Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Women using oral contraceptives (OCs) have been found to excrete increased amounts of several metabolites arising from tryptophan catabolism, the most pronounced change being in xanthurenic acid and kynurenic acid excretion. The abnormality is largely corrected by the administration of pyridoxine, suggesting an increased need for vitamin B6 in OC users. Although a majority of malnourished and well-nourished women show the abnormality in tryptophan metabolism following OC use, investigators differ in their assessment of vitamin B6 status using other tests. The question of vitamin B6 deficiency in OC users is controversial. 2 types of multiparameter assessment approaches have been used to elucidate the vitamin B6 requirement of OC users. In a study of malnourished India women, it was observed that daily supplements of 10 mg pyridoxine from the day of starting contraception largely prevented the development of the abnormality in tryptophan metabolism. This level of supplementation also prevented the OC-mediated deterioration in vitamin B6 status as determined byerythrocyte aspartate aminotransferase activation. In another type of multiparametric approach Brown et al. and Laklem et al. measured the pyridoxine status of OC users on known intakes of the vitamin in a depletion followed by repletion study. Despite the current controversy, it might be advisable to supplement women using OC with pyridoxine to ensure a daily intake of at least 5 mg vitamin B6.
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PMID:The vitamin B6 requirement in oral contraceptive users. 39 35

Patients infected with Schistosoma mansoni showed an abnormal response to a test dose of tryptophan, with little increase in the urinary excretion of kynurenine, hydroxykynurenine, xanthurenic and kynurenic acids, N1-methyl nicotinamide, methyl pyridone carboxamide, 5-hydroxytryptamine or 5-hydroxyindoleacetic acid. In contrast to previous reports, this is different from the pattern of tryptophan metabolism seen in vitamin B6 deficiency. Furthermore, the patients' plasma concentrations of pyridoxal phosphate were within the reference range, and supplementation for 5 days with 20 mg vitamin B6/day did not affect tryptophan metabolism. Treatment with a single dose of Praziquantel resulted in a substantial restoration of normal tryptophan metabolism. In mice infected with S. mansoni there was a similar impairment of tryptophan metabolism, as shown by considerably reduced formation of 14CO2 after the administration of a tracer dose of [14C]tryptophan. Again, the administration of vitamin B6 supplements did not correct tryptophan metabolism in the mice. Treatment with Praziquantel resulted in substantial restoration of the production of 14CO2 from [14C]tryptophan. There was no evidence of vitamin B6 deficiency (as determined by erythrocyte aspartate aminotransferase activation coefficient) associated with infection in the mice, although there was a redistribution of pyridoxal phosphate between tissues, with a reduction in the concentration of liver, spleen and kidney, and an increase in skeletal muscle.
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PMID:Tryptophan metabolism and vitamin B6 nutritional status in patients with schistosomiasis mansoni and in infected mice. 164 Dec 43

Forty-five male Lohmann chicks were grown up to 6 weeks of age. The experimental diet containing a high protein level (30%) was aimed at increasing the metabolic need for PN. Microbiological analysis on the basal ration revealed a marginal content of 4.7 mumol PN/kg. The vitamin B6 status was assessed at the end of the experiment according to the basal activity of aspartate aminotransferase (AspAT) in plasma and in erythrocytes, and the in vitro stimulated activity with pyridoxal 5'-phosphate (PLP). None of the deficient chicks had any clinical signs attributable to malfunction of the nervous system, and they grew as well as those receiving the control diet. Vitamin B6 deficiency was biochemically confirmed by a significant depression of AspAT activity in plasma (p less than 0.001) and in erythrocytes (p less than 0.01). The addition of PLP in vitro enhanced the catalytic activity of the plasma enzyme, but had negligible effect on the erythrocyte enzyme. The degree of stimulation in vitro of the apoenzyme of AspAT not only depends on the endogenous vitamin B6 content, but also on the basal activity of the enzyme. A 15-day repletion period with a daily oral dose (50 mumol PN) did not result in a complete restoration of the enzyme activity, indicating that the availability of apoenzyme had been curtailed. This experiment demonstrated that chicks fed a high protein corn-soyamin diet with a limited amount of PN but containing Saccharomyces yeast showed no nervous signs or perosis, but significant metabolic disturbances.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Aspartate aminotransferase activity in experimentally induced asymptomatic vitamin B6 deficiency in chicks. 205 99

