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

Rosenberg, León E.; Segal, Stanton

doi:10.1042/bj0920345

Cited by 101 publications

(62 citation statements)

References 21 publications

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“…Such an effect, if operative in vivo, would be expected to interfere with the proposed function of the y-glutamyl cycle in amino-acid transport. It is thus of interest that administration of maleate to animals leads to extensive aminoaciduria (33,34). Other studies on aminoacid transport in vivo using a microinjection technique led to the suggestion that maleic acid produces aminoaciduria by increasing efflux of amino acid, leading to or secondary to a loss of cellular amino-acid accumulation (35).…”

Section: Discussionmentioning

confidence: 99%

Stimulation of the Hydrolytic Activity and Decrease of the Transpeptidase Activity of γ-Glutamyl Transpeptidase by Maleate; Identity of a Rat Kidney Maleate-Stimulated Glutaminase and γ-Glutamyl Transpeptidase

Tate

Meister

1974

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACT-y-Glutamyl transpeptidase catalyzes transfer of the y-glutamyl moiety of glutathione (and other y-glutamyl compounds) to amino acid and peptide acceptors; this reaction probably involves (a) formation of a y-glutamyl enzyme and (b) reaction of the y-glutamyl-enzyme with an acceptor. Maleate decreases the latter reaction and markedly increases hydrolysis of the y-glutamyl donor, apparently by affecting the enzyme so as to facilitate reaction of the y-glutamyl enzyme with water. Transpeptidase catalyzes y-glutamyl hydroxamate formation from many y-glutamyl compounds and hydroxylamine; this reaction is stimulated 4-to 5-fold by maleate. Glutamine, a poor substrate for transpeptidation as compared to glutathione, is slowly hydrolyzed and converted to y-glutamyl-glutamine by the transpeptidase; in the presence of maleate, hydrolysis of glutamine is markedly (>10-fold) increased, as is also its conversion to -y-glutamyl hydroxamate in the presence of hydroxylamine. The findings suggest that the previously described "maleate-stimulated phosphate-independent glutaminase" is a catalytic function of -y-glutamyl transpeptidase. Transpeptidase-catalyzed glutaminase activity may play a role in renal ammoniagenesis. The ability of maleate to decrease transpeptidation of y-glutamyl compounds (and to increase their hydrolysis to glutamate), when considered in the light of earlier findings that treatment of animals with maleate produces aminoaciduria, is consistent with function of transpeptidase and the y-glutamyl cycle in amino-acid transport.

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Section: Discussionmentioning

confidence: 99%

Stimulation of the Hydrolytic Activity and Decrease of the Transpeptidase Activity of γ-Glutamyl Transpeptidase by Maleate; Identity of a Rat Kidney Maleate-Stimulated Glutaminase and γ-Glutamyl Transpeptidase

Tate

Meister

1974

Proc. Natl. Acad. Sci. U.S.A.

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“…Citrulline is one of the neutral amino acids and it is generally believed that amino acid groups in the human kidney, such as neutral amino acid, acidic amino acid, cystine and dibasic amino acids, glycine and imino acids, and fl-amino acids, apparently share a common transport system (Rosenberg et al 1962;Wilson and Scriver 1967;Scriver and Wilson 1967). The inborn errors of amino acid transport support the separate membrane transport systems.…”

Section: Discussionmentioning

confidence: 99%

“…Dent and Rose (1951) first postulated that reabsorption of these four amino acids in the renal tubule cell is defective in cystinuric patients. Recent studies (Rosenberg et al 1962;Fox et al 1964;Segal et al 1977) using both rat and human kidney cortex slices revealed that dibasic amino acids shared a common transport system, but that cystine uptake was controlled by an independent mechanism.Several clinical observations, of hyperdibasicaminoaciduria without cystinuria (Oyanagi et al 1970;Whelan and Scriver 1968) and cystinuria without hyperdibasicaminoaciduria (Brodehl et al 1967), support separate membrane transport systems for cystine and dibasic amino acids. The purpose of the present study is to describe the transport interaction of dibasic amino acids and citrulline which was hitherto unrecognized in the human kidney.…”

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confidence: 99%

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confidence: 99%

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A new transport interaction of dibasic amino acids and citrulline in human kidney.

Oyanagi

Sogawa

Minami

et al. 1981

Tohoku J. Exp. Med.

