Role of protein kinase C in bradykinin-induced prostaglandin formation in osteoblasts |
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| Institution: | 1. Department of Internal Medicine, University Hospital, S-751 85 Uppsala, Sweden;2. Department of Pharmacology, Karolinska Institutet, S-104 01 Stockholm, Sweden;3. Department of Oral Cell Biology, University of Umeå, S-901 87 Umeå, Sweden;1. Center for Sustainability and the Global Environment, Nelson Institute for Environmental Studies, University of Wisconsin-Madison, 1710 University Avenue, Madison, WI 53726, USA;2. U.S. Geological Survey, Earth Resources Observation and Science Center, 47914 252nd St, Sioux Falls, SD 57198, USA;3. Department of Geography, University of Wisconsin-Madison, 550 N. Park St., Madison, WI 53726, USA;1. Queen’s University Belfast, University Rd, Belfast BT7 1NN, UK;2. University of Birmingham, Edgbaston, Birmingham B15 2TT, UK;3. Burgundy School of Business, CEREN, EA 7477, 29 Rue Sambin, 21000 Dijon, France;1. University of Cambridge, United Kingdom;2. University of Roehampton, United Kingdom;1. Department of Biomedical Engineering, Eindhoven University of Technology, Eindhoven, the Netherlands;2. Clinical Laboratory, Catharina Hospital, the Netherlands;3. Department of Anesthesiology, Intensive Care & Pain Medicine, Catharina Hospital, the Netherlands;4. Department of Surgery, Catharina Hospital, Eindhoven, the Netherlands;5. Department of Medical Physics, Catharina Hospital, Eindhoven, the Netherlands;6. Department of Electrical Engineering, Eindhoven University of Technology, Eindhoven, the Netherlands;7. Expert Center Clinical Chemistry Eindhoven, Eindhoven, the Netherlands;8. Department of Vascular Medicine, Amsterdam University Medical Centers, Amsterdam, the Netherlands;9. GROW – School for Oncology and Developmental Biology, Maastricht University, Maastricht, the Netherlands |
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| Abstract: | Bradykinin (1 μM 5 min) induced translocation of protein kinase C (PKC) to the plasma membrane fraction in osteoblastic MC3T3-E1 cells. Bradykinin also enhanced the binding of phorbol 12,13-dibutyrate (PDBu) to intact cells, a measure of PKC activation. Addition of bradykinin (1 μM) to cells preincubated with 3H]PDBu (10 nM, 20 min) caused an increase in specific PDBu binding that was maximal after 5–10 min. The bradykinin-induced enhancement of PDBu binding was seen at 1 nM and was maximal at 10 nM. The bradykinin B1 receptor agonist des-Arg9-bradykinin (1 μM) did not enhance specific PDBu binding to intact MC3T3-E1 cells. PDBu at and above 3 nM stimulated the formation of prostaglandin E2 (PGE2) in MC3T3-EI cells. This stimulatory effect was seen after 15–20 min incubation. The Ca2+ ionophore A23187 at and above 1 μM induced a rapid (within seconds) burst of PGE2 formation in MC3T3-E1 cells. The effect of PDBu and A23187 on PGE2 formation was synergistic. The PKC inhibitor staurosporine (200 nM) inhibited basal as well as bradykinin-induced prostaglandin-formation in MC3T3-E1 cells. In conclusion: bradykinin enhances PKC activation in osteoblastic MC3T3-E1 cells. This kinase activation may be involved in bradykinin-induced prostaglandin formation. |
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