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Molecular Pharmacology

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Research ArticleArticle

Taurine: Sodium-Dependent, High-Affinity Transport into Rat Brain Synaptosomes

ROBERT E. HRUSKA, ANTE PADJEN, RUBIN BRESSLER and HENRY I. YAMAMURA
Molecular Pharmacology January 1978, 14 (1) 77-85;
ROBERT E. HRUSKA
Departments of Pharmacology and Internal Medicine, University of Arizona College of Medicine, Tucson, Arizona 85724
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ANTE PADJEN
Departments of Pharmacology and Internal Medicine, University of Arizona College of Medicine, Tucson, Arizona 85724
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RUBIN BRESSLER
Departments of Pharmacology and Internal Medicine, University of Arizona College of Medicine, Tucson, Arizona 85724
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HENRY I. YAMAMURA
Departments of Pharmacology and Internal Medicine, University of Arizona College of Medicine, Tucson, Arizona 85724
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Abstract

Sodium-dependent transport of taurine into rat brain synaptosomes was studied using [3H]taurine of high specific activity (2.8 Ci/mmole). At 2.8 µM [3H]taurine, 57% of the total radioactive accumulation was directly proportional to the sodium ion concentration. The sodium-dependent, high-affinity transport was a linear function of added protein and incubation length, and was maximal between pH 6.6 and 8.6. Kinetic analyses indicated a high-affinity apparent Km value of 4.76 µM and an apparent Vmax value of 5.35 nmoles/g of protein per minute. After correction of the high-affinity transport for that portion contributed by the low-affinity system, the true kinetic constants of the high-affinity system were calculated to be 3.20 µM and 2.96 nmoles/g of protein per minute. Similarly, the true kinetic constants of the low-affinity system were calculated to be 3340 µM and 699 nmoles/g of protein per minute. The Hill plot for both the high- and low-affinity transport systems had a slope of about 1, which suggested a 1:l interaction between taurine and its transport molecule. The sodium-dependent, high-affinity transport of [3H]taurine was decreased by the removal of potassium or chloride ions, and was absent from lysed synaptosomes or when the assay was performed at 2°. The omission of glucose or the addition of dinitrophenol slightly reduced transport. Ouabain inhibited transport in a time- and dose-dependent manner. The Arrhenius plot of [3H]taurine transport revealed an energy of activation (Ea) of 15.6 kcal/mole and an energy quotient (Q10) of 2.34, each of which indicated an active process. The regional distribution of uptake showed that the midbrain, thalamus, and olfactory bulbs had the highest velocity of transport, while the cerebral cortex, spinal cord, and cerebellum had the lowest velocity of transport. Several structural analogues were inhibitors of taurine transport, and analyses of structure-activity relationships revealed that the uptake site was very specific. Only molecules with free anionic and cationic groups were potent inhibitors. These data are consistent with the hypothesis that taurine is a neurotransmitter or neuromodulator in the brain, and we have investigated some of the molecular characteristics of this transport.

ACKNOWLEDGMENTS We would like to thank Dr. Klaus Brendel of the University of Arizona for his kind gift of N-acetyltaurine. We would also like to thank David Chapman and Thomas McManus for expert technical assistance.

  • Copyright © 1978 by Academic Press, Inc.

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Molecular Pharmacology
Vol. 14, Issue 1
1 Jan 1978
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Research ArticleArticle

Taurine: Sodium-Dependent, High-Affinity Transport into Rat Brain Synaptosomes

ROBERT E. HRUSKA, ANTE PADJEN, RUBIN BRESSLER and HENRY I. YAMAMURA
Molecular Pharmacology January 1, 1978, 14 (1) 77-85;

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Research ArticleArticle

Taurine: Sodium-Dependent, High-Affinity Transport into Rat Brain Synaptosomes

ROBERT E. HRUSKA, ANTE PADJEN, RUBIN BRESSLER and HENRY I. YAMAMURA
Molecular Pharmacology January 1, 1978, 14 (1) 77-85;
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