@article{Hauck2001Inhib-7673,
  year={2001},
  title={Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells},
  volume={61},
  journal={Cancer Research},
  pages={7079--7090},
  author={Hauck, Christof R. and Sieg, David J. and Hsia, Datsun A. and Loftus, Joseph C. and Gaarde, William A. and Monia, Brett P. and Schlaepfer, David D.}
}

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    <dcterms:bibliographicCitation>First publ. in: Cancer Research 61 (2001), pp. 7079 7090</dcterms:bibliographicCitation>
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    <dc:contributor>Hsia, Datsun A.</dc:contributor>
    <dcterms:issued>2001</dcterms:issued>
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    <dc:contributor>Sieg, David J.</dc:contributor>
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    <dcterms:title>Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells</dcterms:title>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7673"/>
    <dc:creator>Gaarde, William A.</dc:creator>
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    <dc:contributor>Gaarde, William A.</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:16Z</dcterms:available>
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    <dc:contributor>Loftus, Joseph C.</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:16Z</dc:date>
    <dc:creator>Sieg, David J.</dc:creator>
    <dc:contributor>Hauck, Christof R.</dc:contributor>
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    <dc:contributor>Monia, Brett P.</dc:contributor>
    <dc:creator>Hauck, Christof R.</dc:creator>
    <dcterms:abstract xml:lang="eng">Elevated focal adhesion kinase (FAK) expression in human tumor cells has been correlated with an increased cell invasion potential. In cell culture, studies with FAK-null fibroblasts have shown that FAK function is required for cell migration. To determine the role of elevated FAK expression in facilitating epidermal growth factor (EGF)-stimulated human adenocarcinoma (A549) cell motility, antisense oligonucleotides were used to reduce FAK protein expression &gt;75%. Treatment of A549 cells with FAK antisense (ISIS 15421) but not a mismatched control (ISIS 17636) oligonucleotide resulted in reduced EGF-stimulated p130Cas-Src complex formation, c-Jun NH2-terminal kinase (JNK) activation, directed cell motility, and serum-stimulated cell invasion through Matrigel. Because residual FAK protein in ISIS 15421-treated A549 cells was highly phosphorylated at the Tyr-397/Src homology (SH)2 binding site, expression of the FAK COOH-terminal domain (FRNK) was also used as an inhibitor of FAK function. Adenoviral-mediated infection and expression of FRNK promoted FAK dephosphorylation at Tyr-397, resulted in reduced EGF-stimulated JNK as well as extracellular-regulated kinase 2 (ERK2) kinase activation, inhibited matrix metalloproteinase-9 (MMP-9) secretion, and potently blocked both random and EGF-stimulated A549 cell motility. Equivalent expression of a FRNK (S-1034) point-mutant that did not promote FAK dephosphorylation also did not affect EGF-stimulated signaling or cell motility. Dose-dependent reduction in EGF-stimulated A549 motility was observed with the PD98059 MEK1 inhibitor and the batimastat (BB-94) inhibitor of MMP activity, but not with the SB203580 inhibitor of p38 kinase. Finally, comparisons between normal, FAK-null, and FAK-reconstituted fibroblasts revealed that FAK enhanced EGF-stimulated JNK and ERK2 kinase activation that was required for cell motility. These data indicate that FAK functions as an important signaling platform to coordinate EGF-stimulated cell migration in human tumor cells and support a role for inhibitors of FAK expression or activity in the control of neoplastic cell invasion.</dcterms:abstract>
    <dc:creator>Hsia, Datsun A.</dc:creator>
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    <dc:creator>Schlaepfer, David D.</dc:creator>
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    <dc:creator>Loftus, Joseph C.</dc:creator>
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