We have studied vitamin B6 status in 26 uremic patients, 18 on maintenance hemodialysis and 8 nonhemodialyzed. The vitamin B6 status was estimated by an assay of erythrocyte aspartate aminotransferase and coenzyme stimulation. Hemodialyzed uremic patients were found to have vitamin B6 deficiency. Patients were treated with 150 mg pyridoxine hydrochloride daily for 4 weeks. Erythrocyte aspartate aminotransferase increased significantly in both groups of uremic patients, the increase being greater in hemodialyzed patients. In vitro pyridoxal phosphate stimulation produces an erythrocyte aspartate aminotransferase activity greater than that obtained before pyridoxine hydrochloride administration. After cessation of pyridoxine hydrochloride treatment, erythrocyte aspartate aminotransferase decreases in hemodialyzed patients, while it remains elevated in nonhemodialyzed patients. The data obtained appear to indicate that vitamin B6 administration to patients with chronic renal insufficiency must be appraised not only for correcting the deficit but also for increasing the intracellular pyridoxal phosphate concentration, which could modify the possible functional impairment at the level of apoenzymes that use pyridoxal phosphate.
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PMID:Vitamin B6 status in uremia. 231 6

Twelve patients with carpal tunnel syndrome were studied. Clinical and electrophysiological data were obtained and an estimation of vitamin B6 (pyridoxine) status by an assay of erythrocyte aspartate aminotransferase and coenzyme stimulation assay were done. None of the patients was found to have vitamin B6 deficiency. Patients were treated with 150 mg of pyridoxine daily for 3 months. Erythrocyte aspartate aminotransferase increased significantly (p less than 0.001) in all the patients. In 6 patients there were clinical and electrophysiological improvement and erythrocyte aspartate aminotransferase increased more than in the other 6 patients. The data obtained appear to indicate that although vitamin B6 deficiency is not common in carpal tunnel syndrome patients, pyridoxine supplementation can be recommended as adjuvant treatment in those patients undergoing surgery.
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PMID:Carpal tunnel syndrome and vitamin B6. 292 40

1. In vitro activation of erythrocyte aspartate aminotransferase (EC 2.6.1.1) activity by pyridoxal phosphate was used to assess vitamin B6 nutritional status in forty Sudanese women taking combined, low-dose oral contraceptives (oestrogen-progestogen; OC) and in thirty healthy, non-pregnant women not taking OC. 2. Fourteen (35%) out of forty OC users showed apparent vitamin B6 deficiency. 3. Side-effects associated with OC were more common among the apparently vitamin-B6-deficient OC users than among OC users and non-OC users not deficient in vitamin B6.
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PMID:The effect of oral contraceptives on the apparent vitamin B6 status in some Sudanese women. 367 17

The development of a simple enzymatic method for the determination of blood and plasma pyridoxal 5'-phosphate (PLP) using pig heart apo-aspartate transaminase (apo-AST) is described. The technique requires three steps: sample extraction using perchloric acid, a binding step in which PLP in the sample extract is attached to the apo-AST and the enzymatic assay of the reconstituted holo-AST. PLP extracts were analysed with and without a known concentration of added PLP to correct for variation in recovery between different specimens. Procedures are outlined for manual and automatic analysis of the PLP extracts. Using the KONE Clinical Analyser after the extraction step, it is possible to measure enzyme activity in 100 specimens (i.e. 400 tubes) in a 5 h period. Results are shown from 185 healthy women aged 20-45 years, in which plasma PLP concentrations ranged from 5 to 165 nmol/L, and 142 men and 56 women in government service aged 17-64 years, whose plasma PLP ranged from 8 to 169 nmol/L. Values less than 20 nmol/L are believed to indicate vitamin B6 deficiency and the method is able to measure 5 nmol/L.
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PMID:A direct assay for pyridoxal 5'-phosphate using pig heart apo-aspartate transaminase. 378 39

