ArticlePloS one2008
A minimal fragment of MUC1 mediates growth of cancer cells.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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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
40 citing papers in PubMed, 75 citations in OpenAlex.
- Studying Macromolecular Composition in Cell-Cell Interfaces Using 3D Membrane Reconstitution Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Effective CAR T-cell targeting of an MUC1 cleavage product.Journal for immunotherapy of cancer · 2025Article
- Development of a label-free electrochemical aptasensor for Rift Valley fever virus detection.Scientific reports · 2024Article
- Mucin1 as a potential molecule for cancer immunotherapy and targeted therapy.Journal of Cancer · 2024Review
- Article
- Leveraging 3D Model Systems to Understand Viral Interactions with the Respiratory Mucosa.Viruses · 2020Review
- Novel Antibodies Targeting MUC1-C Showed Anti-Metastasis and Growth-Inhibitory Effects on Human Breast Cancer Cells.International journal of molecular sciences · 2020Article
- The glycoprotein mucin-1 negatively regulates GalNAc transferase 5 expression in pancreatic cancer.FEBS letters · 2019Article
- Use of CA15‑3 for screening breast cancer: An antibody‑lectin sandwich assay for detecting glycosylation of CA15‑3 in sera.Oncology reports · 2018Article
- The 'known-knowns', and 'known-unknowns' of extracellular Nm23-H1/NDPK proteins.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- Extracellular NME proteins: a player or a bystander?Laboratory investigation; a journal of technical methods and pathology · 2018Review
- Glycans define the stemness of naïve and primed pluripotent stem cells.Glycoconjugate journal · 2017Review
- Binding of Galectin-3, a β-Galactoside-binding Lectin, to MUC1 Protein Enhances Phosphorylation of Extracellular Signal-regulated Kinase 1/2 (ERK1/2) and Akt, Promoting Tumor Cell Malignancy.The Journal of biological chemistry · 2015Article
- Chemically tunable mucin chimeras assembled on living cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The case for extracellular Nm23-H1 as a driver of acute myeloid leukaemia (AML) progression.Naunyn-Schmiedeberg's archives of pharmacology · 2015Review
- Regulatory functions of Nm23-H2 in tumorigenesis: insights from biochemical to clinical perspectives.Naunyn-Schmiedeberg's archives of pharmacology · 2015Review
- MUC1: a multifaceted oncoprotein with a key role in cancer progression.Trends in molecular medicine · 2014Review
- MUC1 Is Expressed by Human Skin Fibroblasts and Plays a Role in Cell Adhesion and Migration.BioResearch open access · 2014Article
- Erythropoietin increases neuronal NDPKA expression, and NDPKA up-regulation as well as exogenous application protects cortical neurons from in vitro ischemia-related insults.Cellular and molecular neurobiology · 2014Article
- Human mucin MUC1 RNA undergoes different types of alternative splicing resulting in multiple isoforms.Cancer immunology, immunotherapy : CII · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The MUC1 protein is aberrantly expressed on many solid tumor cancers. In contrast to its apical clustering on healthy epithelial cells, it is uniformly distributed over cancer cells. However, a mechanistic link between aberrant expression and cancer has remained elusive. Herein, we report that a membrane-bound MUC1 cleavage product, that we call MUC1*, is the predominant form of the protein on cultured cancer cells and on cancerous tissues. Further, we demonstrate that transfection of a minimal fragment of MUC1, MUC1*(1110), containing a mere forty-five (45) amino acids of the extracellular domain, is sufficient to confer the oncogenic activities that were previously attributed to the full-length protein. By comparison of molecular weight and function, it appears that MUC1* and MUC1*(1110) are approximately equivalent. Evidence is presented that strongly supports a mechanism whereby dimerization of the extracellular domain of MUC1* activates the MAP kinase signaling cascade and stimulates cell growth. These findings suggest methods to manipulate this growth mechanism for therapeutic interventions in cancer treatments.
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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.