We have located links that may give you full text access.
JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Increased expression of HSP27 linked to vincristine resistance in human gastric cancer cell line.
Journal of Cancer Research and Clinical Oncology 2009 Februrary
PURPOSE: To understand the mechanisms of multidrug resistance (MDR) in vincristine-resistant human gastric cancer cell line SGC7901/VCR.
METHODS: Comparative proteomics involving two-dimensional gel electrophoresis (2-DE) and ESI-Q-TOF Mass Spectrometry (MS) was performed on total proteins extracts from vincristine-resistant SGC7901/VCR and its parental cell line SGC7901. Then the association of heat shock protein 27 (HSP27), one of the highly expressed proteins in SGC7901/VCR, with MDR was analyzed using antisense oligonucleotides (ASOs) inhibition. To further elucidate the biological functions executed by HSP27 in SGC7901/VCR, we investigated a comprehensive interactome map of HSP27 by coimmunoprecipitation (IP) coupled with MS.
RESULTS: In this study, HSP27 was identified as a protein showing increased expression in SGC7901/VCR. The suppression of HSP27 expression by HSP27 ASOs could enhance vincristine and adriamycin chemosensitivity in SGC7901/VCR. Identified 25 HSP27-interacting proteins by IP coupled with MS could be classified into eight categories based on their functions: cytoskeleton organization, chaperones, metabolic enzymes, proteins relative to signal transduction, ribosomal proteins, DNA repair proteins, proteins involved in transcription and translation, and RNA processing, which correspond to the reported functions of HSP27 with MDR.
CONCLUSION: These data clearly link HSP27 and multidrug resistance mechanisms in gastric cancer.
METHODS: Comparative proteomics involving two-dimensional gel electrophoresis (2-DE) and ESI-Q-TOF Mass Spectrometry (MS) was performed on total proteins extracts from vincristine-resistant SGC7901/VCR and its parental cell line SGC7901. Then the association of heat shock protein 27 (HSP27), one of the highly expressed proteins in SGC7901/VCR, with MDR was analyzed using antisense oligonucleotides (ASOs) inhibition. To further elucidate the biological functions executed by HSP27 in SGC7901/VCR, we investigated a comprehensive interactome map of HSP27 by coimmunoprecipitation (IP) coupled with MS.
RESULTS: In this study, HSP27 was identified as a protein showing increased expression in SGC7901/VCR. The suppression of HSP27 expression by HSP27 ASOs could enhance vincristine and adriamycin chemosensitivity in SGC7901/VCR. Identified 25 HSP27-interacting proteins by IP coupled with MS could be classified into eight categories based on their functions: cytoskeleton organization, chaperones, metabolic enzymes, proteins relative to signal transduction, ribosomal proteins, DNA repair proteins, proteins involved in transcription and translation, and RNA processing, which correspond to the reported functions of HSP27 with MDR.
CONCLUSION: These data clearly link HSP27 and multidrug resistance mechanisms in gastric cancer.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app