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Journal of Dental Research
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Biological

Bradykinin Mediates Phosphorylation of eNOS in Odontoblasts

Y. Korkmaz1,*, W. Bloch2, D. Steinritz3, M.A. Baumann4, K. Addicks5, K. Schneider1 and W.H.-M. Raab1

1 Department of Operative and Preventive Dentistry and Endodontics, Heinrich-Heine-University, Moorenstr. 5, 40225 Düsseldorf, Germany;
2 Department of Molecular and Cellular Sport Medicine, German Sport University, Cologne, Germany;
3 Bundeswehr Institute of Pharmacology and Toxicology, Munich, Germany;
4 Department of Operative Dentistry and Periodontology, University of Cologne, Germany; and
5 Department I of Anatomy, University of Cologne, Germany

Correspondence: * corresponding author, yueksel.korkmaz{at}uni-duesseldorf.de

While the activation of eNOS by Akt/PKB-dependent phosphorylation, leading to NO release, and the inhibition of enzyme activity by bradykinin (BK)-mediated phosphorylation of eNOS in endothelial cells are established, the phosphorylation of eNOS in odontoblasts is unknown. To clarify the regulation of eNOS in odontoblasts by BK, we examined the phosphorylation of eNOS, Akt/PKB, and ERK1/2 in odontoblasts of rat molars. BK (10–7 M) transiently induced the phosphorylation of eNOS at Ser1177, Akt/PKB in odontoblasts, while it induced the phosphorylation of eNOS at Thr495 throughout the entire period of BK treatment. BK receptor 2 antagonist HOE 140 (10–6 M) significantly reduced signal intensities of phosphorylated-eNOS at Ser1177, Thr495, and phosphorylated-Akt/PKB. These results suggest that BK has dual effects on the activation of eNOS in odontoblasts, the Akt/PKB-dependent up-regulation of eNOS by the transient phosphorylation at Ser1177, and the ERK1/2-independent down-regulation of eNOS by the phosphorylation at Thr495.

Key Words: eNOS • phosphorylation of eNOS • Akt/PKB • ERK1/2 • odontoblasts

Journal of Dental Research, Vol. 85, No. 6, 536-541 (2006)
DOI: 10.1177/154405910608500611
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Home page
 Exp Biol MedHome page
V. L. Watts and E. D. Motley
Role of Protease-Activated Receptor-1 in Endothelial Nitric Oxide Synthase-Thr495 Phosphorylation
Exp Biol Med, February 1, 2009; 234(2): 132 - 139.
[Abstract] [Full Text] [PDF]