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  4. A peptide that inhibits function of Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) reduces lung cancer metastasis
 
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A peptide that inhibits function of Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) reduces lung cancer metastasis

Journal
Oncogene
Journal Volume
33
Journal Issue
28
Pages
3696-3706
Date Issued
2014
Author(s)
Chen C.-H.
Thai P.
Yoneda K.
Adler K.B.
PAN-CHYR YANG  
Wu R.
DOI
10.1038/onc.2013.336
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
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.
SDGs

[SDGs]SDG3

Other Subjects
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
Publisher
Nature Publishing Group
Type
journal article

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