The Mechanism of MAP Kinase Activation under Acidic Condition in Feline Esophageal Smooth Muscle Cells
- Authors
- Park, Sun Young; Lee, Young Ju; Min, Youngsil; Kim, Hak Rim; Jeong, Ji Hoon; Sohn, Uy Dong
- Issue Date
- Oct-2011
- Publisher
- PHARMACEUTICAL SOC KOREA
- Keywords
- Esophageal epithelial cell; Acid; ERK 1/2; p38 MAPK; Reflux esophagitis; Signal transduction
- Citation
- ARCHIVES OF PHARMACAL RESEARCH, v.34, no.10, pp 1759 - 1768
- Pages
- 10
- Journal Title
- ARCHIVES OF PHARMACAL RESEARCH
- Volume
- 34
- Number
- 10
- Start Page
- 1759
- End Page
- 1768
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21236
- DOI
- 10.1007/s12272-011-1020-4
- ISSN
- 0253-6269
- Abstract
- Reflux esophagitis results from repeated exposure of the esophagus to acidic gastric juice or bile-containing duodenal contents. In Barrett's adenocarcinoma, acid increases proliferation via ERK and p38 MAPK activation. This study was focused on determination of the mechanism(s) underlying MAPKs (ERK 1/2, p38 MAPK, and JNK) activation induced by acidic medium at pH 4 in normal feline primary cultured esophageal smooth muscle cells (FESMCs). We detected ERK 1/2 and p38 MAPK phosphorylation after exposure to pH 4 or neutral media in the presence or absence of several inhibitors and quantified the MAPK levels using western blotting analysis and densitometry. Acidic medium markedly increased the phosphorylation of ERK 1/2 and p38 MAPK within 10 min. Acid-induced ERK 1/2 and p38 MAPK activation was inhibited by pertussis toxin (PTX-sensitive G(i/o) protein inhibitor), DEDA (phospholipase (PL) A(2) inhibitor), pCMB (PLD inhibitor), GF109203X (protein kinase C (PKC) inhibitor) and D609 (phosphatidylcholine-specific PLC inhibitor). But, genistein (tyrosine kinase inhibitor), forskolin (adenylate cyclase activator) and U73122 (phosphatidylinositol-specific PLC inhibitor) had no effect on acid-induced ERK1/2 and p38 MAPK activation. These findings indicate that the activation of ERK 1/2 and p38 MAPK pathways by acidic conditions, at least in part, may be mediated by activation of the G(i/o) protein coupled receptors, PC-PLC, PLD, PLA(2), and PKC in FESMCs.
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Collections - College of Pharmacy > School of Pharmacy > 1. Journal Articles
- College of Medicine > College of Medicine > 1. Journal Articles
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