The Heat Production and Blood and Urine Constituents after Administration of d-Lysine Monohydrochloride to the Dog

Doty, John R.; Eaton, A. G.

doi:10.1093/jn/17.5.497

Cited by 3 publications

(2 citation statements)

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“…Although its chemical reactivity is identical to that of its levo-isomer, the principle of using D-lysine as a nonenzymatic glycation inhibitor is namely: (i) it is not used as a building block for mammalian proteins; (ii) it is apparently not toxic; (iii) it is excreted mainly by glomerular filtration with little or no renal tubular reabsorption [17,18], and (iv) D-amino acid oxidase activity is very low against o-lysine [17,26,27]. These characteristics would explain the finding of significant urinary recovery of D-lysine following i.v.…”

Section: Discussionmentioning

confidence: 99%

“…We have approached the problem from a different angle: to try to reduce the extent of non-enzymatic glycation by actively subtracting some of the reactive glucose (the open aldose form with the free carbonyl group, which makes up only a very small proportion of circulating sugar molecules, since, at any time, most of the glucose is in the form of the closed pyranose ring [16] ) from the protein reacting sites. For this purpose the dextro-isomer of L-lysine, D-lysine, has been chosen, on the principle that it pos- [17,18]. In two in vitro studies we have shown that the inhibitory action of D-lysine on nonenzymatic glycation is specific and amino acid concentration-dependent [19] and is effective in reducing AGE levels [20].…”

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confidence: 99%

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d-Lysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats

et al. 1993

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D-Lysine, the non-physiological isomer of L-lysine, can competitively reduce protein non-enzymatic glycation in vitro. To study the effect of D-lysine in vivo, 6-8-week old Sprague-Dawley rats with streptozotocin-induced diabetes mellitus were treated from diagnosis for 45 days with two daily subcutaneous injections of D-lysine (0.5 g.ml-1.day-1). Another group of diabetic rats was only injected with equal volumes of physiological saline (0.9% NaCl). Glycated haemoglobin was measured by ion exchange chromatography, and glycated serum and lens proteins by boronate affinity gel chromatography. Serum and urinary creatinine concentrations were evaluated by the alkaline-picrate reaction. Urinary lysine concentrations at mid- and end-study were evaluated by cation exchange chromatography. Blood glucose concentrations, serum creatinine levels and creatinine clearances, measured at the end of the study, were similar in both diabetic groups (> 22.0 mmol/l, < or = 106 mumol/l and approximately 0.02 ml/s, respectively). Urinary lysine concentration in D-lysine-treated diabetic animals was more than 50-fold higher than in placebo-treated diabetic rats. In D-lysine-treated vs placebo-treated diabetic animals, a statistically significant reduction was found in the levels of glycated haemoglobin (stable HbA1; mean +/- SD = 3.00 +/- 0.74% vs 4.02 +/- 0.46%, p < 0.05; labile HbA1 = 3.92 +/- 0.89% vs 5.84 +/- 0.61%, p < 0.005), glycated serum proteins (1.40 +/- 0.47% vs 2.52 +/- 1.15%, p < 0.05) and glycated lens proteins (4.90 +/- 0.96% vs 5.98 +/- 0.65%, p < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

d-Lysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats

et al. 1993

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Biological Value of Proteins in Relation to the Essential Amino Acids Which They Contain

Hawley

Edwards

1946

The Journal of Nutrition

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The Reabsorption of Glycine and Other Amino Acids in the Kidneys of Man

Ussing

1945

Acta Physiologica Scandinavica

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Summary. 1. Methods are described for the estimation of total amino‐N, glycine, leucine + valine and histidine in blood plasma and urine. The amino‐N determination method is a modification of FOLIN'S method. Glycine is estimated from the fall in amino‐N on repeated adsorptions on carbon. For the determination of leucine + valine in urine a method is described modifying a method previously worked out by the author for the determination of the sum of these amino acids in small tissue samples. Histidine is partly isolated from urine by adsorption on carbon and eluation with 50% acetic acid. 2. The content of different amino acids in plasma and urine from human subjects is examined. It is found that glycine is not the all dominating amino acid, neither in plasma nor in urine. Moreover it is found that the concentration index for glycine (possibly + other little adsorbed amino acids) is somewhat higher than that for total amino‐N. Leucine and valine are very efficiently reabsorbed compared with for instance glycine and histidine. 3. The effect of glycine ingestion in human subjects is examincd. It is found that the taking of 20–25 g glycine may increase the amino acid content in the urine up to 14 times. The excess excretion is, however, shown to consist of glycine only, the excretion of histidine and tyrosine remaining at the fasting level. 4. The results are discussed and a working hypothesis is set forth to explain the apparent independent reabsorption of glycine and other amino acids.

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The Heat Production and Blood and Urine Constituents after Administration of d-Lysine Monohydrochloride to the Dog

Cited by 3 publications

References 16 publications

d-Lysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats

d-Lysine reduces the non-enzymatic glycation of proteins in experimental diabetes mellitus in rats

Biological Value of Proteins in Relation to the Essential Amino Acids Which They Contain

The Reabsorption of Glycine and Other Amino Acids in the Kidneys of Man

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