Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.14.16.2 (tyrosine hydroxylase)
 14,760 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This investigation was carried out to determine if calcium prolongation of ethanol-induced sleep is mediated by calmodulin and a calmodulin-dependent protein kinase. The duration of ethanol-induced sleeping time in ddY male mice was measured following the administration of CaCl2 (20, 40, 80 and 200 mumol/kg, intraperitoneally (IP) both with and without the calmodulin antagonists, W-7: [N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide] (4.2 micrograms/mouse, intraventricular (IVT) or trifluoperazine (TFP; 1.8 micrograms/mouse, IVT). When CaCl2 was administered in a dose dependent manner the duration of ethanol-induced sleep was prolonged. The prolongation was antagonized by W-7 and TFP. When mice were treated with W-7 or TFP together with serotonin (5-HT; 15 nmol/mouse, IVT), dopamine (DA; 30 nmol/mouse, IVT) or norepinephrine (NE; 30 nmol/mouse, IVT), the sleeping time induced by ethanol and calcium was enhanced. This finding suggests that W-7 and TFP selectively inhibit the synthesis of 5-HT, DA and NE, but they do not affect other neuronal functions of these biogenic amines. The results would suggest a probable mechanism in which Ca++ prolongs ethanol-induced sleeping time by activating tyrosine hydroxylase and tryptophan hydroxylase through intracerebral calmodulin and calmodulin-dependent protein kinase, which subsequently raise the levels of 5-HT, DA and NE.
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PMID:Effect of calmodulin antagonists on calcium and ethanol-induced sleeping time in mice. 407 Mar 38

l-Ascorbate stimulates the enzymic hydroxylation of phenylalanine in vitro by recycling tetrahydrobiopterin, which reduces O(2) utilized in the reaction. It is suggested that ascorbate might have a similar function in vivo; this would explain the apparent regulation of tyrosine hydroxylase and tryptophan hydroxylase activities by this vitamin.
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PMID:The effect of L-ascorbate on catecholamine biosynthesis. 414 53

A selection procedure was devised for neurons and related cells that depends upon the ability of the cells to synthesize certain amine neurotransmitters. The rationale for selection is that tyrosine is an essential amino acid for most mammalian cells and that three enzymes from mammalian sources can catalyze the synthesis of tyrosine: phenylalanine hydroxylase (EC 1.14.16.1), tyrosine hydroxylase (EC 1.14.16.2), and tryptophan hydroxylase (EC 1.14.16.4). Tyrosine hydroxylase is found predominantly in adrenergic neurons and related cells that synthesize dopamine, norepinephrine, and epinephrine, and tryptophan hydroxylase in cells synthesizing serotonin or melatonin. Only 1 out of 70,000 uncloned mouse neuroblastoma cells grew well in the absence of tyrosine. Approximately 50% of the cell lines obtained by selection had tyrosine hydroxylase activity. This selection procedure thus provides a simple means of obtaining cell lines of neural origin on the basis of their ability to synthesize putative transmitters.
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PMID:Selection for neuroblastoma cells that synthesize certain transmitters. 415 49

Preference for ethyl alcohol was significantly reduced or totally abolished in rats given orally p-chlorophenylalanine, a tryptophan hydroxylase inhibitor that selectively depletes brain serotonin. Some aversion to alcohol was observed while p-chlorophenylalanine was administered, but the rats' rejection of alcohol was even more marked after the drug was discontinued. Oral administration of alpha-methyl-p-tyrosine, a tyrosine hydroxylase inhibitor that depletes brain catecholamines, slightly reduced selection of alcohol, but preference returned to normal as soon as alpha-methyl-p-tyrosine was terminated.
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PMID:Alcohol preference in the rat: reduction following depletion of brain serotonin. 569 Jan 48

Circadian variations in the activity of tyrosine hydroxylase, tyrosine aminotransferase, and tryptophan hydroxylase were observed in the rat brain stem. Tyrosine hydroxylase exhibited a bimodal pattern with peaks occurring during both the light and dark phases of the circadian cycle. Tyrosine aminotransferase had one daily peak of activity occurring late in the light phase, whereas tryptophan hydroxylase activity was maximal late in the dark phase. Circadian fluctuations in tyrosine hydroxylase activity did not correlate well with circadian variations in the turnover rates of norepinephrine or dopamine nor with levels of these catecholamines. This supports the idea that although tyrosine hydroxylase is the rate-limiting enzyme in the synthesis of catecholamines, other factors must also be involved in the in vivo regulation of this process. Administration of alpha-methyl-p-tyrosine (AMT) methyl ester HCl (100 mg/kg) had no effect on the activity of tryptophan hydroxylase, but effectively eliminated the peak of tyrosine hydroxylase activity that occurred during the light phase. AMT also lowered levels of tyrosine aminotransferase, but only at times near the daily light to dark transition. These chronotypic effects of AMT emphasize the importance of "time of day" as a factor that must be taken into account in evaluating the biochemical as well as the pharmacological and toxicological effects of drugs.
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PMID:Circadian variations in the activity of tyrosine hydroxylase, tyrosine aminotransferase, and tryptophan hydroxylase: relationship to catecholamine metabolism. 611 1

