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H-Ras induces Nrf2-Pin1 interaction: Implications for breast cancer progression
DC Field | Value | Language |
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dc.contributor.author | Saeidi, Soma | - |
dc.contributor.author | Kim, Su-Jung | - |
dc.contributor.author | Han, Hyeong-jun | - |
dc.contributor.author | Kim, Seong Hoon | - |
dc.contributor.author | Zheng, Jie | - |
dc.contributor.author | Lee, Han-Byoel | - |
dc.contributor.author | Han, Wonshik | - |
dc.contributor.author | Noh, Dong-Young | - |
dc.contributor.author | Na, Hye-Kyung | - |
dc.contributor.author | Surh, Young-Joon | - |
dc.date.accessioned | 2021-01-31T10:24:50Z | - |
dc.date.available | 2021-01-31T10:24:50Z | - |
dc.date.created | 2020-08-24 | - |
dc.date.created | 2020-08-24 | - |
dc.date.issued | 2020-09 | - |
dc.identifier.citation | Toxicology and Applied Pharmacology, Vol.402, p. 115121 | - |
dc.identifier.issn | 0041-008X | - |
dc.identifier.other | 111396 | - |
dc.identifier.uri | https://hdl.handle.net/10371/172910 | - |
dc.description.abstract | Aberrant activation of H-Ras is often associated with tumor aggressiveness in breast cancer. Peptidyl-prolyl cistrans isomerase NIMA-interacting 1 (Pin1) is a unique enzyme that interacts with phosphorylated serine or threonine of a target protein and isomerizes the adjacent proline residue. Pin1 is prevalently overexpressed in human cancers, and its overexpression correlates with poor prognosis. Nuclear factor E2-related factor 2 (Nrf2) is a master regulator of cellular redox homeostasis. The sustained activation/accumulation of Nrf2 has been observed in many different types of human malignancies, conferring an advantage for growth and survival of cancer cells. The activated form of H-Ras (GTP-H-Ras) is highly overexpressed in human breast cancer tissues. In our present study, silencing of H-Ras decreased the invasiveness of MDA-MB-231 human breast cancer cells and abrogated the interaction between Pin1 and Nrf2 in these cells. Pin1 knockdown blocked the accumulation of Nrf2, thereby suppressing proliferation and clonogenicity of MCF10A-Ras human mammary epithelial cells. We found that Pin1 binds to Nrf2 which stabilizes this transcription factor by hampering proteasomal degradation. In conclusion, H-Ras activation in cooperation with the Pin1-Nrf2 complex represents a novel mechanism underlying breast cancer progression and constitutive activation of Nrf2 and can be exploited as a therapeutic target. | - |
dc.language | 영어 | - |
dc.publisher | Academic Press | - |
dc.title | H-Ras induces Nrf2-Pin1 interaction: Implications for breast cancer progression | - |
dc.type | Article | - |
dc.contributor.AlternativeAuthor | 서영준 | - |
dc.identifier.doi | 10.1016/j.taap.2020.115121 | - |
dc.citation.journaltitle | Toxicology and Applied Pharmacology | - |
dc.identifier.wosid | 000556589200006 | - |
dc.identifier.scopusid | 2-s2.0-85088825288 | - |
dc.citation.startpage | 115121 | - |
dc.citation.volume | 402 | - |
dc.identifier.sci | 000556589200006 | - |
dc.description.isOpenAccess | N | - |
dc.contributor.affiliatedAuthor | Han, Wonshik | - |
dc.contributor.affiliatedAuthor | Noh, Dong-Young | - |
dc.contributor.affiliatedAuthor | Surh, Young-Joon | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | PROLYL-ISOMERASE PIN1 | - |
dc.subject.keywordPlus | TRANSCRIPTIONAL ACTIVITY | - |
dc.subject.keywordPlus | GENE-EXPRESSION | - |
dc.subject.keywordPlus | RETINOIC ACID | - |
dc.subject.keywordPlus | NRF2 | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | TRANSFORMATION | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordAuthor | H-Ras | - |
dc.subject.keywordAuthor | Pin1 | - |
dc.subject.keywordAuthor | Nrf2 | - |
dc.subject.keywordAuthor | Protein-protein interaction | - |
dc.subject.keywordAuthor | Breast cancer | - |
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