Cycloleucine (1-amino-cyclopentane carboxylic acid): Tubular reabsorption and inhibitory effect on amino acid transport in the rat kidney (microperfusion experiments)

1975 ◽  
Vol 353 (3) ◽  
pp. 241-253 ◽  
Author(s):  
Stefan Silbernagl
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Amino Acid Transport ◽  
Rat Kidney ◽  
Inhibitory Effect ◽  
Tubular Reabsorption ◽  
Acid Transport

scholarly journals Competitive Inhibition of Dibasic Amino Acid Transport in Rat Kidney

1962 ◽  
Vol 237 (7) ◽  
pp. 2265-2270
Author(s):  
Leon E. Rosenberg ◽  
Sylvia J. Downing ◽  
Stanton Segal
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Competitive Inhibition ◽  
Rat Kidney ◽  
Acid Transport ◽  
Dibasic Amino Acid

Amino Acid Transport in a Water-mould: The Possible Regulatory Roles of Calcium and N6-(Δ2-isopentenyl)adenine

1975 ◽  
Vol 53 (9) ◽  
pp. 975-988 ◽  
Author(s):  
Danny P. Singh ◽  
Hérb. B. LéJohn
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Osmotic Shock ◽  
Inhibitory Effect ◽  
Transport Systems ◽  
Acid Transport ◽  
Isopentenyl Adenine ◽  
Energy Dependent ◽  
Water Mould

Transport of amino acids in the water-mould Achlya is an energy-dependent process. Based on competition kinetics and studies involving the influence of pH and temperature on the initial transport rates, it was concluded that the 20 amino acids (L-isomers) commonly found in proteins were transported by more than one, possibly nine, uptake systems. This is similar to the pattern elucidated for some bacteria but unlike those uncovered for all fungi studied to date. The nine different transport systems elucidated are: (i) methionine, (ii) cysteine, (iii) proline, (iv) serine–threonine, (v) aspartic and glutamic acids, (vi) glutamine and asparagine, (vii) glycine and alanine, (viii) histidine, lysine, and arginine, and (ix) phenylalanine–tyrosine–tryptophan and leucine–isoleucine–valine as two overlapping groups. Transport of all of these amino acids was inhibited by azide, cyanide, and its derivatives and 2,4-dinitrophenol. These agents normally interfere with metabolism at the level of the electron transport chain and oxidative phosphorylation. Osmotic shock treatment of the cells released, into the shock fluid, a glycopeptide that binds calcium as well as tryptophan but no other amino acid. The shocked cells are incapable of concentrating amino acids, but remain viable and reacquire this capacity when the glycopeptide is resynthesized.Calcium played more than a secondary role in the transport of the amino acids. When bound to the membrane-localized glycopeptide, it permits concentrative transport to take place. However, excess calcium can inhibit transport which can be overcome by chelating with citrate. Calculations show that the concentration of free citrate is most important. At low citrate concentrations (less than 1 mM) in the absence of exogenously supplied calcium, enhancement of amino acid transport occurs. At high concentrations (greater than 5 mM), citrate inhibits but this effect can be reversed by titrating with calcium. Evidently, the glycopeptide acts as a calcium sink to regulate the concentration of calcium made available to the cell for its membrane activities.N6-(Δ2-isopentenyl) adenine (a plant growth 'hormone') and analogues mimic the inhibitory effect of citrate and bind to the glycopeptide as well. Replot data for citrate and N6-(Δ2-isopentyl) adenine inhibition indicate that both agents have no more than one binding constant. These results implicate calcium, glycopeptide, and energy-dependent transport of solutes in some, as yet undefinable, way.

Sodium dependence of the amino acid transport in the proximal convolution of the rat kidney

1974 ◽  
Vol 351 (1) ◽  
pp. 49-60 ◽  
Author(s):  
K. J. Ullrich ◽  
G. Rumrich ◽  
S. Kl�ss
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Rat Kidney ◽  
Acid Transport ◽  
Sodium Dependence ◽  
Proximal Convolution

Expression of mRNA (D2) encoding a protein involved in amino acid transport in S3 proximal tubule

1992 ◽  
Vol 263 (6) ◽  
pp. F1087-F1092 ◽  
Author(s):  
Y. Kanai ◽  
M. G. Stelzner ◽  
W. S. Lee ◽  
R. G. Wells ◽  
D. Brown ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Proximal Tubule ◽  
Amino Acid Transport ◽  
Glucose Transporter ◽  
Rat Kidney ◽  
Expression Cloning ◽  
Acid Transport ◽  
Specific Expression ◽  
High Affinity

