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| Content Provider | PubMed Central |
|---|---|
| Author | Samak, G. Aggarwal, S. Rao, R. K. |
| Copyright Year | 2011 |
| Abstract | The role of mitogen-activated protein kinases (MAPK) in the mechanism of EGF-mediated prevention of acetaldehyde-induced tight junction disruption was evaluated in Caco-2 cell monolayers. Pretreatment of cell monolayers with EGF attenuated acetaldehyde-induced decrease in resistance and increase in inulin permeability and redistribution of occludin, zona occludens-1 (ZO-1), E-cadherin, and β-catenin from the intercellular junctions. EGF rapidly increased the levels of phospho-ERK1/2, phospho-p38 MAPK, and phospho-JNK1. Pretreatment of cell monolayers with U-0126 (inhibitor of ERK activation), but not SB-202190 and SP-600125 (p38 MAPK and JNK inhibitors), significantly attenuated EGF-mediated prevention of acetaldehyde-induced changes in resistance, inulin permeability, and redistribution of occludin and ZO-1. U-0126, but not SB-202190 and SP-600125, also attenuated EGF-mediated prevention of acetaldehyde effect on the midregion F-actin ring. However, EGF-mediated preservation of junctional distribution of E-cadherin and β-catenin was unaffected by all three inhibitors. Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells. MEK1 expression did not alter E-cadherin distribution in acetaldehyde-treated cells in the presence or absence of EGF. Furthermore, EGF attenuated acetaldehyde-induced tyrosine-phosphorylation of occludin, ZO-1, claudin-3, and E-cadherin. U-0126, but not SB-202190 and SP-600125, prevented EGF effect on tyrosine-phosphorylation of occludin and ZO-1, but not claudin-3, E-cadherin, or β-catenin. These results indicate that EGF-mediated protection of tight junctions from acetaldehyde requires the activity of ERK1/2, but not p38 MAPK or JNK1/2, and that EGF-mediated protection of adherens junctions is independent of MAPK activities. |
| Related Links | http://dx.doi.org/10.1152/ajpgi.00494.2010 |
| Starting Page | 50 |
| File Format | |
| ISSN | 01931857 |
| e-ISSN | 15221547 |
| Journal | American Journal of Physiology - Gastrointestinal and Liver Physiology |
| Issue Number | 1 |
| Volume Number | 301 |
| Language | English |
| Publisher | American Physiological Society |
| Publisher Date | 2011-07-01 |
| Access Restriction | Open |
| Rights Holder | American Physiological Society |
| Subject Keyword | Hepatology Gastroenterology Physiology (medical) Physiology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Hepatology Physiology Physiology (medical) Gastroenterology |
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