Abstract
The effects of 20 mM taurine on the phosphorylation of specific proteins in mitochondrial and rod outer segment subcellular fractions of the rat retina were measured. A band of protein with an apparent molecular wieght of ∼ 20K was consistently inhibited by taurine. Densitometry measurements performed on gel electrophoresis autoradiograms from the mitochondrial fraction demonstrated a 42.7±8.3% decrease due to taurine (20 mM) in the area corresponding to radioactivity from the ∼ 20K phosphoprotein. However, only a 21.2±9.0% decrease was observed due to taurine in the rod outer segment preparation. These data suggest that taurine is exerting its primary effect on the phosphorylation of the ∼ 20K molecular weight protein in the mitochondria of the retina. In addition, calmodulin and phorbol ester had no effect on the phosphorylation of the ∼ 20K molecular weight protein.
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Voaden, J. J., Oraedu, A. C. I., Marshall, J., and Lake, N. 1981. Taurine in the retina. Pages 145–160,in Schaffer, S. W., Baskin, S. I., and Kocsis, J. J. (eds.), The Effects of Taurine on Excitable Tissues, Spectrum Publications, New York.
Pasantes-Morales, H., Arzate, N. E., and Cruz, C. 1982. The role of taurine in nervous tissues: Its effect on ionic fluxes. Pages 273–292,in Huxtable, R. J. and Pasantes-Morales, H. (eds.), Taurine in Nutrition and Neurology, Plenum, New York.
Lombardini, J. B. 1991. Taurine: retinal function. Brain Res. Reviews 16:151–169.
Lombardini, J. B. 1985. Effects of taurine on calcium ion uptake and protein phosphorylation in rat retinal membrane preparations. J. Neurochem. 45:268–275.
Lombardini, J. B. 1985. Inhibition by taurine of the phosphorylation of rat retinal membranes. Pages 383–396,in Oja, S. S., Ahtee, L., Kontro, P., and Paasonen, M. K. (eds.), Progress in Clinical and Biological Research, Vol. 179, Taurine: Biological Actions and Clinical Perspectives, Alan R. Liss, New York.
Liebowitz, S. M., Lombardini, J. B., and Allen, C. I. 1988. Effects of aminocycloalkanesulfonic acid analogs of taurine on ATP-dependent calcium ion uptake and protein phosphorylation. Biochem. Pharmacol. 37:1303–1309.
Li, Y.-P., and Lombardini, J. B. 1990. Taurine inhibits the phosphorylation of two endogenous proteins (Mr ∼ 140 and ∼ 20K) in subcellular preparations of rat cortex. Neurochem. Int. 17:389–399.
Li, Y.,-P., and Lombardini, J. B. 1991. Taurine inhibits protein kinase C-catalyzed phosphorylation of specific proteins in a rat cortical P2 fraction. J. Neurochem. 56:1747–1753.
Li, Y.-P., and Lombardini, J. B. 1991. Inhibition by taurine of the phosphorylation of specific synaptosomal proteins in the rat cortex: Effects of taurine on the stimulation of calcium uptake in mitochondria and inhibition of phosphoinositide turnover. Brain Res. 553:89–96.
Lombardini, J. B., and Liebowitz, S. J. 1989. Taurine modifies calcium ion uptake and protein phosphorylation in rat heart. Pages 117–137,in Iwata, H., Lombardini, J. B., and Segawa, T. (eds.), Taurine and the Heart, Kluwer Academic Publishers, Boston.
Schaffer, S. W., Allo, S., Harada, H., and Azuma, J. 1990. Regulation of calcium homeostasis by taurine: Role of calmodulin. Pages 217–225,in Pasantes-Morales, H., Martin, D. L., Shain, W., and Martin del Rio, R. (eds.), Taurine: Functional Neurochemistry, Physiology, and Cardiology, Wiley-Liss, New York.
Lombardini, J. B., Liebowitz, S. M., and Chou, T.-C. 1989. Analogues of taurine as stimulators and inhibitors of ATP-dependent calcium ion uptake in rat retina: Combination kinetics. Mol. Pharmacol. 36:256–264.
Liebowitz, S. M., Lombardini, J. B., and Allen, C. I. 1989. Sulfone analogues of taurine as modifiers of calcium uptake and protein phosphorylation in rat retina. Biochem. Pharmocol. 38:399–406.
Lombardini, J. B. 1988. Effects of taurine and mitochondrial metabolic inhibitors on ATP-dependent Ca2+ uptake in synaptosomal and mitochondrial subcellular fractions of rat retina. J. Neurochem. 51:200–205.
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
Redburn, D. A., and Thomas T. N. 1979. Isolation of synaptosomal fractions from rabbit retina. J. Neurosci. Methods 1:235–242.
Schubart, U. K., Alago, W., Jr., and Danoff, A. 1987. Properties of p19, a novel cAMP-dependent kinase substrate protein purified from bovine brain. J. Biol. Chem. 262:11871–11877.
Chneiweiss, H., Beretta, L., Cordier, J., Boutterin, M.-C., Glowinski, J., and Sobel, A. 1989. Stathmin is a major phosphoprotein and cyclic AMP-dependent protein kinase substrate in mouse brain neurons but not in astrocytes in culture: regulation during ontogenesis. J. Neurochem. 53:856–863.
Lyn-Cook, B. D., Ruder, F. J., and Wilson, J. E. 1985. Regulation of phosphate incorporation into four brain phosphoproteins that are affected by experience. J. Neurochem. 44:552–559.
Suzuki, T. and Siekevitz, P. 1989. Properties of a protein kinase C activity in synaptic plasma membrane and postsynaptic density fractions isolated from canine cerebral cortex. J. Neurochem. 53:1751–1762.
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Lombardini, J.B. Effects of taurine on the phosphorylation of specific proteins in subcellular fractions of the rat retina. Neurochem Res 17, 821–824 (1992). https://doi.org/10.1007/BF00969019
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DOI: https://doi.org/10.1007/BF00969019