CIP2A is a target of bortezomib in human triple negative breast cancer cells
Open accessAbstract
Introduction: Triple negative breast cancer (TNBC) is very aggressive and currently has no specific therapeutic targets, such as hormone receptors or human epidermal growth factor receptor type 2 (HER2); therefore, prognosis is poor. Bortezomib, a proteasome inhibitor, may exert efficacy in TNBC through its multiple cellular effects. Here, we tested the efficacy of bortezomib and examined the drug mechanism in breast cancer cells. Methods: Five breast cancer cell lines: TNBC HCC-1937, MDA-MB-231, and MDA-MB-468; HER2-overexpressing MDA-MB-453; and estrogen receptor positive MCF-7 were used for in vitro studies. Apoptosis was examined by both flow cytometry and Western Blot. Signal transduction pathways in cells were assessed by Western Blot. Gene silencing was done by small interfering RNA (siRNA). In vivo efficacy of bortezomib was tested in nude mice with breast cancer xenografts. Immunohistochemical study was performed on tumor tissues from patients with TNBC. Results: Bortezomib induced significant apoptosis, which was independent of its proteasome inhibition, in the three TNBC cell lines, but not in MDA-MB-453 or MCF-7 cells. Furthermore, cancerous inhibitor of protein phosphatase 2A (CIP2A), a cellular inhibitor of protein phosphatase 2A (PP2A), mediated the apoptotic effect of bortezomib. We showed that bortezomib inhibited CIP2A in association with p-Akt downregulation in a dose- and time-dependent manner in all sensitive TNBC cells, whereas no alterations in CIP2A expression and p-Akt were noted in bortezomib-resistant cells. Overexpression of CIP2A upregulated p-Akt and protected MDA-MB-231 and MDA-MB-468 cells from bortezomib-induced apoptosis, whereas silencing CIP2A by siRNA overcame the resistance to bortezomib-induced apoptosis in MCF-7 cells. In addition, bortezomib downregulated CIP2A mRNA but did not affect the degradation of CIP2A protein. Furthermore, bortezomib exerted in vivo antitumor activity in HCC-1937 xenografted tumors, but not in MCF-7 tumors. Bortezomib downregulated CIP2A expression in the HCC-1937 tumors but not in the MCF-7 tumors. Importantly, CIP2A expression is readily detectable in tumor samples from TNBC patients. Conclusions: CIP2A is a major determinant mediating bortezomib-induced apoptosis in TNBC cells. CIP2A may thus be a potential therapeutic target in TNBC.
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CIP2A promotes phosphorylation and activity of both MYC and Akt.
“CIP2A has been shown to promote phosphorylation and activity of both of these critical PP2A targets [6,9,10,12,16]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [9]
The Introduction says CIP2A inhibits PP2A activity toward c-Myc, and the Results (Figure 3) report higher phospho-Akt in cells overexpressing CIP2A. These passages support CIP2A’s effects on the two targets, but the paper does not explicitly establish increased phosphorylation and activity of MYC or increased Akt activity as distinct outcomes. Page numbers are unavailable in our copy. (LLM, conf=0.82)
Experimental — accuracy not yet measuredInhibition of L533E mutant expression correlated with significantly lower capacity to support expression of the CIP2A target pAkt compared to WT CIP2A.
“Furthermore, inhibition of L533E mutant expression correlated very well with significantly lower capacity to support expression of a well-established CIP2A target pAkt [9,16], as compared to WT CIP2A (Fig 5K and L).”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [9]
CIP2A is a long-lived protein in cancer cells.
“CIP2A is a long-lived protein in cancer cells [9]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [9]
The Results (Figure 4A; page unavailable) assess CIP2A protein stability in breast cancer cells, and the Discussion says bortezomib did not affect its degradation half-life. Neither passage states how long CIP2A persists or establishes that it is a long-lived protein. (LLM, conf=0.75)
Experimental — accuracy not yet measuredCIP2A is a very long-lived protein.
“as CIP2A is a very long-lived protein [9]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [9]
The Results section (‘Bortezomib downregulates transcription of CIP2A in breast cancer cells’; page unavailable) measures CIP2A degradation after blocking protein synthesis, but reports only that bortezomib did not significantly change its degradation rate. The Discussion likewise says bortezomib did not affect CIP2A’s half-life. Neither passage states how long that half-life is or establishes that CIP2A is very long-lived. (LLM, conf=0.76)
Experimental — accuracy not yet measured
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- Authors
- Tseng, L.-M., Liu, C.-Y., Chang, K.-C., Chu, P.-Y., Shiau, C.-W., & Chen, K.-F.
- Affiliations
- Taipei Veterans General Hospital (TW)
- St. Martin de Porres Hospital (TW)
- National Yang Ming University (TW)
- National Taiwan University Hospital (TW)
- Corresponding author
- Liu, Chun-Yu
- Chen, Kuen-Feng
- Venue
- Breast Cancer Research
- Published
- 2012-04-26
- Volume
- 14
- Issue
- 2
- Pages
- R68-R68
- ISSN
- 1465-5411 (ISSN-L)
- 1465-542X
- PMC
- PMC3446403
- OpenAlex
- W2106359723
- Cited by
- 122
- References
- 48
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 5 · 2023: 4 · 2022: 8 · 2021: 5 · 2020: 8 · 2019: 10 · 2018: 8 · 2017: 11 · 2016: 11 · 2015: 15 · 2014: 13 · 2013: 13 · 2012: 4
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Breast Cancer Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Science Council
- National Taiwan University Hospital
- National Taiwan University
- Yen Tjing Ling Medical Foundation
- Taiwan Clinical Oncology Research Foundation
- Taipei Veterans General Hospital
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Breast Cancer Treatment Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- bortezomib, triple-negative breast cancer, CIP2A, protein phosphatase 2A, apoptosis, Akt phosphorylation, proteasome inhibitors, drug resistance, breast cancer xenografts, anticancer activity, HER2-positive breast cancer, estrogen receptor-positive breast cancer, MDA-MB-231 cells, MDA-MB-468
- MeSH terms
- Bortezomib, Animals, Antineoplastic Agents, Autoantigens, Boronic Acids, Breast Neoplasms, Dose-Response Relationship, Drug, Female, Humans, Membrane Proteins, Mice, Nude, Pyrazines, Receptors, Estrogen, Apoptosis, Drug Resistance, Neoplasm, Xenograft Model Antitumor Assays, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Proto-Oncogene Proteins c-akt, Mice, MCF-7 Cells, Proteasome Inhibitors
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