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Submitted on July 12, 2004
Accepted on August 26, 2004
Department of Biology (S.D'A., S.I., F.A., M.M.,), University of Rome "Roma Tre", 00146 Roma, Italy; INSIBIO (Conicet-UNT) (R.N.F.) Chacabuco 461 (4000) San Miguel De Tucuman, Tucuman, Argentina; and Veterans Affairs Healthcare Network Upstate New York and Ordway Research Institute (F.B. Davis, P.J. Davis), Albany, New York 12208, USA
* To whom correspondence should be addressed. E-mail: incerpi{at}uniroma3.it.
3,5,3'-Triiodo-L-thyronine (L-T3) and L-Thyroxine (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, since 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 IP3-receptors and without contributions from extracellular calcium or ryanodine receptors; 2) protein phosphorylation involving protein kinase C and mitogen-activated protein kinase (MAPK; ERK1/2), as shown by the use of kinase inhibitors and by immunoblotting for activated kinases.
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