Amino Acid-dependent Sodium Transport in Plasma Membrane Vesicles from Rat Liver

Overview

Journal J Membr Biol

Date 1981 Jan 1

PMID 7328632

Citations 3

Authors

H J Sips

K van Dam

Affiliations

Soon will be listed here.

Abstract

The L-alanine-dependent transport of sodium ions across the plasma membrane of rat-liver parenchymal cells was studied using isolated plasma membrane vesicles. Sodium uptake is stimulated specifically by the L-isomer of alanine and other amino acids, whose transport is sodium-dependent in rat-liver plasma membrane vesicles. The L-alanine-dependent sodium flux across the membrane is inhibited by an excess of Li+ ions, but not by K+ or choline ions. Sodium transport is sensitive to -SH reagents and ionophores, and is an electrogenic process: a membrane potential (negative inside) can enhance L-alanine-dependent sodium accumulation. The data presented provide further evidence for a sodium-alanine cotransport mechanism.

Citing Articles

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A rapid method for the functional reconstitution of amino acid transport systems from rat liver plasma membranes. Partial purification of System A.

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Sensitivity of system A and ASC transport activities to thiol-group-modifying reagents in rat liver plasma-membrane vesicles. Evidence for a direct binding of N-ethylmaleimide and iodoacetamide on A and ASC carriers.

Pola E, Bertran J, Roca A, Palacin M, Zorzano A, Testar X Biochem J. 1990; 271(2):297-303.

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