Effect of amino acid intake on brush-border membrane uptake of sulfur amino acids

1986 ◽  
Vol 251 (1) ◽  
pp. F125-F131
Author(s):  
R. W. Chesney ◽  
N. Gusowski ◽  
M. Padilla ◽  
S. Lippincott

Alterations in the intake of sulfur amino acids (SAA) changes the rat renal brush-border membrane uptake of the beta-amino acid, taurine. A low-SAA diet enhances and a high-taurine diet reduces uptake (Chesney et al., Kidney Int. 24: 588-594, 1983). Neither the low-SAA diet nor the high-taurine diet alters the time course or concentration-dependent accumulation of the sulfur amino acids methionine and cystine or of inorganic sulfate. By contrast the uptake of beta-alanine, another beta-amino acid that competes with taurine, is greater in animals on the low-SAA diet. The high-taurine diet does not change beta-alanine uptake. The plasma levels of taurine are altered by dietary change, but not the values for methionine and cystine. This study indicates that renal adaptation is expressed for beta-alanine, a nonsulfur-containing beta-amino acid. By contrast, methionine, cystine, and sulfate, which participate in a variety of synthetic and conjugative processes, are not conserved by the renal brush-border surface following ingestion of either a low-methionine and -cystine diet or high-taurine diet.

1986 ◽  
Vol 251 (4) ◽  
pp. F734-F742 ◽  
Author(s):  
P. D. McNamara ◽  
C. T. Rea ◽  
S. Segal

Lysine uptake by isolated rat renal brush-border membrane vesicles occurs via a single saturable system plus a significant diffusion component with indication of a single energy of activation on an Arrhenius plot. Initial uptake is not sodium dependent, and intravesicular accumulation of lysine at longer time points is greatest in the absence of sodium. Accumulation levels differ in the presence or absence of NaCl or choline chloride and are specific for the cation used. Lysine uptake is membrane potential sensitive and inhibitable by cystine, dibasic amino acids, and cycloleucine. Heteroexchange diffusion of lysine with cystine and lysine with arginine occurs, but no heteroexchange occurs with cycloleucine, indicating that lysine shares a transport system with cystine and dibasic amino acids but not with cycloleucine.


1992 ◽  
Vol 281 (1) ◽  
pp. 95-102 ◽  
Author(s):  
F A Doyle ◽  
J D McGivan

Amino acid transport activity from bovine renal brush-border membrane vesicles (BBMV) was reconstituted into phospholipid vesicles composed of phosphatidylcholine/5% stearylamine. Reconstitutable transport activity was enhanced in protein fractions binding to various lectins. When solubilized BBMV were fractionated on peanut lectin, a single protein band of average molecular mass 132 kDa was obtained. When this protein fraction was reconstituted into phospholipid membrane vesicles, amino acid transport activity was obtained with properties similar to those in native BBMV with regard to amino acid specificity, although the cation specificity was different. A monoclonal antibody which reacted with the same protein removed reconstitutable amino acid transport activity from solubilized BBMV. These findings may provide the first identification of a renal amino acid-transporting protein, although confirmation of this identification by other approaches will be required.


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