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PubMed1982

Effects of 3,4-dihydroxyphenylpyruvic acid and its triacetylated derivative on DOPA decarboxylase.

Various drugs have been studied in order to improve the bioavailability of L-DOPA. In the present study, the alpha-ketoacid of L-DOPA, 3,4-dihydroxyphenylpyruvic acid (DHPPA) and its fully acetylated derivative, triacetoxyphenylpyruvic acid (TAPPA), were investigated. These substances were shown to be equally strong DOPA decarboxylase inhibitors in vitro. The inhibitory activity was, however, only about 1/2000 of that of carbidopa and 1/10 of that of L-alpha-methyldopa. In vivo studies in the rat showed that when either DHPPA or TAPPA was given orally concomitantly with L-DOPA, only DHPPA, which is a transaminase inhibitor, enhanced the L-DOPA induced rise in the cerebral dopamine concentration. TAPPA had, however, an enhancing effect on the L-DOPA-induced rise in the serum L-DOPA concentration. The weak L-DOPA-sparing effect of TAPPA could be explained by its inhibitory effect on DOPA decarboxylase and the marked L-DOPA-sparing effect of DHPPA by its action on both transamination and decarboxylation.

Animals↗
PubMed1979

The effect of simultaneous administration of 3,4-dihydroxyphenylpyruvic acid and L-dopa on the bioavailability of L-dopa in rat and mouse.

In the rat, administration of 3-(3,4-dihydroxy)-L-phenylalanine (L-dopa) simultaneously with the corresponding alpha-keto acid, 3,4-dihydroxyphenylpyruvic acid (DHPPA), gives significantly higher concentrations of L-dopa in the serum and of dopamine and homovanillic acid in the brain than the same dose of L-dopa alone. Correspondingly, DHPPA potentiates the effect of L-dopa on the locomotor activity in reserpine-treated mice. DHPPA is postulated to increase the absorption of intact L-dopa from the gut by preventing the transamination reaction between L-dopa and the physiological alpha-keto acids.

Animals↗
PubMed1990

The effect of glutamine on protein turnover in chick skeletal muscle in vitro.

The effect of glutamine on the rates of protein synthesis and degradation was studied in isolated chick extensor digitorum communis muscles incubated in the presence of plasma concentrations of amino acids. Addition of 0.5-15 mM-glutamine increases (P less than 0.01) intracellular glutamine concentrations by 31-670%. There is a positive relationship (r = 0.975, P less than 0.01) between intracellular glutamine concentration and the rate of muscle protein synthesis measured by the incorporation of [3H]phenylalanine. The stimulating effect of 15 mM-glutamine on protein synthesis was decreased from 58 to 19% in muscles incubated in the absence of tyrosine. The rates of protein degradation, estimated from [3H]phenylalanine release from muscle proteins prelabelled in vivo, decreased (P less than 0.05) by 15-30% in the presence of 4-15 mM-glutamine when compared with muscles incubated in the presence of physiological concentrations of glutamine (0.5-1 mM). Glutamine concentrations ranging from 2 to 15 mM appear to have an overall anabolic effect on chick skeletal muscles incubated in vitro.

Amino Acids↗
PubMed1980

Effects of 3,4-dihydroxyphenylpyruvic acid and L-glutamic acid on some pharmacokinetic parameters of L-dopa in the rat.

In the rat, various oral doses of 3,4-dihydroxyphenylpyruvic acid (DHPPA) administered simultaneously with L-dopa were shown to elevate the serum L-dopa and cerebral dopamine concentrations dose-dependently. With increasing DHPPA: L-dopa ratio the L-dopa-sparing effect became greater. Although oral and intravenous doses of DHPPA showed that it was readily converted to L-dopa in the serum, only small amounts of dopamine (DA) were detected in the brain. The high 3-O-methyldopa concentrations, measured in the serum after DHPPA administration, might be responsible for the failure of the L-dopa formed to pass the blood-brain barrier. Concomitant administration of L-dopa and glutamic acid gave significantly higher L-dopa values in the serum and DA and homovanillic acid values in the brain than did the same dose of L-dopa alone. This indicates that the transamination of L-dopa can also be effected by coadministration of L-dopa and an amino group donor in vivo.

Animals↗
PubMed1975

[Specificity of tyrosine metabolism depending on the state of melaninogenesis].

The excretion of metabolites of tyrosine (p-hydroxypyruvic acid-p-HPA, homogentisinic acid-HGA, total keto acids-TKA) and the activity of tyrosine aminotransferase of the tissues of 36 albino and 36 black rabbits was measured. The initial level of tyrosine metabolites in the urine of black and albino rabbits differed but little from one another. With the introduction of L-tyrosine, the quantity of the excreted p-HPA increased sharply, and of the HGA decreased in the albino rabbits. Among black rabbits an increase of the HGA excretion with a comparatively stable level of the excreted p-HPA was noted. Among all the tissues investigated only in the skin and the liver of albino rabbits there was a sharp increase in the initial tyrosine aminotransferase activity after the feeding of L-tyrosine, which testified to a probable adaptive synthesis of the enzyme. Analysis of the data obtained showed that tyrosine metabolism probably depended on the state of melaninogenesis.

Adrenal Glands↗