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Biomedical subjects

F Hirata

Publications and source records attributed to F Hirata.

At least 181 records · Page 10Linked to original sources
PubMed1978

Effects of indoleamines and their newly identified metabolites on prolactin release in rats.

Plasma immunoreactive PRL responses to indoleamines and their metabolites were studied in urethane-anesthetized rats. All drugs were injected into the lateral ventricle and blood samples were serially collected from a jugular vein. Serotonin and melatonin caused a significant increase in plasma PRL with peak values at 10-20 min after the injection. Significant increase in plasma PRL were also observed after the administration of 5-hydroxykynurenamine (5-HK), a newly identified serotonin metabolite. The potency of 5-HK was less than that of serotonin but much greater than that of melatonin. In contrast, plasma PRL did not change significantly in response to N-acetyl-5-methoxykynurenamine, another newly identified metabolite of melatonin, or a vehicle solution. Simultaneous administration of melatonin significantly blunted the plasma PRL response to serotonin, whereas the rise in plasma PRL induced by 5-HK was not blunted by melatonin. These results suggest that indoleamines as well as their metabolites play a role in regulating PRL secretion in rats.

5-Hydroxytryptophan↗
PubMed1977

Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes.

The participation of superoxide anion (O2-) in the intracellular indoleamine 2,3-dioxygenase activity was studied using the dispersed cell suspension of the rabbit small intestine. The dioxygenase activity was assayed by measuring [14C]formate released from DL-[ring-2-14C]tryptophan. The addition of diethyldiethiocarbamate, a superoxide dismutase inhibitor, markedly accelerated the intracellular dioxygenase activity while the superoxide dismutase activity decreased concomitantly. Furthermore, substrates of xanthine oxidase such as inosine, adenosine, and hypoxanthine also increased the dioxygenase activity in the cells, particularly in the presence of methylene blue. This increase was completely abolished by the addition of allopurinol, a specific inhibitor of xanthine oxidase. These results, taken together, indicate that the intracellular accumulation of O2- results in acceleration of the in situ dioxygenase activity, and that indoleamine 2,3-dioxygenase utilizes O2- in the isolated intestinal cells.

Animals↗
PubMed1977

Studies on aspartase. IV. Reversible denaturation of Escherichia coli aspartase.

Aspartase (L-aspartate ammonia lyase, EC 4.3.1.1) of Escherichia coli, denatured in 4 M guanidine-HCl, was renatured in vitro by simple dilution with a concomitant restoration of the activity. While the native enzyme exhibited a marked negative Cotton effect centered at 233 +/- 1 nm in optical rotatory dispersion, the enzyme denatured in 4 M guanidine-HCl retained little optical activity. Upon dilution of the denatured enzyme, however, more than 90% of the ordered structure was recovered in 1 min, while the restoration of the activity proceeded much more slowly. Estimation of molecular weights by gel permeation chromatography indicated that the tetrameric enzyme is subject to reversible dissociation into monomeric subunits under the experimental conditions. Various environmental factors such as temperature, pH and protein concentration exhibited profound influence on the rate and extent of the reactivation. In order to examine the correlation between the restoration of the activity and the quaternary structure, electron microscopic inspection of the kinetic processes of reversible denaturation was attempted. Upon dilution of the denatured enzyme at 4 degrees C, neither the activity nor tetrameric images were detected over several min. Upon the temperature shift up to 25 degrees C, however, the activity regain was rapidly proceeded concomitant with the appearance of tetrameric molecules. These results are compatible with the possibility that the subunit assembly is an essential prerequisite, thought not sufficient, for enzyme activity.

Ammonia-Lyases↗
PubMed1976

The levels of main urinary metabolite of prostaglandin F1alpha and F2alpha in human subjects measured by radioimmunoassay.

Radioimmunoassay technique for measuring 5alpha, 7alpha-dihydroxy-11-keto-tetranorprosta-1, 16-dioic acid, the main urinary metabolite of PGF1alpha and PGF2alpha (PGF2alpha-MUM), was further improved. It was postulated based on some experimental data that the PGF2alpha-MUM exists in the urine mostly as dioic acid form, not as delta-lactone form the daily excretion of PGF2alpha-MUM in men ranged from 14.43 mug to 36.14 mug and in women from 5.21 mug to 14.25 mug.

Female↗
PubMed1976

Antagonism of 5-hydroxykynurenamine against serotonin action on platelet aggregation.

Serotonin induced an aggregation of human platelets, whereas 5-hydroxykynurenamine, produced from serotonin by the action of indoleamine 2,3-dioxygenase, did not cause any significant degree of platelet aggregation. 5-Hydroxykynurenamine specifically inhibited both a serotonin-induced aggregation of platelets and the potentiation of the ADP-induced platelet aggregation by serotonin. It did not, however, alter the profiles of the platelet aggregation induced by ADP, collagen, or adrenaline. The degree of inhibition was proportional to the time of preincubation of platelets with 5-hydroxykynurenamine, and to the concentration of 5-hydroxykynurenamine used. Available evidence indicated that 5-hydroxykynurenamine completed with serotonin for the same receptor sites. Studies with analogues of 5-hydroxykynurenamine indicated that the substitutions of 0-amino-benzyl moiety with hydroxy or methoxy groups were somewhat tolerated, whereas the masking of alkylamine moiety with N-acetylation completely lost the inhibitory activity.

Adenosine Diphosphate↗
PubMed1975

Studies on indoleamine 2,3-dioxygenase. I. Superoxide anion as substrate.

Indoleamine 2,3-dioxygenase purified to apparent homogeneity from rabbit intestine was inhibited by scavengers for superoxide anion such as superoxide dismutase and 1,2-dihydroxybenzene-3,5-disulfonic acid (Tiron). On the other hand, beta-carotene and 1,4-diazobicyclo-(2,2,2)-octane, scavengers for singlet oxygen, did not affect the enzyme activity significantly. The degree of inhibition of the dioxygenase by superoxide dismutase preparations from bovine erythrocytes, green peas, spinach leaves, and Escherichia coli paralleled that observed with these dismutase preparations on the aerobic reduction of cytochrome c by xanthine oxidase and its substrate. The pH profiles of the inhibition by dismutase of the dioxygenase and cytochrome c reduction were also similar and the maximal inhibition was observed around pH 10 in both cases. The degree of inhibition was not affected by the concentration of substrate but was a function of the concentration of dismutase. It was inversely related to the concentrations of the dioxygenase and its cofactors, ascorbic acid and methylene blue, both of which were required for maximum activity. Ascorbic acid could be replaced either by xanthine oxidase and its substrate, or by tetrabutylammonium superoxide prepared by electrolytic reduction of molecular oxygen, or by potassium superoxide. When limited amounts of superoxide anion were added to the reaction mixture containing a substrate amount of the dioxygenase, the ratio of the amount of superoxide anion added to that of the product formed was approximately unity both under aerobic and anaerobic conditions. Taken together, these findings indicate that superoxide anion, rather than molecular oxygen, is utilized as substrate by indoleamine 2,3-dioxygenase.

1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium ↗