Log in

Relevant bibliographies by topics / Tryptophane hydroxylase / Journal articles

To see the other types of publications on this topic, follow the link: Tryptophane hydroxylase.

Journal articles on the topic 'Tryptophane hydroxylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Tryptophane hydroxylase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Bókay, János. "A tetrahidrobiopterin (BH4)-deficientia diagnosztikája és kezelése." Orvosi Hetilap 158, no. 48 (December 2017): 1897–902. http://dx.doi.org/10.1556/650.2017.30895.

Full text

Abstract:

Abstract: Since the initial breaking discovery of Følling that the severe neurological consequences of phenylketonuria could be prevented by use of low phenylalanine (Phe) diet, it has been shortly recognised that defective phenylalanine metabolism may also arise from the deficiency of tetrahydrobiopterin (BH4) cofactor, required for phenylalanine-hydroxylase activity. Furthermore, as BH4 is in Phe metabolism, it is also a cofactor for the activities of tyrosine hydroxylase and tryptophane hydroxylase, enzymes required for the synthesis of catecholamines and serotonin neurotransmitters. Besides hyperphenylalaninemia in patients with tetrahydrobiopterin deficiencies, dopamine and serotonin deficiencies, with different disorders of the central nervous system also develop. Mild form of tetrahydrobiopterin deficiency is rare, most of the patients have severe neurological abnormalities including progressive mental retardation if not treated properly. Early diagnosis and treatment are essential and can improve the clinical course and prognosis. Orv Hetil. 2017; 158(48): 1897–1902.

APA, Harvard, Vancouver, ISO, and other styles

2

Mallet, J. "Control of the expression of genes related to serotonergic transmission: The tryptophane hydroxylase implication." European Neuropsychopharmacology 8 (November 1998): S74. http://dx.doi.org/10.1016/s0924-977x(98)80036-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Werner, Ernst R. "Three classes of tetrahydrobiopterin-dependent enzymes." Pteridines 24, no. 1 (June 1, 2013): 7–11. http://dx.doi.org/10.1515/pterid-2013-0003.

Full text

Abstract:

AbstractCurrent knowledge distinguishes three classes of tetrahydrobiopterin-dependent enzymes as based on protein sequence similarity. These three protein sequence clusters hydroxylate three types of substrate atoms and use three different forms of iron for catalysis. The first class to be discovered was the aromatic amino acid hydroxylases, which, in mammals, include phenylalanine hydroxylase, tyrosine hydroxylase, and two isoforms of tryptophan hydroxylases. The protein sequences of these tetrahydrobiopterin-dependent aromatic amino acid hydroxylases are significantly similar, and all mammalian aromatic amino acid hydroxylases require a non-heme-bound iron atom in the active site of the enzyme for catalysis. The second classes of tetrahydrobiopterin-dependent enzymes to be characterized were the nitric oxide synthases, which in mammals occur as three isoforms. Nitric oxide synthase protein sequences form a separate cluster of homologous sequences with no similarity to aromatic amino acid hydroxylase protein sequences. In contrast to aromatic amino acid hydroxylases, nitric oxide synthases require a heme-bound iron for catalysis. The alkylglycerol monooxygenase protein sequence was the most recent to be characterized. This sequence shares no similarity with aromatic amino acid hydroxylases and nitric oxide synthases. Motifs contained in the alkylglycerol monooxygenase protein sequence suggest that this enzyme may use a di-iron center for catalysis.

APA, Harvard, Vancouver, ISO, and other styles

4

Cotton, R. G. H., W. McAdam, I. Jennings, and F. J. Morgan. "A monoclonal antibody to aromatic amino acid hydroxylases. Identification of the epitope." Biochemical Journal 255, no. 1 (October 1, 1988): 193–96. http://dx.doi.org/10.1042/bj2550193.

Full text

Abstract:

PH8 monoclonal antibody has previously been shown to react with all three aromatic amino acid hydroxylases, being particularly useful for immunohistochemical staining of brain tissue [Haan, Jennings, Cuello, Nakata, Chow, Kushinsky, Brittingham & Cotton (1987) Brain Res. 426, 19-27]. Western-blot analysis of liver extracts showed that PH8 reacted with phenylalanine hydroxylase from a wide range of vertebrate species. The epitope for antibody PH8 has been localized to the human phenylalanine hydroxylase sequence between amino acid residues 139 and 155. This highly conserved region of the aromatic amino acid hydroxylases has 11 out of 17 amino acids identical in phenylalanine hydroxylase, tyrosine hydroxylase and tryptophan hydroxylase.

APA, Harvard, Vancouver, ISO, and other styles

5

Triki, S., A. Fakhfakh, I. Marbouk, F. Neffati, A. Omezzine, and M. F. Najjar. "Implication du polymorphisme A218C du gène de la tryptophane hydroxylase 1 (TPH1) dans la dépression chez les diabétiques type 2." Annales d'Endocrinologie 79, no. 4 (September 2018): 269. http://dx.doi.org/10.1016/j.ando.2018.06.214.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Rodriguez Cetina Biefer, Hector, Anju Vasudevan, and Abdallah Elkhal. "Aspects of Tryptophan and Nicotinamide Adenine Dinucleotide in Immunity: A New Twist in an Old Tale." International Journal of Tryptophan Research 10 (January 1, 2017): 117864691771349. http://dx.doi.org/10.1177/1178646917713491.