Acute administration of methamphetamine produced a dose-dependent depression of tryptophan hydroxylase (TPH) activity. The depression was observed in several serotonergic nerve terminal regions of the rat brain and spinal cord. Complete recovery of TPH activity following methamphetamine treatment occurred in all regions, but the time to recovery varied with the dose administered. In contrast to TPH, tyrosine hydroxylase (TH) was not affected by a single injection of methamphetamine. The data are discussed in the context of the effects of single versus repeated doses of methamphetamine on tryptophan and tyrosine hydroxylase.
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PMID:Methamphetamine-induced depression of tryptophan hydroxylase: recovery following acute treatment. 612 Aug 43

Neonatal changes in the activities of tyrosine hydroxylase (TH) and tryptophan hydroxylase (TrpH) and in the content of the co-factor, biopterin, were studied in rat midbrain for the first 20 days after birth. Changes in TH activity in the parotid and submandibular glands were also examined. Changes in TH activity per unit weight in the developing rat brain were briefly similar to those in the salivary glands; the activity increased from day 2 or 4 to day 9 after birth, and remained constant or slightly decreased at day 12, then rapidly increased on day 16. TrpH activity in the midbrain increased about twofold up to day 16. The biopterin concentration in the brain increased, reached a maximum level on day 12 after birth, and thereafter decreased. The effect of hyperthyroidism in rats given 0.2 mg/kg i.p. of thyroxine every 2 days postnatally was studied on the activity of TH in rat salivary glands at 12-day-old rats. In parotid or submandibular gland of hyperthyroid rats, TH activity increased at day 12 postnatally. In comparison with the effect on TH activity in the salivary glands, TH activity in the midbrain on day 20 postnatally was not induced by hyperthyroidism. Furthermore, increase of the TrpH activity and biopterin and catecholamine levels in the midbrain of hyperthyroid rats was not found on day 20 after birth in comparison with the corresponding controls. From these data, we suppose that postnatal hyperthyroidism may cause precocious induction of TH in rat salivary gland, but may not increase the activity of TH or TrpH, and the level of their co-factor, biopterin, in rat midbrain.
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PMID:Ontogenesis of monoamine-synthesizing enzyme activities and biopterin levels in rat brain or salivary glands, and the effects of thyroxine administration. 612 Oct 4

Unilateral injection of 5,7-dihydroxytryptamine (DHT) into the rat neostriatum markedly reduced not only striatal tryptophan hydroxylase (TPH) activity but also striatal tyrosine hydroxylase (TH) activity and dopamine (DA) concentration measured 10--15 days later. The decrease in striatal TH activity was dose related over the range of 8--32 micrograms of DHT; a dose of 16 micrograms reduced striatal TH activity to 40--50% of control, DA concentration to 38% of control, and TPH activity to 5--20% of control. Intrastriatal injection of 16 micrograms of DHT reduced TH activity in the ipsilateral substantia nigra to 51% of control. Pretreatment with amfonelic acid, a potent DA uptake inhibitor, significantly reduced the effect of DHT on striatal and nigral TH activity and striatal DA concentration without affecting the DHT-induced decrease in striatal TPH activity. Desmethylimipramine (5 and 25 mg/kg) had no effect on the DHT-induced decrease in striatal TH activity. Striatal choline acetyltransferase and glutamic acid decarboxylase activities were not decreased by 16 micrograms of DHT. The results indicate that DHT can alter dopaminergic function in the rat neostriatum through a direct effect of the drug on DA neurons.
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PMID:Biochemical evidence for alteration of neostriatal dopaminergic function by 5,7-dihydroxytryptamine. 612 Oct 11

The effect of dihydralazine on monoamine metabolism in the rat was investigated. Dihydralazine, 5 mg/kg i.v., reduced noradrenaline (NA) in the heart. After pretreatment with phenoxybenzamine an NA depletion was evident also in the brain. Dihydralazine did not affect the utilization of NA or dopamine in the brain as judged by the disappearance rates of these amines following synthesis inhibition by alpha-methyl-p-tyrosine. However, dihydralazine reduced the synthesis of monoamines as evidenced by a decreased accumulation of the monamine precursor dihydroxyphenylalanine (and 5-hydroxytryptamine) subsequent to treatment with NSD 1015. It is concluded that dihydralazine inhibits central tyrosine hydroxylase (and tryptophan hydroxylase) in the rat.
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PMID:Dihydralazine inhibits tyrosine hydroxylase in vivo in the rat. 612 15

L-Glutamine at the concentration present in cerebrospinal fluid decreases the steady-state accumulation of the aromatic amino acids tryptophan, tyrosine and dihydroxyphenylalanine (DOPA) in rat striatal synaptosomes. Glutamine significantly inhibits synaptosomal tryptophan hydroxylase activity; it has less marked effects on tyrosine hydroxylase and DOPA decarboxylase activities. Thus, interaction between glutamine and tryptophan transport into nerve terminals may be one of the factors regulating the rate of serotonin synthesis in vivo.
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PMID:Glutamine inhibits the accumulation and hydroxylation of tryptophan in rat striatal synaptosomes. 613 81


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