NDLI: Type II cGMP-dependent protein kinase inhibits ligandinduced activation of EGFR in gastric cancer cells.

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Year: 2014 Volume: 9 Issue: 3

Year: 2014 Volume: 9 Issue: 2

Year: 2014 Volume: 9 Issue: 1

Type II cGMP-dependent protein kinase inhibits ligandinduced activation of EGFR in gastric cancer cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wu, Min Li, Yueying Wang, Ying Qian, Hai Lan, Ting Jiang, Lu Chen, Yongchang
Description	Author Affiliation: Jiang L ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.); Chen Y ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.); Li Y ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.); Lan T ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.); Wu M ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.); Wang Y ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.); Qian H ( Department of Physiology, School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang, Jiangsu 212013, P.R. China.)
Abstract	Our previous data demonstrated that type II cGMPdependent protein kinase (PKG II) inhibited epidermal growth factor (EGF)-induced MAPK/ERK/JNKmediated signal transduction through inhibiting the phosphorylation/activation of the epidermal growth factor receptor (EGFR). Since the EGFR also binds with several other ligands as well as EGF, the present study was designed to investigate whether PKG II inhibited transforming growth factor- (TGF- ), betacellulin (BTC) and epiregulin (EPR) induced phosphorylation/activation of the EGFR and consequent MAPK/ERKmediated signaling. The human gastric cancer cell line AGS, was infected with adenoviral constructs encoding cDNA of PKG II (Ad-PKG II) to increase the expression of PKG II and was treated with 8-pCPT-cGMP to activate the kinase. Western blotting was applied to detect the phosphorylation of EGFR and MAPK/ERK. The results demonstrated that treatment with EGF (100 ng/ml, 5 min), TGF- (100 ng/ml, 5 min), BTC (100 ng/ml, 5 min) and EPR (100 ng/ml, 5 min) increased the tyrosine (tyr) 1068 phosphorylation of the EGFR and the threonine (thr) 202/tyr 204 phosphorylation of MAPK/ERK. Infecting the cells with Ad-PKG II and stimulating the kinase with 8-pCPT-cGMP efficiently inhibited the phosphorylation of the EGFR and MAPK/ERK induced by EGF, TGF- , BTC and EPR. The results indicated that PKG II also inhibits the activation of the EGFR caused by diverse ligands of the receptor.
ISSN	17912997
e-ISSN	17913004
Journal	Molecular Medicine Reports
Issue Number	4
Volume Number	9
Language	English
Publisher	Spandidos Publications
Publisher Date	2014-04-01
Publisher Place	Greece
Access Restriction	Open
Subject Keyword	Cyclic Gmp-dependent Protein Kinase Type Ii Metabolism Receptor, Epidermal Growth Factor Antagonists & Inhibitors Stomach Neoplasms Betacellulin Cell Line, Tumor Enzyme Activation Drug Effects Epidermal Growth Factor Pharmacology Epiregulin Extracellular Signal-regulated Map Kinases Intercellular Signaling Peptides And Proteins Ligands Phosphorylation Phosphotyrosine Enzymology Transforming Growth Factor Alpha 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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