Clinical significance of cancerous inhibitor of protein phosphatase 2A in human cancers
Open accessAbstract
Cancerous Inhibitor of Protein Phosphatase 2A (CIP2A), a recently identified oncogene, has emerged as a potential drug target for a range of different tumor types. High CIP2A expression has been reported in almost all solid organ cancers and in some hematological tumors and is associated with high grade and poor prognosis. Notably, high CIP2A expression is determined in over 70% of tumor patient samples in the majority of human cancers. High expression of CIP2A has also been proposed as a useful biomarker that predicts therapeutic response to chemotherapeutics such as Bortezomib, Erlotinib, Checkpoint Kinase 1 inhibitors and pro‐senescence based therapies. In this review, we highlight, critically evaluate and discuss the ambiguity in CIP2A's prognostic role in different human cancers and its role in modulating response and resistance to chemotherapeutics.
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High CIP2A protein expression predicts poor patient survival in over a dozen different cancer types.
“high CIP2A protein expression predicts poor patient survival in over a dozen different cancer types [20]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [20]
The Prognostic Role section says CIP2A expression has an established prognostic role in over 10 tumor types and reports associations with poorer survival in several cancers. It does not establish the claim’s more specific count of over a dozen types with poor survival predicted by high CIP2A protein expression; the section also notes conflicting prognostic findings. (LLM, conf=0.85)
Experimental — accuracy not yet measuredCIP2A shows the most prevalent overexpression and is associated with poor patient survival across different types of cancer.
“Among these proteins, CIP2A shows the most prevalent overexpression and is associated with poor patient survival across different types of cancer [20].”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [20]
The Conclusion describes CIP2A overexpression as one of the commonest molecular alterations in human cancers, and the Prognostic Role section reports associations with poor survival in several cancer types. Neither passage establishes that CIP2A has the most prevalent overexpression among the proteins the citing sentence compares it with; the review also notes exceptions to the survival association. Page numbers were not available in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredHigh CIP2A expression associates with poor patient survival in more than 15 different human cancer types.
“and its high expression associates with poor patient survival in more than 15 different human cancer types [20].”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [20]
The Prognostic Role section reports that CIP2A expression has an established prognostic role in over 10 tumor types and describes associations with poorer survival in several cancers. It does not establish the claim’s more specific count of more than 15 cancer types with a poor-survival association; the review also notes conflicting prognostic findings in some cancers. No page number is available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCIP2A drives tumour growth in xenograft and transgenic mouse models.
“Of these, CIP2A is widely over-expressed in different human cancer types and drives tumour growth both in xenograft and transgenic mouse models18–24.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [19]
The Abstract says CIP2A promotes carcinogenesis, and the ‘Role of CIP2A as a Biomarker for Anticancer Drugs’ section describes it as an effector of tumour growth. Neither passage reports tumour-growth results from xenograft or transgenic mouse models; the mouse findings in the Abstract concern lifespan and fibroblast senescence instead. (LLM, conf=0.78)
Experimental — accuracy not yet measuredCIP2A is widely over-expressed in different human cancer types.
“Of these, CIP2A is widely over-expressed in different human cancer types and drives tumour growth both in xenograft and transgenic mouse models18–24.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [19]
High CIP2A protein expression is observed across human cancers.
“high CIP2A protein expression, as observed across human cancers19,33.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [19]
CIP2A is overexpressed in many human cancers, and high CIP2A expression correlates with poor patient survival across a broad spectrum of malignancies.
“CIP2A is overexpressed in a vast variety of human cancers, and high CIP2A expression has been shown to correlate with poor patient survival in a broad spectrum of human malignancies (3)(4)(5)(6).”
From Discovery of a Novel CIP2A Variant (NOCIVA) with Clinical Relevance in Predicting TKI Resistance in Myeloid Leukemias (2021) · cites this paper as [5]
CIP2A is overexpressed with high frequency in most human malignancies.
“but it is overexpressed with high frequency in most human malignancies (4,7).”
From Ovarian cancers with low CIP2A tumor expression constitute an APR-246 sensitive disease subtype (2021) · cites this paper as [7]
Among these cancer types there is a significant number of patients with CIP2A low subtype.
“Similar to OvCa, also among these cancer types there is a significant number of patients with CIP2A low subtype (4, 7).”
