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    Endotoxin/lipopolysaccharide activates NF-kappa B and enhances tumor cell adhesion and invasion through a beta 1 integrin-dependent mechanism.

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    Authors
    Wang, Jiang Huai
    Manning, Brian J
    Wu, Qiong Di
    Blankson, Siobhan
    Bouchier-Hayes, D
    Redmond, H Paul
    Affiliation
    Department of Academic Surgery, National University of Ireland, Cork University, Hospital, Ireland. jh.wang@ucc.i.e
    Issue Date
    2012-02-03T15:09:53Z
    MeSH
    Adjuvants, Immunologic/*pharmacology
    Antigens, CD14/biosynthesis/metabolism/pharmacology
    Antigens, CD29/biosynthesis/*physiology
    Cell Adhesion/immunology
    Cell Membrane/immunology/metabolism
    Cell Movement/*immunology
    Endotoxins/*pharmacology
    Humans
    I-kappa B Proteins/genetics
    Integrin alphaVbeta3/biosynthesis
    Lipopolysaccharides/*pharmacology
    NF-kappa B/antagonists & inhibitors/*metabolism
    Peptides/pharmacology
    Signal Transduction/immunology
    Solubility
    Transfection
    Tumor Cells, Cultured/immunology/metabolism/*pathology
    Up-Regulation/immunology
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    Metadata
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    Citation
    J Immunol. 2003 Jan 15;170(2):795-804.
    Journal
    Journal of immunology (Baltimore, Md. : 1950)
    URI
    http://hdl.handle.net/10147/209012
    PubMed ID
    12517943
    Abstract
    Beta(1) integrins play a crucial role in supporting tumor cell attachment to and invasion into the extracellular matrix. Endotoxin/LPS introduced by surgery has been shown to enhance tumor metastasis in a murine model. Here we show the direct effect of LPS on tumor cell adhesion and invasion in extracellular matrix proteins through a beta(1) integrin-dependent pathway. The human colorectal tumor cell lines SW480 and SW620 constitutively expressed high levels of the beta(1) subunit, whereas various low levels of alpha(1), alpha(2), alpha(4), and alpha(6) expression were detected. SW480 and SW620 did not express membrane-bound CD14; however, LPS in the presence of soluble CD14 (sCD14) significantly up-regulated beta(1) integrin expression; enhanced tumor cell attachment to fibronectin, collagen I, and laminin; and strongly promoted tumor cell invasion through the Matrigel. Anti-beta(1) blocking mAbs (4B4 and 6S6) abrogated LPS- plus sCD14-induced tumor cell adhesion and invasion. Furthermore, LPS, when combined with sCD14, resulted in NF-kappaB activation in both SW480 and SW620 cells. Inhibition of the NF-kappaB pathway significantly attenuated LPS-induced up-regulation of beta(1) integrin expression and prevented tumor cell adhesion and invasion. These results provide direct evidence that although SW480 and SW620 cells do not express membrane-bound CD14, LPS in the presence of sCD14 can activate NF-kappaB, up-regulate beta(1) integrin expression, and subsequently promote tumor cell adhesion and invasion. Moreover, LPS-induced tumor cell attachment to and invasion through extracellular matrix proteins is beta(1) subunit-dependent.
    Language
    eng
    ISSN
    0022-1767 (Print)
    0022-1767 (Linking)
    Collections
    Cork University Hospital

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