Human gastrin-releasing peptide receptor mediates sustained CREB phosphorylation and transactivation in HuTu 80 duodenal cancer cells.

Abstract	The G protein-coupled human gastrin-releasing peptide receptor (hGRP-R) is frequently found aberrantly expressed in human cancers of the colon, stomach, and lung, and its ligand-specific activation has been implicated in cell proliferation and differentiation. Here, we demonstrated hGRP-R activation stimulated sustained cyclic AMP response element binding protein (CREB) phosphorylation and transactivation in duodenal cancer cells through a protein kinase C and partially p38 mitogen-activated protein kinase-dependent pathway. In contrast, intracellular calcium, ERK1/2, protein kinase A, and PI3 kinase were not involved. This novel signaling mechanism might be of importance for regulation of CREB-dependent gene expression in human cancer expressing functional hGRP-R.
Authors	Xiangping Qu, Dongmei Xiao, H Christian Weber
Journal	FEBS letters (FEBS Lett) Vol. 527 Issue 1-3 Pg. 109-13 (Sep 11 2002) ISSN: 0014-5793 [Print] England
PMID	12220644 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References	Cyclic AMP Response Element-Binding Protein Enzyme Inhibitors Imidazoles Pyridines Receptors, Bombesin Recombinant Fusion Proteins Serine Cyclic AMP-Dependent Protein Kinases Protein Kinase C Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases p38 Mitogen-Activated Protein Kinases SB 203580 Bombesin Calcium
Topics	Bombesin (pharmacology) Calcium (metabolism) Cyclic AMP Response Element-Binding Protein (drug effects, genetics, metabolism) Cyclic AMP-Dependent Protein Kinases (metabolism) Duodenal Neoplasms (metabolism) Enzyme Inhibitors (pharmacology) Humans Imidazoles (pharmacology) Mitogen-Activated Protein Kinase 1 (metabolism) Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases (antagonists & inhibitors, metabolism) Phosphorylation (drug effects) Protein Kinase C (metabolism) Pyridines (pharmacology) Receptors, Bombesin (metabolism) Recombinant Fusion Proteins (drug effects, genetics, metabolism) Serine (metabolism) Transcription, Genetic Transcriptional Activation Tumor Cells, Cultured p38 Mitogen-Activated Protein Kinases

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