scholarly journals Influence of Dietary Protein Levels on the Fate of Methylmercury and on Amino Acid Transport at the Renal Brush Border Membrane in Rats

2005 ◽  
Vol 51 (2) ◽  
pp. 138-146 ◽  
Author(s):  
Tatsumi Adachi ◽  
Kimiko Hirayama
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Dietary Protein ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Acid Transport ◽  
Protein Levels ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

scholarly journals Reconstitution and identification of the major Na+-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles

1992 ◽  
Vol 281 (1) ◽  
pp. 95-102 ◽  
Author(s):  
F A Doyle ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Acid Transport ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

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.

scholarly journals A role for aminopeptidase N in Na+-dependent amino acid transport in bovine renal brush-border membranes

1993 ◽  
Vol 290 (1) ◽  
pp. 59-65 ◽  
Author(s):  
S Plakidou-Dymock ◽  
M J Tanner ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Membrane Vesicles ◽  
Aminopeptidase N ◽  
Aminopeptidase Activity ◽  
Acid Transport ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

A monoclonal antibody FD19 which removes reconstitutable Na(+)-dependent amino acid transport activity from solubilized bovine renal brush-border membrane vesicles was found to react specifically with the enzyme aminopeptidase N. Cleavage of aminopeptidase N from the membranes with papain inhibited Na(+)-dependent amino acid transport activity without affecting that of alpha-methyl D-glucoside. Removal of aminopeptidase substantially increased the Km values for the Na(+)-dependent transport of alanine, glutamine, leucine and phenylalanine without affecting the Vmax. Both Na(+)-dependent amino acid transport and aminopeptidase activity in intact vesicles were competitively inhibited by amino acids with very similar specificity. These results suggest that the amino acid-binding sites of aminopeptidase N and the transporter interact in some way to increase the Km of the transport process for its substrates. However, independent direct inactivation of the transport system by papain cannot be ruled out.

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
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Brush Border ◽  
Time Course ◽  
Brush Border Membrane ◽  
Sulfur Amino Acids ◽  
Beta Alanine ◽  
Renal Brush Border Membrane ◽  
Amino Acid Intake ◽  
Renal Brush Border

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.

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