Focal adhesion kinase as well as p130Cas and paxillin is crucially involved in the enhanced malignant properties under expression of ganglioside GD3 in melanoma cells.

Abstract	Mass spectrometry analysis of immunoprecipitates from serum-treated GD3-expressing melanoma cells with PY20 (anti-phosphotyrosine antibody) revealed that focal adhesion kinase (FAK) is more strongly activated in GD3-expressing cells than in GD3-negative cells. Involvement of FAK in the increased proliferation and invasion in GD3-expressing melanomas was demonstrated by siRNA-mediated knockdown. Also, it was shown that FAK is located up-stream of p130Cas and paxillin in the enhanced signaling pathway. GD3 expression enhanced the association of FAK with p130Cas after treatment with fetal calf serum. Thus, focal adhesion kinase as well as p130Cas and paxillin should be a crucial molecule undergoing stronger tyrosine phosphorylation in GD3-expressing melanoma cells. Molecules linking GD3 and FAK such as integrins in the enhanced signaling pathway remain to be investigated.
Authors	Kazunori Hamamura, Momoko Tsuji, Yuki Ohkawa, Hideyuki Nakashima, Sayaka Miyazaki, Takeshi Urano, Noriyuki Yamamoto, Minoru Ueda, Koichi Furukawa, Keiko Furukawa
Journal	Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1780 Issue 3 Pg. 513-9 (Mar 2008) ISSN: 0006-3002 [Print] Netherlands
PMID	18078823 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Antibodies, Monoclonal BCAR1 protein, human Crk-Associated Substrate Protein Gangliosides Paxillin Phosphotyrosine ganglioside, GD3 Focal Adhesion Protein-Tyrosine Kinases
Topics	Amino Acid Sequence Animals Antibodies, Monoclonal (pharmacology) Cattle Cell Line, Tumor Cell Proliferation (drug effects) Crk-Associated Substrate Protein (metabolism) Focal Adhesion Protein-Tyrosine Kinases (chemistry, metabolism) Gangliosides (metabolism) Humans Immunoprecipitation Mass Spectrometry Melanoma (enzymology, pathology) Molecular Sequence Data Mutation (genetics) Neoplasm Invasiveness Paxillin (metabolism) Phosphorylation (drug effects) Phosphotyrosine (metabolism) Protein Binding (drug effects) Serum Transfection

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