Skip navigation
  • 中文
  • English

DSpace CRIS

  • DSpace logo
  • Home
  • Organizations
  • Researchers
  • Research Outputs
  • Explore by
    • Organizations
    • Researchers
    • Research Outputs
  • Academic & Publications
  • Sign in
  • 中文
  • English
  1. NTU Scholars
  2. 醫學院
  3. 醫學系
Please use this identifier to cite or link to this item: https://scholars.lib.ntu.edu.tw/handle/123456789/523528
Title: A peptide that inhibits function of Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) reduces lung cancer metastasis
Authors: Chen C.-H.
Thai P.
Yoneda K.
Adler K.B.
PAN-CHYR YANG 
Wu R.
Issue Date: 2014
Publisher: Nature Publishing Group
Journal Volume: 33
Journal Issue: 28
Start page/Pages: 3696-3706
Source: Oncogene
Abstract: 
Myristoylated Alanine-Rich C Kinase Substrate (MARCKS), a substrate of protein kinase C, is a key regulatory molecule controlling mucus granule secretion by airway epithelial cells as well as directed migration of leukocytes, stem cells and fibroblasts. Phosphorylation of MARKCS may be involved in these responses. However, the functionality of MARCKS and its related phosphorylation in lung cancer malignancy have not been characterized. This study demonstrated elevated levels of MARCKS and phospho-MARCKS in highly invasive lung cancer cell lines and lung cancer specimens from non-small-cell lung cancer patients. siRNA knockdown of MARCKS expression in these highly invasive lung cancer cell lines reduced cell migration and suppressed PI3K (phosphatidylinositol 3′-kinase)/Akt phosphorylation and Slug level. Interestingly, treatment with a peptide identical to the MARCKS N-terminus sequence (the MANS peptide) impaired cell migration in vitro and also the metastatic potential of invasive lung cancer cells in vivo. Mechanistically, MANS peptide treatment resulted in a coordination of increase of E-cadherin expression, suppression of MARCKS phosphorylation and AKT/Slug signalling pathway but not the expression of total MARCKS. These results indicate a crucial role for MARCKS, specifically its phosphorylated form, in potentiating lung cancer cell migration/metastasis and suggest a potential use of MARCKS-related peptides in the treatment of lung cancer metastasis. ? 2014 Macmillan Publishers Limited.
URI: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84904250528&doi=10.1038%2fonc.2013.336&partnerID=40&md5=d945246704229ef835993bc9f6439aca
https://scholars.lib.ntu.edu.tw/handle/123456789/523528
ISSN: 0950-9232
DOI: 10.1038/onc.2013.336
SDG/Keyword: antineoplastic agent; MARCKS n terminus sequence peptide; MARCKS protein; peptide; phosphatidylinositol 3 kinase; protein inhibitor; protein kinase B; small interfering RNA; transcription factor Slug; unclassified drug; uvomorulin; actin filament; animal experiment; animal model; animal tissue; article; cancer inhibition; cell contact; cell culture; cell migration; cell population; cell spreading; controlled study; enzyme phosphorylation; epithelium cell; human; human tissue; in vitro study; in vivo study; lung cancer cell line; lung metastasis; lung non small cell cancer; metastasis potential; mouse; nonhuman; priority journal; protein expression; protein phosphorylation; signal transduction; Animals; Cell Line, Tumor; Cell Movement; Epithelial-Mesenchymal Transition; Gene Expression Regulation, Neoplastic; Humans; Intracellular Signaling Peptides and Proteins; Lung Neoplasms; Membrane Proteins; Mice; Neoplasm Invasiveness; Neoplasm Metastasis; Oncogenes; Peptide Fragments; Phosphatidylinositol 3-Kinases; Phosphoproteins; Phosphorylation; Proto-Oncogene Proteins c-akt; Signal Transduction
[SDGs]SDG3
Appears in Collections:醫學系

Show full item record

SCOPUSTM   
Citations

54
checked on Mar 13, 2023

WEB OF SCIENCETM
Citations

54
checked on Mar 19, 2023

Page view(s)

6
checked on Mar 27, 2023

Google ScholarTM

Check

Altmetric

Altmetric

Related Items in TAIR


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

臺大位居世界頂尖大學之列,為永久珍藏及向國際展現本校豐碩的研究成果及學術能量,圖書館整合機構典藏(NTUR)與學術庫(AH)不同功能平台,成為臺大學術典藏NTU scholars。期能整合研究能量、促進交流合作、保存學術產出、推廣研究成果。

To permanently archive and promote researcher profiles and scholarly works, Library integrates the services of “NTU Repository” with “Academic Hub” to form NTU Scholars.

總館學科館員 (Main Library)
醫學圖書館學科館員 (Medical Library)
社會科學院辜振甫紀念圖書館學科館員 (Social Sciences Library)

開放取用是從使用者角度提升資訊取用性的社會運動,應用在學術研究上是透過將研究著作公開供使用者自由取閱,以促進學術傳播及因應期刊訂購費用逐年攀升。同時可加速研究發展、提升研究影響力,NTU Scholars即為本校的開放取用典藏(OA Archive)平台。(點選深入了解OA)

  • 請確認所上傳的全文是原創的內容,若該文件包含部分內容的版權非匯入者所有,或由第三方贊助與合作完成,請確認該版權所有者及第三方同意提供此授權。
    Please represent that the submission is your original work, and that you have the right to grant the rights to upload.
  • 若欲上傳已出版的全文電子檔,可使用Sherpa Romeo網站查詢,以確認出版單位之版權政策。
    Please use Sherpa Romeo to find a summary of permissions that are normally given as part of each publisher's copyright transfer agreement.
  • 網站簡介 (Quickstart Guide)
  • 使用手冊 (Instruction Manual)
  • 線上預約服務 (Booking Service)
  • 方案一:臺灣大學計算機中心帳號登入
    (With C&INC Email Account)
  • 方案二:ORCID帳號登入 (With ORCID)
  • 方案一:定期更新ORCID者,以ID匯入 (Search for identifier (ORCID))
  • 方案二:自行建檔 (Default mode Submission)
  • 方案三:學科館員協助匯入 (Email worklist to subject librarians)
Build with DSpace-CRIS - Extension maintained and optimized by Logo 4SCIENCE Feedback