Abstract
8-iso-prostaglandin F2α (8-iso-PGF2α), an F2-isoprostane, is produced in vivo by a cyclooxygenase-independent, free radical-catalyzed mechanism involving peroxidation of arachidonic acid1. This isoprostane is a highly potent renal vasoconstrictor2 and stimulates proliferation of cultured rat aortic smooth muscle cells (AoSMC) through enhancement of phosphoinositide turnover3. AoSMC have distinct F2-isoprostane binding sites, although these putative receptors bear homology to the thromboxane A2 (TxA2) receptor4. In this study, we report the activation of mitogen activated protein kinases (MAP-kinases)5 by 8-iso-PGF2α in AoSMC and its regulating mechanism involving protein kinase C (PKC) and pertussis toxin (PT)-sensitive GTP binding proteins.
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Fukunaga, M., Yura, T., Takahashi, K., Badr, K.F. (1997). Regulation of MAP-Kinase Activation by 8-Iso-Prostaglandin F2a in Cultured Rat Aortic Smooth Muscle Cells. In: Sinzinger, H., Samuelsson, B., Vane, J.R., Paoletti, R., Ramwell, P., Wong, P.YK. (eds) Recent Advances in Prostaglandin, Thromboxane, and Leukotriene Research. Advances in Experimental Medicine and Biology, vol 433. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1810-9_40
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DOI: https://doi.org/10.1007/978-1-4899-1810-9_40
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