Uptake of lysine and prolinevia separate α-neutral amino acid transport pathways inMytilus gill brush border membranes

1989 ◽  
Vol 107 (3) ◽  
pp. 237-247 ◽  
Author(s):  
Ana M. Pajor ◽  
Stephen H. Wright
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Neutral Amino Acid ◽  
Acid Transport ◽  
Transport Pathways ◽  
Brush Border Membranes

scholarly journals A rapid method for the reconstitution of Na+-dependent neutral amino acid transport from bovine renal brush-border membranes

1987 ◽  
Vol 244 (3) ◽  
pp. 503-508 ◽  
Author(s):  
A M Lynch ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Rapid Method ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Neutral Amino Acid ◽  
Acid Transport ◽  
Transport Activity ◽  
Brush Border Membranes ◽  
Renal Brush Border Membranes ◽  
Renal Brush Border

1. A simple and rapid method for the reconstitution of Na+-dependent neutral amino acid transport activity from bovine renal brush border membranes is described. 2. The neutral detergent decanoyl-N-methylglucamide (‘MEGA-10’) was employed to solubilize the membrane protein. This obviated the necessity for a prolonged dialysis step. 3. The properties of amino acid transport in these vesicles were similar to those observed in native membranes. 4. This should be a useful procedure in the eventual identification and isolation of amino acid transport proteins.

Delineation of sodium-stimulated amino acid transport pathways in rabbit kidney brush border vesicles

1982 ◽  
Vol 64 (1-2) ◽  
pp. 113-122 ◽  
Author(s):  
Austin K. Mircheff ◽  
Ian Kippen ◽  
Bruce Hirayama ◽  
Ernest M. Wright
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Rabbit Kidney ◽  
Acid Transport ◽  
Transport Pathways

Neutral amino acid transport pathways in uptake of L-thyroxine by Ehrlich ascites cells

1975 ◽  
Vol 229 (1) ◽  
pp. 172-177 ◽  
Author(s):  
LK Stitzer ◽  
JA Jacquez
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Extracellular Fluid ◽  
Neutral Amino Acid ◽  
Acid Transport ◽  
Transport Pathways ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cells ◽  
Amino Acid Concentrations ◽  
Extracellular Amino Acid

Neutral amino acid pathways were investigated as possible mediators of L-thyroxine (T4) entry into ascites cells. 14C-Labeled T4, alpha-aminoisobutyric acid (AIB), L-phenylalanine (Phe), and cycloleucine (cLeu) uptakes were measured at initial extracellular amino acid concentrations of 1 muM in a modified Krebs-Ringer phosphate buffer, pH 7.4. T4 uptake was markedly slower than that of AIB, Phe, or cLeu over a 25-min period. T4 uptake was neither competitively stimulated nor inhibited by either AIB or Phe when these latter amino acids were varied over the concentration range 1.0 x 10(-6) to 1.0 x 10(-2) M. Preloading cells with 30 mM L-methionine did not enhance the uptake of T4. TJ efflux from preloaded cells was not affected by either AIB or Phe in the extracellular fluid (ECF). The uptakes of AIB, Phe, and cLeu were markedly altered by replacement of ECF Na+ with choline+, whereas T4 uptake was unchanged. It was concluded that neural amino acid transport pathways (specifically A, L, ASC, and beta) do not participate in the transmembrane transfer of L-thyroxine into Ehrlich ascites cells.

Brush-border amino acid transport mechanisms in carnivorous eel intestine

1989 ◽  
Vol 257 (3) ◽  
pp. R506-R510 ◽  
Author(s):  
C. Storelli ◽  
S. Vilella ◽  
M. P. Romano ◽  
M. Maffia ◽  
G. Cassano
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Membrane Vesicles ◽  
Anguilla Anguilla ◽  
Neutral Amino Acid ◽  
Transport Systems ◽  
European Eel ◽  
Acid Transport

Brush-border membrane vesicles (BBMV) were prepared from European eel (Anguilla anguilla) intestinal epithelium by a magnesium-ethylene glycolbis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) precipitation technique. Amino acid transport by these purified vesicle preparations was investigated using either radiolabeled substrates or the voltage-sensitive fluorescent dye 3,3'-diethylthiadicarbocyanine iodide [DiSC2(5)]. All amino acids tested exhibited carrier-mediated, Na+-dependent and Na+-independent transfer processes plus diffusion. The only exceptions were glutamic acid and proline, which displayed Na+ dependency and diffusion but did not appear to be transported by Na+-independent agencies. Carrier-mediated transport kinetic constants (Kapp and Jmax) for several amino acids are reported. Cis-inhibition experiments suggested the presence of at least four distinct Na+-dependent transport systems in eel intestinal BBMV: 1) an anionic transport process for glutamic and aspartic acids; 2) a cationic mechanism for lysine and arginine; 3) a relatively specific neutral amino acid carrier for proline and alpha-(methylamino)isobutyric acid; and 4) a nonspecific neutral amino acid system for most other substrates of this group. This scheme for carnivorous fish intestine most closely approximates that reported for mammalian gut with minor dissimilarities that may relate to metabolic differences or specific dietary requirements of the two vertebrate groups.

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