Journal of Neurochemistry · 1985 · 101 citations · 21 references
Life SciencesBiochemistryPharmacologyCalcium HomeostasisCellular BiochemistryMembrane BiochemistryCalcium SignalingCalcium Transport ProteinsIntracellular Calcium SignalingPhotoreceptor PhysiologyCalcium Ion SignalingCalcium Signaling In PhotoreceptorsGel ElectrophoresisPhosphatase Enzyme ActivityPhosphatase InhibitionRetinal PharmacologySubcellular Fraction AssaysSubcellular Fractionation
The effects of taurine on ATP-dependent calcium ion uptake and protein phosphorylation of rat retinal membrane preparations were investigated. Taurine (20 mM) stimulates ATP-dependent calcium ion uptake by twofold in crude retinal homogenates. In contrast, it inhibits the phosphorylation of specific membrane proteins as shown by acrylamide gel electrophoresis and autoradiography. The close structural analogue of taurine, 2-aminoethylhydrogen sulfate, demonstrates similar effects in both systems, i.e., stimulation of ATP-dependent calcium ion uptake and inhibition of protein phosphorylation, whereas isethionic acid and guanidinoethanesulfonate have no effect on either system. A P1 subcellular fraction of the retinal membrane preparation that contains photoreceptor cell synaptosomes has a higher specific activity for the uptake of calcium ions. Phosphorylation of specific proteins in the P1 fraction is also inhibited by the addition of 20 mM taurine. Taurine has no effect on retinal ATPase activities or on phosphatase activity, thus suggesting that it directly affects a kinase system.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations