Precise definition of PTEN C-terminal epitopes and its implications in clinical oncology
Open accessAbstract
Anti-PTEN monoclonal antibodies (mAb) are arising as important tools for immunohistochemistry (IHC) and protein quantification routine analysis in clinical oncology. Although an effort has been made to document the reliability of tumor tissue section immunostaining by anti-PTEN mAb, and to standardize their IHC use in research and in the clinical practice, the precise topological and biochemical definition of the epitope recognized by each mAb has been conventionally overlooked. In this study, six commercial anti-PTEN mAb have been validated and characterized for sensitivity and specificity by IHC and FISH, using a set of prostate and urothelial bladder tumor specimens, and by immunoblot, using PTEN positive and PTEN negative human cell lines. Immunoblot precise epitope mapping, performed using recombinant PTEN variants and mutations, revealed that all mAb recognized linear epitopes of 6–11 amino acid length at the PTEN C-terminus. Tumor-associated or disease-associated mutations at the PTEN C-terminus did not affect subcellular localization or PIP3 phosphatase activity of PTEN in cells, although resulted in specific loss of reactivity for some mAb. Furthermore, specific mimicking-phosphorylation mutations at the PTEN C-terminal region also abolished binding of specific mAb. Our study adds new evidence on the relevance of a precise epitope mapping in the validation of anti-PTEN mAb for their use in the clinics. This will be substantial to provide a more accurate diagnosis in clinical oncology based on PTEN protein expression in tumors and biological fluids.
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Recruitment and the extent of activation of membrane-associated PTEN depend on membrane composition, including surface characteristics such as charge.
“Recruitment and the extent of activation of membrane-associated PTEN depends on the composition, and thus the surface characteristics such as charge, of the membrane (reviewed in [187]).”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [187]
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Nunes‐Xavier, C. E., Mingo, J., Emaldi, M., Karlsen, K. F., Mælandsmo, G. M., Fodstad, Ø., Llarena, R., Lopez, J. I., & Pulido, R. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.873516 · Cited by 17 · see citing works
Self-citationLuna, S., Torices, L., Mingo, J., Amo, L., Rodríguez‐Escudero, I., Ruiz‐Ibarlucea, P., Erramuzpe, A., Cortés, J. M., Tejada, M., Molina, M., et al. (2021) · Human Mutation · doi:10.1002/humu.24186 · Cited by 16 · see citing works
Self-citationPrecise Immunodetection of PTEN Protein in Human Neoplasia.Preprint
Pulido, R., Mingo, J., Gaafar, A., Nunes-Xavier, C., Luna, S., Torices, L., Angulo, J., & López, J. (2019) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a036293 · Cited by 17 · see citing works
Self-citationEmaldi, M., Rey‐Iborra, E., Marín, Á., Mosteiro, L., Lecumberri, D., Øyjord, T., Roncier, N., Mælandsmo, G. M., Angulo, J. C., Errarte, P., et al. (2024) · OncoImmunology · doi:10.1080/2162402x.2024.2419686 · Cited by 9 · see citing works
Self-citationUtilizing PTEN immunohistochemistry as a screening test for Cowden syndrome
Hartsough, E. M., DeSimone, M. S., Lorenzo, M. E., Dias-Santagata, D. C., Nosé, V., & Hoang, M. P. (2024) · American Journal of Clinical Pathology · doi:10.1093/ajcp/aqad177 · Cited by 9 · see citing works
Chemical and structural approaches to investigate PTEN function and regulation
Viennet, T., Ospina, S. R., Lu, Y., Cui, A., Arthanari, H., & Dempsey, D. R. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.007 · Cited by 9 · see citing works
