543 Opioid Stimulation of Mitogen-Activated Protein Kinase (MAPK) in Enteric Neurons Is Mediated by Dynamin-Dependent μ Opioid Receptor (pOR) Endocytosis

2013 ◽  
Vol 144 (5) ◽  
pp. S-99
Author(s):  
Celine C. Duraffourd ◽  
Laura Anselmi ◽  
Catia Sternini
1998 ◽  
Vol 273 (20) ◽  
pp. 12402-12406 ◽  
Author(s):  
Roberto D. Polakiewicz ◽  
Sandra M. Schieferl ◽  
Lydia F. Dorner ◽  
Vikram Kansra ◽  
Michael J. Comb

2001 ◽  
Vol 74 (1) ◽  
pp. 414-422 ◽  
Author(s):  
Harald Schmidt ◽  
Stefan Schulz ◽  
Marcus Klutzny ◽  
Thomas Koch ◽  
Manuela Händel ◽  
...  

1999 ◽  
Vol 277 (6) ◽  
pp. G1165-G1172 ◽  
Author(s):  
Cynthia R. L. Webster ◽  
M. Sawkat Anwer

cAMP stimulates Na+-taurocholate (TC) cotransport by translocating the Na+-TC-cotransporting peptide (Ntcp) to the plasma membrane. The present study was undertaken to determine whether the phosphatidylinositol-3-kinase (PI3K)-signaling pathway is involved in cAMP-mediated translocation of Ntcp. The ability of cAMP to stimulate TC uptake declined significantly when hepatocytes were pretreated with PI3K inhibitors wortmannin or LY-294002. Wortmannin inhibited cAMP-mediated translocation of Ntcp to the plasma membrane. cAMP stimulated protein kinase B (PKB) activity by twofold within 5 min, an effect inhibited by wortmannin. Neither basal mitogen-activated protein kinase (MAPK) activity nor cAMP-mediated inhibition of MAPK activity was affected by wortmannin. cAMP also stimulated p70S6K activity. However, rapamycin, an inhibitor of p70S6K, failed to inhibit cAMP-mediated stimulation of TC uptake, indicating that the effect of cAMP is not mediated via p70S6K. Cytochalasin D, an inhibitor of actin filament formation, inhibited the ability of cAMP to stimulate TC uptake and Ntcp translocation. Together, these results suggest that the stimulation of TC uptake and Ntcp translocation by cAMP may be mediated via the PI3K/PKB signaling pathway and requires intact actin filaments.


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