NDLI: Phosphorylation of cMet tyrosine residues in murine ascitic hepatic cancer cell lines with different lymph node metastatic potentials.

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Phosphorylation of cMet tyrosine residues in murine ascitic hepatic cancer cell lines with different lymph node metastatic potentials.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Li, Ying Huang, Xiaohua Ma, Keli Zhang, Qiaoshu
Description	Author Affiliation: Li Y ( Department of Clinical Laboratory, Second Affiliated Hospital of Dalian Medical University, Dalian 116023, P.R. China.)
Abstract	The aim of the present study was to determine the molecular mechanism by which the hepatocyte growth factor (HGF) receptor (cMet) regulates lymphatic metastasis in hepatocellular carcinoma. Mouse hepatoma ascites cell lines with different lymph node metastatic potentials, HcaF (high metastatic potential) and HcaP (low metastatic potential), were cultured in vitro. Cells were treated with HGF, fibronectin (FN) and laminin (LN), and the phosphorylated tyrosine residues of cMet and the activities of intracellular phospholipase CÎ³/diacylglycerol/protein kinase C (PLCÎ³/DAG/PKC) and phosphoinositol3kinase/protein kinase B (PI3K/AKT) signaling pathways were analyzed comparatively in the two cell lines using western blot analysis and migration assays. Following HGF treatment, the phosphorylation of cMet at Tyr 1313 and 1365 in HcaF cells was higher, while the phosphorylation of cMet at Tyr 1349 was lower than that in HcaP. The activity of PLCÎ³/DAG/PKC was increased in HcaF cells compared with HcaP cells, whereas the activity of PI3K/AKT was reduced. After FN treatment, the phosphorylation of cMet at Tyr 1313 and the activity of the PLCÎ³/DAG/PKC signaling pathway was increased in HcaF cells compared with HcaP cells. Following LN treatment, the phosphorylation of cMet at Tyr 1365 and the activity of PLCÎ³/DAG/PKC was higher in HcaF cells than in HcaP cells. Results of the current study indicate that a number of ligands stimulate the phosphorylation of cMet at various tyrosine residues, activating different signaling transduction pathways. In addition, the same ligand was observed to phosphorylate different tyrosine residues on cMet in the two cell lines, as well as activate different intracellular signaling transduction pathways. After cMet is activated, various tyrosine residues are phosphorylated, leading to the activation of the PI3K/AKT and PLCÎ³/DAG/PKC signaling pathways to different extents in the two cells lines. These results may be important in determining the lymph node metastatic potentials of the two cell lines.
ISSN	17912997
e-ISSN	17913004
Journal	Molecular Medicine Reports
Issue Number	2
Volume Number	8
Language	English
Publisher	Spandidos Publications
Publisher Date	2013-08-01
Publisher Place	Greece
Access Restriction	Open
Subject Keyword	Carcinoma, Hepatocellular Metabolism Pathology Liver Neoplasms Proto-oncogene Proteins C-met Animals Cell Line, Tumor Cell Movement Drug Effects Fibronectins Pharmacology Hepatocyte Growth Factor Lymph Nodes Lymphatic Metastasis Mice Phosphatidylinositol 3-kinases Phospholipase C Gamma Phosphorylation Protein Kinase C Proto-oncogene Proteins C-akt Signal Transduction Research Support, Non-u.s. Gov't Discipline Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Genetics Biochemistry Molecular Biology Cancer Research Molecular Medicine Oncology

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