The vitamin B6 status of 60 institutionalised elderly subjects (group A: 31 men, mean age = 77 yr and 29 women, mean age = 84 yr) and 41 healthy young adults (group B or control group: 18 men, mean age = 30 yr and 23 women, mean age = 27 yr) was evaluated using erythrocyte aspartate aminotransferase activity coefficient (alpha EGOT) and plasma pyridoxal phosphate (PLP) level (vitamin B6-deficient subjects = alpha greater than 2.0 and PLP less than 80 nmol/l). The kilocalorie, protein and pyridoxine intakes were also estimated. Regarding calories and protein, the diets may be generally considered satisfactory in respect to the French 1981 RDA. The mean dietary intake of vitamin B6 was less than 2 mg/day in all groups. Ninety per cent of the aged, 80 per cent of females in group B in contrast to 56 per cent of males in group B consumed less than their individual vitamin B6 requirements as determined by a probability method. As the incidence of vitamin B6 biochemical deficiency was much higher in the group A (71% for males and 86% for females) than in the control group (11% for males and 30% for females), it is concluded that the high incidence of biochemical vitamin B6 deficiency noted in the aged appeared more relevant from an altered metabolism of the vitamin than from a too low energy intake. Supplements with high doses of vitamin B6 to aged subjects caused a significant decrease in alpha EGOT and a significant increase in PLP levels.
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PMID:Evaluation of pyridoxine intake and pyridoxine status among aged institutionalised people. 650 Aug 42

Vitamin B6 deficiency led to a decrease in aspartate: 2-oxoglutarate aminotransferase activity and to a marked increase in phenylalanine:2-oxoglutarate aminotransferase activity in rat small intestines. The increased phenylalanine aminotransferase activity was found to be due to a newly appeared aromatic aminotransferase without the aspartate aminotransferase activity in the cytosol of the small intestinal mucosa. The enzyme preparation had an isoelectric point of pH 8.5, a pH optimum near 8.0, and a molecular weight of approximately 100,000 with two identical subunits. The enzyme showed aminotransferase activities towards various aromatic L-amino acids with 2-oxoglutarate as the amino acceptor. The order of effectiveness of aromatic L-amino acids was phenylalanine > tryptophan > tyrosine > 5-hydroxytryptophan; very little activity was detected with other L-amino acids that were tested. The enzyme was specific for 2-oxoglutarate as the amino acceptor. The enzyme was not detected in other tissues (liver, kidney, heart, and brain) from both control and vitamin B6-deficient rats. The enzyme has never been described before in animal tissues.
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PMID:The appearance of a new aromatic aminotransferase in the small intestines of vitamin B6-deficient rats. 743 Jan 6

The level of mRNA for cytosolic aspartate aminotransferase (cAST) in the liver of vitamin B6-deficient rats was found to be 7-fold higher than that of the control rats. The administration of hydrocortisone to adrenalectomized vitamin B6-deficient rats induced expression of hepatic cAST mRNA and the induction was suppressed by the simultaneous administration of pyridoxine. Since the 5' regulatory region of the rat cAST gene contains several sequences showing homology to glucocorticoid-responsive elements, we synthesized an oligonucleotide probe of glucocorticoid-responsive element sequence and assayed the binding activity of liver nuclear extract to the oligonucleotide by gel mobility shift analysis. We found that the binding activity of nuclear extract prepared from the liver of vitamin B6-deficient rats was far greater than that of the control rats, indicating that the DNA-binding activity of glucocorticoid receptor was enhanced by vitamin B6 deficiency. We further found that preincubation of the nuclear extract from the vitamin-deficient liver with pyridoxal 5'-phosphate brought about a rapid and extensive decrease in the binding of the extract to the glucocorticoid-responsive element. Congeners of pyridoxal phosphate, such as pyridoxamine 5'-phosphate, pyridoxal, pyridoxamine and pyridoxine, did not show an inhibitory effect. These observations suggest that pyridoxal 5'-phosphate modulates cAST gene expression by inactivating the binding activity of glucocorticoid receptor to glucocorticoid-responsive elements.
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PMID:Pyridoxal 5'-phosphate modulates expression of cytosolic aspartate aminotransferase gene by inactivation of glucocorticoid receptor. 747 80


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