A rat kidney- and intestine-specific cDNA (D2) that induces high-affinity, Na(+)-independent uptake of cystine and dibasic and neutral amino acids into cRNA-injected Xenopus oocytes was recently isolated by expression cloning in our laboratory (R. G. Wells and M. A. Hediger. Proc. Natl. Acad. Sci. USA 89: 5596-5600, 1992). At present it is not known whether the D2-encoded protein functions as a transporter or as a transporter activator. To gain more insight into the role of D2 in renal amino acid transport, we studied the site of its expression in the kidney. This was determined by Northern blot analysis and by using a combination of in situ hybridization and immunocytochemistry with antibodies that recognize specific proximal tubule segments. D2 antisense RNA hybridized to the same tubular segments that were strongly positive for anti-ecto-adenosinetriphosphatase but negative for carbonic anhydrase type IV and the facilitated glucose transporter GLUT2. We conclude that D2 mRNA is strongly expressed in the rat kidney proximal tubule S3 segment, although there is weak hybridization to the S1 and S2 segments. The signal is absent in all other parts of the kidney. The S3 specific expression of D2 mRNA coincides with the site of high-affinity transport of cystine and other amino acids, consistent with the proposed involvement of D2 in these processes.

scholarly journals Maleic acid-induced inhibition of amino acid transport in rat kidney

1964 ◽  
Vol 92 (2) ◽  
pp. 345-352 ◽  
Author(s):  
LE Rosenberg ◽  
S Segal
Keyword(s):  
Amino Acid ◽  
Maleic Acid ◽  
Amino Acid Transport ◽  
Rat Kidney ◽  
Acid Transport

CHARACTERISTICS OF ACIDIC AMINO ACID TRANSPORT IN MAMMALIAN KIDNEY

1963 ◽  
Vol 41 (1) ◽  
pp. 131-137 ◽  
Author(s):  
William A. Webber
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Tubular Reabsorption ◽  
Side Chain ◽  
Acid Transport ◽  
Acidic Amino Acid ◽  
Neutral Amino Acids ◽  
Wide Range ◽  
Renal Tubular

A series of clearance experiments on dogs were carried out which were designed to confirm and characterize the renal tubular reabsorption of glutamic and aspartic acids. Tubular reabsorption was measured and found to reach a maximum of about 100 μmole/minute for L-glutamic and L-aspartic acids and a slightly lower level for D-aspartic. Competitive studies using substituted amino acids were performed and three patterns of inhibition of amino acid reabsorption observed. Acidic amino acids inhibited the reabsorption of each other, while neutral amino acids (and an acidic amino acid substituted so as to have a neutral side chain) inhibited the reabsorption of a wide range of other amino acids. Compounds with the amino group or either carboxyl group substituted or absent, but not resembling neutral amino acids, were not inhibitory. There appears to be a specialized mechanism for acidic amino acid transport which probably requires all three functional groups but which may be interfered with by a compound with alpha carboxyl and amino groups and a neutral side chain.

Inhibitory effect of somatostatin on neutral amino acid transport in isolated brain microvessels

2001 ◽  
Vol 78 (2) ◽  
pp. 349-357
Author(s):  
Patrizia Cardelli ◽  
Anna Fiori ◽  
Vito D. Corleto ◽  
Maria Rosaria Savi ◽  
Filippo Granata ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Inhibitory Effect ◽  
Neutral Amino Acid ◽  
Acid Transport ◽  
Brain Microvessels

CHARACTERISTICS OF ACIDIC AMINO ACID TRANSPORT IN MAMMALIAN KIDNEY

1963 ◽  
Vol 41 (1) ◽  
pp. 131-137 ◽  
Author(s):  
William A. Webber
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Tubular Reabsorption ◽  
Side Chain ◽  
Acid Transport ◽  
Acidic Amino Acid ◽  
Neutral Amino Acids ◽  
Wide Range ◽  
Renal Tubular

A series of clearance experiments on dogs were carried out which were designed to confirm and characterize the renal tubular reabsorption of glutamic and aspartic acids. Tubular reabsorption was measured and found to reach a maximum of about 100 μmole/minute for L-glutamic and L-aspartic acids and a slightly lower level for D-aspartic. Competitive studies using substituted amino acids were performed and three patterns of inhibition of amino acid reabsorption observed. Acidic amino acids inhibited the reabsorption of each other, while neutral amino acids (and an acidic amino acid substituted so as to have a neutral side chain) inhibited the reabsorption of a wide range of other amino acids. Compounds with the amino group or either carboxyl group substituted or absent, but not resembling neutral amino acids, were not inhibitory. There appears to be a specialized mechanism for acidic amino acid transport which probably requires all three functional groups but which may be interfered with by a compound with alpha carboxyl and amino groups and a neutral side chain.

The ontogeny of amino acid transport in rat kidney II. Kinetics of uptake and effect of anoxia

1971 ◽  
Vol 249 (2) ◽  
pp. 364-372 ◽  
Author(s):  
Kurt E. Baerlocher ◽  
Charles R. Scriver ◽  
Fazl Mohyuddin
Keyword(s):  
Amino Acid ◽  
Amino Acid Transport ◽  
Rat Kidney ◽  
Acid Transport ◽  
Kinetics Of Uptake ◽  
Kinetics Of
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