Structural basis for depletion of heat shock protein 90 client proteins by deguelin
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Oh, SH | - |
dc.contributor.author | Woo, JK | - |
dc.contributor.author | Yazici, YD | - |
dc.contributor.author | Myers, JN | - |
dc.contributor.author | Kim, WY | - |
dc.contributor.author | Jin, Q | - |
dc.contributor.author | Hong, SS | - |
dc.contributor.author | Park, HJ | - |
dc.contributor.author | Suh, YG | - |
dc.contributor.author | Kim, KW | - |
dc.contributor.author | Hong, WK | - |
dc.contributor.author | Lee, HY | - |
dc.date.accessioned | 2022-04-19T11:21:46Z | - |
dc.date.available | 2022-04-19T11:21:46Z | - |
dc.date.issued | 2007-06 | - |
dc.identifier.issn | 0027-8874 | - |
dc.identifier.issn | 1460-2105 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/148416 | - |
dc.description.abstract | Background The molecular chaperone heat shock protein 90 (Hsp90) participates in preserving the expression and activity of various oncoproteins, including hypoxia-inducible factor la (HIF-1 alpha) and Akt. Deguelin is a rotenoid with antitumor activities. We investigated whether the antitumor activities of deguelin involve the functional inhibition of Hsp90. Method Human xenograft tumors were generated in mice from H1299 (n = 6 per group) and A549 (n = 4 per group) non-small-cell lung cancer cells, UMSCC38 (n = 5 per group) head and neck cancer cells, MKN45 (n = 5 per group) stomach cancer cells, and PC-3 (n = 3 per group) prostate cancer cells. Tumor-bearing mice were treated with deguelin at 4 or 8 mg/kg or with vehicle (as a control) twice a day by oral gavage for 15-28 days. Protein expression was assessed by western blot analysis. Akt and Hsp90 were assessed by use of adenoviral vectors expressing constitutively active Akt or Hsp90. Binding of deguelin to Hsp90 was examined by docking analysis and by competition binding experiments with ATP-Sepharose beads. The proteasome inhibitor MG132 was used to investigate deguelin's effect on the induction of ubiquitin-mediated proteasomal degradation of HIF-1a. All statistical tests were two-sided. Results Deguelin bound to the ATP-binding pocket of Hsp90 and disrupt | - |
dc.format.extent | 13 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | OXFORD UNIV PRESS INC | - |
dc.title | Structural basis for depletion of heat shock protein 90 client proteins by deguelin | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1093/jnci/djm007 | - |
dc.identifier.scopusid | 2-s2.0-34347256360 | - |
dc.identifier.wosid | 000247918000010 | - |
dc.identifier.bibliographicCitation | JOURNAL OF THE NATIONAL CANCER INSTITUTE, v.99, no.12, pp 949 - 961 | - |
dc.citation.title | JOURNAL OF THE NATIONAL CANCER INSTITUTE | - |
dc.citation.volume | 99 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 949 | - |
dc.citation.endPage | 961 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.identifier.url | https://academic.oup.com/jnci/article/99/12/949/965680?login=true | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
Sookmyung Women's University. Cheongpa-ro 47-gil 100 (Cheongpa-dong 2ga), Yongsan-gu, Seoul, 04310, Korea02-710-9127
Copyright©Sookmyung Women's University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.