cellular and molecular medicine · 2023Article
- Role of protein tyrosine phosphatase receptor type M in epithelial ovarian cancer progression.Journal of ovarian research · 2023Article
- Artificial Intelligence-Based Computational Screening and Functional Assays Identify Candidate Small Molecule Antagonists of PTPmu-Dependent Adhesion.International journal of molecular sciences · 2023Article
- Article
- Therapeutic Potential of Targeting Regulated Intramembrane Proteolysis Mechanisms of Voltage-Gated Ion Channel Subunits and Cell Adhesion Molecules.Pharmacological reviews · 2022Review
- The complex interactions between the cellular and non-cellular components of the brain tumor microenvironmental landscape and their therapeutic implications.Frontiers in oncology · 2022Review
- Ultrasound-Based Molecular Imaging of Tumors with PTPmu Biomarker-Targeted Nanobubble Contrast Agents.International journal of molecular sciences · 2021Article
- Detection of Tumor-Specific PTPmu in Gynecological Cancer and Patient Derived Xenografts.Diagnostics (Basel, Switzerland) · 2021Article
- PTPmu-targeted nanoparticles label invasive pediatric and adult glioblastoma.Nanomedicine : nanotechnology, biology, and medicine · 2020Article
- RIP at the Synapse and the Role of Intracellular Domains in Neurons.Neuromolecular medicine · 2020Review
- DDIAS promotes STAT3 activation by preventing STAT3 recruitment to PTPRM in lung cancer cells.Oncogenesis · 2020Article
- PTPRM, a candidate tumor suppressor gene in small intestinal neuroendocrine tumors.Endocrine connections · 2019Article
- Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma.Cellular and molecular life sciences : CMLS · 2019Review
- A PTPmu Biomarker is Associated with Increased Survival in Gliomas.International journal of molecular sciences · 2019Article
- Review
- The impact of phosphatases on proliferative and survival signaling in cancer.Cellular and molecular life sciences : CMLS · 2018Review
- Review
- SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.BMC bioinformatics · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Glioblastoma multiforme (GBM), the most common malignant primary brain tumor, represents a significant disease burden. GBM tumor cells disperse extensively throughout the brain parenchyma, and the need for tumor-specific drug targets and pharmacologic agents to inhibit cell migration and dispersal is great. The receptor protein tyrosine phosphatase mu (PTPmu) is a homophilic cell adhesion molecule. The full-length form of PTPmu is down-regulated in human glioblastoma. In this article, overexpression of full-length PTPmu is shown to suppress migration and survival of glioblastoma cells. Additionally, proteolytic cleavage is shown to be the mechanism of PTPmu down-regulation in glioblastoma cells. Proteolysis of PTPmu generates a series of proteolytic fragments, including a soluble catalytic intracellular domain fragment that translocates to the nucleus. Only proteolyzed PTPmu fragments are detected in human glioblastomas. Short hairpin RNA-mediated down-regulation of PTPmu fragments decreases glioblastoma cell migration and survival. A peptide inhibitor of PTPmu function blocks fragment-induced glioblastoma cell migration, which may prove to be of therapeutic value in GBM treatment. These data suggest that loss of cell surface PTPmu by proteolysis generates catalytically active PTPmu fragments that contribute to migration and survival of glioblastoma cells.
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What OpenQuestion holds
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.