From Ovarian cancers with low CIP2A tumor expression constitute an APR-246 sensitive disease subtype (2021) · cites this paper as [7]
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Self-citation
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- V C 2015 UICC 10970215, 2016, 3, Downloaded from https://onlinelibrary.wiley.com/doi/10.1002/ijc.29431, Wiley Online Library on [14/08/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
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Non-genomic mechanisms of protein phosphatase 2A (PP2A) regulation in cancer
Kauko, O., & Westermarck, J. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.01.005 · Cited by 111 · see citing works
Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56
Wang, J., Okkeri, J., Pavic, K., Wang, Z., Kauko, O., Halonen, T., Sarek, G., Ojala, P. M., Rao, Z., Xu, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201642788 · Cited by 95 · see citing works
Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96 · see citing works
Laine, A., Nagelli, S. G., Farrington, C., Butt, U., Cvrljevic, A. N., Vainonen, J. P., Feringa, F. M., Grönroos, T. J., Gautam, P., Khan, S., et al. (2020) · doi:10.1101/2020.08.27.269902 · Cited by 54 · see citing works
Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A
Pavic, K., Gupta, N., Omella, J. D., Derua, R., Aakula, A., Huhtaniemi, R., Määttä, J. A., Höfflin, N., Okkeri, J., Wang, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36693-9 · Cited by 36 · see citing works
“The data show that the CIP2A(1-560) residues cross-linked to B56α are located primarily in the N-terminal head domain (K18, K21, E23, E34, K40) with an additional residue at the C-terminus (K490) (Fig.”
BackgroundMethodInfluentialMäkelä, E., Pavic, K., Varila, T., Salmenniemi, U., Löyttyniemi, E., Nagelli, S. G., Ammunét, T., Kähäri, V.-M., Clark, R. E., Elo, L. L., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-3679 · Cited by 18 · see citing works
Ovarian Cancers with Low CIP2A Tumor Expression Constitute an APR-246–Sensitive Disease Subtype
Cvrljevic, A. N., Butt, U., Huhtinen, K., Grönroos, T. J., Böckelman, C., Lassus, H., Butzow, R., Haglund, C., Kaipio, K., Arsiola, T., et al. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0622 · Cited by 5 · see citing works
Ovarian cancers with low CIP2A tumor expression constitute an APR-246 sensitive disease subtype
Cvrljevic, A. N., Butt, U., Huhtinen, K., Grönroos, T. J., Böckelman, C., Lassus, H., Kaipio, K., Arsiola, T., Laajala, T. D., Connolly, D. C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.31.437804 · Cited by 5 · see citing works
- Authors
- Khanna, A., & Pimanda, J. E.
- Affiliations
- UNSW Sydney (AU)
- Corresponding author
- Khanna, Anchit
- ORCID
- Pimanda, John E.
- Venue
- International Journal of Cancer
- Publisher
- Wiley
- Published
- 2015-01-28
- Volume
- 138
- Issue
- 3
- Pages
- 525-532
- ISSN
- 0020-7136 (ISSN-L)
- 1097-0215
- OpenAlex
- W1682873785
- Cited by
- 57
- References
- 79
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 2 · 2023: 7 · 2022: 4 · 2021: 6 · 2020: 2 · 2019: 4 · 2018: 10 · 2017: 7 · 2016: 4 · 2015: 6
- FWCI
- 1.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- International Journal of Cancer (publishedVersion)
- PubMed (publishedVersion)
- UNSWorks (UNSW Sydney) (submittedVersion, cc-by-nc-nd)
- UNSWorks (University of New South Wales, Sydney, Australia) (submittedVersion, cc-by-nc-nd)
- Funders
- National Health and Research Medical Council (NH&MRC)-Peter-Doherty Research Fellow
- National Health and Research Medical Council (NH&MRC), Australia
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- CIP2A, protein phosphatase 2A inhibitor, oncogenes, prognostic factors, chemotherapy response, chemoresistance, bortezomib, erlotinib, senescence therapy, solid organ cancer, hematologic cancer
- MeSH terms
- Checkpoint Kinase 1, Autoantigens, Humans, Membrane Proteins, Neoplasms, Prognosis, Protein Kinases, Biomarkers, Tumor, Genes, myc, Intracellular Signaling Peptides and Proteins
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