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The oral loading tests of lysine in 9 healthy men and the intravenous loading tests of lysine, ornithine and arginine in 3 healthy men were carried out. The results indicated that the membrane transport system of citrulline in the human kidney was clearly inhibited by dibasic amino acids, lysine, ornithine, and arginine. dibasic amino acids; citrulline; membrane transport Cystinuria is a well-known transport disorder of cystine and the dibasic amino acids, lysine, ornithine, and arginine. Dent and Rose (1951) first postulated that reabsorption of these four amino acids in the renal tubule cell is defective in cystinuric patients. Recent studies (Rosenberg et al. 1962;Fox et al. 1964;Segal et al. 1977) using both rat and human kidney cortex slices revealed that dibasic amino acids shared a common transport system, but that cystine uptake was controlled by an independent mechanism.Several clinical observations, of hyperdibasicaminoaciduria without cystinuria (Oyanagi et al. 1970;Whelan and Scriver 1968) and cystinuria without hyperdibasicaminoaciduria (Brodehl et al. 1967), support separate membrane transport systems for cystine and dibasic amino acids. The purpose of the present study is to describe the transport interaction of dibasic amino acids and citrulline which was hitherto unrecognized in the human kidney. SUBJECTS AND METHODSNine healthy colleagues of our Department participated in the following experiments. Oral loading tests of L-lysine. After overnight fasting, 150 mg of L-lysine per kg of body weight were administered orally. Urine specimens were collected before and after the loading for 4 hr. Quantitative analyses of amino acids were performed by a Technicon Amino-Acid Auto Analyzer.Constant infusion tests with L-lysine, L-ornithine, and L-arginine. 12 ml/kg body weight/hr of 20 mM, 40 mM, and 80 mM L-lysine, L-ornithine, and L-arginine solutions were constantly infused for 90 min on separate days, and blood samples were taken before

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“…Two-tenths-milliliter sampies of aqueous tissue extract and of the media were counted in a liquid scintillation spectrometer. Tissue accumulation of 14 C-labeled amino acid was calculated as a distribution ratio, (counts per minute per milliliter of intracellular fluid) j (counts per minute per milliliter of medium), using inulin space and total tissue water as described previously [6,7].…”

Section: Methodsmentioning

confidence: 99%

Transport of L-Methionine in Rat Intestine and Kidney

1974

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ExtractL-Methionine transport was studied in vitro in rat kidney cortex slices and intestinal segments.In both tissues L-(C 14 )methionine at concentrations of 0.065 mmol was accumulated against a chemical concentration gradient by processes which obeyed saturation kinetics. In both tissues anaerobic conditions (incubation in 95% N 2 and 5% 0 2 atmosphere) inhibited methionine accumulation (P < 0.001 and P < 0.025, respectively). The processes were sodium dependent. Addition of 0.3 M sucrose producedL-Methionine transport was essentially pH independent. A series of amino acids, including representatives of the neutral, dibasic and imino acid groups at 2.4 mM concentrations, failed to inhibit methionine transport with the exception that valine proved a potent inhibitor of transport in the intestine (P < 0.0 l) and ethionine in the kidney (P < 0.025). Methionine inhibited glycine accumulation in the kidney (P < 0.025) and intestine (P < 0.001), but failed to affect lysine transport in either tissue. SpeculationThe data presented indicate that methionine uptake in the gut and the kidney has the characteristics of an active transport process which is unaffected by most other amino acids. These findings suggest that methionine is either transported by an independent mechanism and / or by a transport system which is shared with the other neutral amino acids but for which it has a much higher affinity.

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

Cited by 101 publications

References 21 publications

Stimulation of the Hydrolytic Activity and Decrease of the Transpeptidase Activity of γ-Glutamyl Transpeptidase by Maleate; Identity of a Rat Kidney Maleate-Stimulated Glutaminase and γ-Glutamyl Transpeptidase

Stimulation of the Hydrolytic Activity and Decrease of the Transpeptidase Activity of γ-Glutamyl Transpeptidase by Maleate; Identity of a Rat Kidney Maleate-Stimulated Glutaminase and γ-Glutamyl Transpeptidase

A new transport interaction of dibasic amino acids and citrulline in human kidney.

Transport of L-Methionine in Rat Intestine and Kidney

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