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Department of Biology (S.D., S.I., F.A., M.M.,), University of Rome "Roma Tre," 00146 Roma, Italy; Instituto Superior de Investigaciones Biológicas (Conicet-Universidad Nacional de Tucumán) (R.N.F.), Tucumán 4000, Argentina; and Veterans Affairs Healthcare Network Upstate New York and Ordway Research Institute (F.B.D., P.J.D.), Albany, New York 12208
Address all correspondence and requests for reprints to: Dr. Sandra Incerpi, Department of Biology, University of Rome "Roma Tre," Viale Marconi, 446, 00146 Roma, Italy. E-mail: incerpi{at}uniroma3.it.
L-T3 and L-T4 activated the Na+/H+ exchanger of L-6 myoblasts, with a fast nongenomic mechanism, both in the steady state and when cells undergo acid loading with ammonium chloride. Monitored with the intracellular pH-sensitive fluorescent probe 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein, activation of the exchanger appeared to be initiated at the plasma membrane, because T3-agarose reproduced the effect of L-T3, and triiodothyroacetic acid, a hormone analog previously shown to inhibit membrane actions of thyroid hormone, blocked the action of L-T3 on the exchanger. We show here for the first time that transduction of the hormone signal in this nongenomic response requires tyrosine kinase-dependent phospholipase C activation and two different signaling pathways: 1) mobilization of intracellular calcium, assessed by the fluorescent probe fura-2, through activation of inositol trisphosphate receptors and without contributions from extracellular calcium or ryanodine receptors; and 2) protein phosphorylation involving protein kinase C and MAPK (ERK1/2), as shown by the use of kinase inhibitors and by immunoblotting for activated kinases.
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