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• W2477599896 abstract "G-protein-coupled receptor (GPCR) agonists, including gastrointestinal peptides, neurotransmitters, hormones, chemokines, and bioactive lipids, are increasingly implicated in the regulation of a variety of normal and abnormal processes, including development, proliferation, inflammation, and malignant transformation. Typically, the binding of an agonistic ligand to its cognate GPCR triggers the activation of multiple signal transduction pathways that act in a synergistic and combinatorial fashion to elicit rapid physiological responses and, subsequently, relay mitogenic signals to the nucleus and promote cell proliferation. A rapid increase in the activity of phospholipases C, D, and A 2 leading to the synthesis of lipid-derived second messengers, Ca 2+ fluxes, and subsequent activation of protein phosphorylation cascades, including PKC/PKD, Raf/MEK/ERK, and Akt/mTOR/p70S6K, is an important early response to mitogenic GPCR agonists. The EGF receptor (EGFR) tyrosine kinase has emerged as a transducer in the signaling by GPCRs, a process termed transactivation. GPCR signal transduction also induces striking morphological changes and rapid tyrosine phosphorylation of multiple cellular proteins, including the non-receptor tyrosine kinases Src, focal adhesion kinase (FAK), and Pyk-2 and the adaptor proteins CAS and paxillin. The pathways stimulated by GPCRs are extensively interconnected by synergistic and antagonistic cross talks that play a critical role in signal transmission, integration, and dissemination. The purpose of this article is to review recent advances in defining the pathways that play a role in transducing responses induced by GPCRs relevant to the homeostatic balance, function, and pathobiology of the digestive system." @default.
• W2477599896 created "2016-08-23" @default.
• W2477599896 creator A5077935609 @default.
• W2477599896 date "2012-01-01" @default.
• W2477599896 modified "2023-10-16" @default.
• W2477599896 title "Signaling Pathways Induced by G-protein-coupled Receptors" @default.
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