Murthy, A. S. N., Suresh, R. V., & Ramachandra, N. B. (2020) · Genomics · doi:10.1016/j.ygeno.2020.10.035 · Cited by 5 · see citing works
Mishra, R. K., Ahmad, A., Vyawahare, A., Kumar, A., & Khan, R. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200616133814 · Cited by 6 · see citing works
Brain Circuit Alterations and Cognitive Disability in Late-Onset Cobalamin D Disorder
Heras, J. D. L., Diez, I. P., Jiménez-Marín, A., Cabrera, A., Ramos‐Usuga, D., Diaz-Fernandez, M. V., Torices, L., Nunes‐Xavier, C. E., Pulido, R., Arango‐Lasprilla, J. C., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9040990 · Cited by 5 · see citing works
Self-citationTorices, L., Heras, J. D. L., Arango‐Lasprilla, J. C., Cortés, J. M., Nunes‐Xavier, C. E., & Pulido, R. (2021) · Molecular Genetics and Metabolism Reports · doi:10.1016/j.ymgmr.2021.100710 · Cited by 4 · see citing works
Self-citationTorices, L., Nunes‐Xavier, C. E., Mingo, J., Luna, S., Erramuzpe, A., Cortés, J. M., & Pulido, R. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3569-8_1 · Cited by 3 · see citing works
Self-citationTorices, L., Nunes‐Xavier, C. E., & Pulido, R. (2024) · Cancers · doi:10.3390/cancers16162836 · Cited by 3 · see citing works
Self-citationTorices, L., Nunes‐Xavier, C. E., Lopez, J. I., & Pulido, R. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289369 · Cited by 2 · see citing works
Self-citationProbing the properties of PTEN specific botulinum toxin type E mutants
Schiavone, G., Richter, S., Henke, T., Koch, I., Thies, L., Klöpper, F., Megighian, A., Pirazzini, M., & Binz, T. (2025) · Journal of Neural Transmission · doi:10.1007/s00702-025-02879-2
Specificity of Aberrant Exons in a Saturated Background of Differentially Expressed ExonsPreprint
Das, U., Nguyen, H. D., Yang, J., Ogunsola, S. S., Hamilton, M., Wu, Y., Liu, L., Cao, W., Liu, C., & Xie, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.25.661610
Sajjadi, E., Venetis, K., Piciotti, R., Gambini, D., Blundo, C., Runza, L., Ferrero, S., Guerini-Rocco, E., & Fusco, N. (2021) · Figshare · doi:10.6084/m9.figshare.16893094
Sajjadi, E., Venetis, K., Piciotti, R., Gambini, D., Blundo, C., Runza, L., Ferrero, S., Guerini-Rocco, E., & Fusco, N. (2021) · Figshare · doi:10.6084/m9.figshare.16893091
Kolesarić, N., Pezelj, I., Tomašković, I., Štimac, G., Ulamec, M., & Krušlin, B. (2026) · Cancers · doi:10.3390/cancers18152477
- Authors
- Mingo, J., Luna, S., Gaafar, A., Nunes-Xavier, C. E., Torices, L., Mosteiro, L., Ruiz, R., Guerra, I., Llarena, R., Angulo, J. C., López, J. I., & Pulido, R.
- Affiliations
- BioCruces Health research Institute (ES)
- Hospital de Cruces (ES)
- Hospital Universitario Araba (ES)
- University of the Basque Country (ES)
- Hospital Universitario de Getafe (ES)
- Ikerbasque (ES)
- Corresponding author
- Pulido, Rafael
- Venue
- npj Precision Oncology
- Published
- 2019-04-15
- Volume
- 3
- Issue
- 1
- Pages
- 11-11
- ISSN
- 2397-768X (ISSN-L)
- PMC
- PMC6465295
- OpenAlex
- W2939521850
- Cited by
- 22
- References
- 84
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 2 · 2022: 3 · 2021: 6 · 2020: 4 · 2019: 1
- FWCI
- 1.16
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- npj Precision Oncology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ABACUS. Repositorio de Producción Científica (Universidad Europea) (submittedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Ministerio de Economía y Competitividad (SAF2013-48812-R, SAF2016-79847-R)
- The Norwegian Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- PTEN, epitope mapping, C-terminal epitope, antibody validation, prostate cancer, bladder urothelial carcinoma, PTEN mutation, subcellular localization, immunohistochemistry, fluorescence in situ hybridization
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