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Methionine transport in S37 cells. Substrate-dependent function of amino acid transport system A in exchange processes
Authors:Richard H. Matthews  Robert Zand
Affiliation:1. Department of Physiological Chemistry, The Ohio State University, Columbus, OH 43210 U.S.A.;2. Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, MI 48105 U.S.A.
Abstract:Methionine had been observed to interact with two principal transport systems for amino acids in mammalian cells, the A and L systems. The present study of methionine transport and of exchange processes through system A arose in the course of a study to define the specificity of a transinhibition effect caused by cysteine.Methionine uptake through two transport systems in the S37 cell was confirmed by the occurrence of a biphasic double-reciprocal plot for labeled methionine uptake. Preloading cells with methionine stimulated labeled histidine uptake through both systems A and L. Efflux of labeled methionine from cells was stimulated by histidine in a biphasic manner, so that both systems A and L can be used for exchange when methionine is the intracellular amino acid. Aminocycloheptanecarboxylic acid elicited exchange efflux of labeled methionine only through system L. α-Aminoisobutyric acid and N-methyl-α-aminoisobutyric acid both stimulated efflux of labeled N-methyl-α-aminoisobutyric acid from S37 cells. These findings are interpreted a showing that transport system A is capable of functioning as an exchange system depending upon the identity of intracellular and extracellular substrates available.
Keywords:Amino acid transport  Methionine  Exchange process  Methylaminoisobutyrate  (Ascites tumor cell)  extracellular concentration of an amino acid  AC7C aminocycloheptanecarboxylic acid  S37  mouse sarcoma 37 ascites tumor
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