Full text

Abstract:

Increasing evidence underscores the interesting ability of tryptophan to regulate immune responses. However, the exact mechanisms of tryptophan’s immune regulation remain to be determined. Tryptophan catabolism via the kynurenine pathway is known to play an important role in tryptophan’s involvement in immune responses. Interestingly, quinolinic acid, which is a neurotoxic catabolite of the kynurenine pathway, is the major pathway for the de novo synthesis of nicotinamide adenine dinucleotide (NAD+). Recent studies have shown that NAD+, a natural coenzyme found in all living cells, regulates immune responses and creates homeostasis via a novel signaling pathway. More importantly, the immunoregulatory properties of NAD+ are strongly related to the overexpression of tryptophan hydroxylase 1 (Tph1). This review provides recent knowledge of tryptophan and NAD+ and their specific and intriguing roles in the immune system. Furthermore, it focuses on the mechanisms by which tryptophan regulates NAD+ synthesis as well as innate and adaptive immune responses.

APA, Harvard, Vancouver, ISO, and other styles

7

Iyer, Shyam R., Kasper D. Tidemand, Jeffrey T. Babicz, Ariel B. Jacobs, Leland B. Gee, Lærke T. Haahr, Yoshitaka Yoda, et al. "Direct coordination of pterin to FeII enables neurotransmitter biosynthesis in the pterin-dependent hydroxylases." Proceedings of the National Academy of Sciences 118, no. 15 (April 5, 2021): e2022379118. http://dx.doi.org/10.1073/pnas.2022379118.

Full text

Abstract:

The pterin-dependent nonheme iron enzymes hydroxylate aromatic amino acids to perform the biosynthesis of neurotransmitters to maintain proper brain function. These enzymes activate oxygen using a pterin cofactor and an aromatic amino acid substrate bound to the FeII active site to form a highly reactive FeIV = O species that initiates substrate oxidation. In this study, using tryptophan hydroxylase, we have kinetically generated a pre-FeIV = O intermediate and characterized its structure as a FeII-peroxy-pterin species using absorption, Mössbauer, resonance Raman, and nuclear resonance vibrational spectroscopies. From parallel characterization of the pterin cofactor and tryptophan substrate–bound ternary FeII active site before the O2 reaction (including magnetic circular dichroism spectroscopy), these studies both experimentally define the mechanism of FeIV = O formation and demonstrate that the carbonyl functional group on the pterin is directly coordinated to the FeII site in both the ternary complex and the peroxo intermediate. Reaction coordinate calculations predict a 14 kcal/mol reduction in the oxygen activation barrier due to the direct binding of the pterin carbonyl to the FeII site, as this interaction provides an orbital pathway for efficient electron transfer from the pterin cofactor to the iron center. This direct coordination of the pterin cofactor enables the biological function of the pterin-dependent hydroxylases and demonstrates a unified mechanism for oxygen activation by the cofactor-dependent nonheme iron enzymes.

APA, Harvard, Vancouver, ISO, and other styles

8

Kulikov, A. V., V. S. Naumenko, D. V. Bazovkina, V. Yu Dee, D. V. Osipova, and N. K. Popova. "Effect of Mouse Chromosome 13 Terminal Fragment on Liability to Catalepsy and Expression of Tryptophane Hydroxylase-2, Serotonin Transporter, and 5-HT1A Receptor Genes in the Brain." Bulletin of Experimental Biology and Medicine 147, no. 5 (May 2009): 621–24. http://dx.doi.org/10.1007/s10517-009-0567-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Betari, Nibal, Kristoffer Sahlholm, Yuta Ishizuka, Knut Teigen, and Jan Haavik. "Discovery and biological characterization of a novel scaffold for potent inhibitors of peripheral serotonin synthesis." Future Medicinal Chemistry 12, no. 16 (August 2020): 1461–74. http://dx.doi.org/10.4155/fmc-2020-0127.

Full text

Abstract:

Aim: Tryptophan hydroxylase 1 (TPH1) catalyzes serotonin synthesis in peripheral tissues. Selective TPH1 inhibitors may be useful for treating disorders related to serotonin dysregulation. Results & methodology: Screening using a thermal shift assay for TPH1 binders yielded Compound 1 (2-(4-methylphenyl)-1,2-benzisothiazol-3(2 H)-one), which showed high potency (50% inhibition at 98 ± 30 nM) and selectivity for inhibiting TPH over related aromatic amino acid hydroxylases in enzyme activity assays. Structure–activity relationships studies revealed several analogs of 1 showing comparable potency. Kinetic studies suggested a noncompetitive mode of action of 1, with regards to tryptophan and tetrahydrobiopterin. Computational docking studies and live cell assays were also performed. Conclusion: This TPH1 inhibitor scaffold may be useful for developing new therapeutics for treating elevated peripheral serotonin.

APA, Harvard, Vancouver, ISO, and other styles

10

Rönnberg, Elin, Gabriela Calounova, and Gunnar Pejler. "Mast cells express tyrosine hydroxylase and store dopamine in a serglycin-dependent manner." Biological Chemistry 393, no. 1-2 (January 1, 2012): 107–12. http://dx.doi.org/10.1515/bc-2011-220.

Full text

Abstract:

AbstractHere we show that mast cells contain dopamine and that mast cell activation causes dopamine depletion, indicating its presence within secretory granules. Dopamine storage increased during mast cell maturation from bone marrow precursors, and was dependent on the presence of serglycin. Moreover, the expression of tyrosine hydroxylase, the key enzyme in dopamine biosynthesis, was induced during mast cell maturation; histidine decarboxylase and tryptophan hydroxylase 1 were also induced. Mast cell activation caused a robust induction of histidine decarboxylase, but no stimulation of tyrosine hydroxylase or tryptophan hydroxylase 1 expression. The present study points toward a possible role of dopamine in mast cell function.

APA, Harvard, Vancouver, ISO, and other styles

11

Ren, Guiqi, Song Li, Hanbing Zhong, and Shuo Lin. "Zebrafish Tyrosine Hydroxylase 2 Gene Encodes Tryptophan Hydroxylase." Journal of Biological Chemistry 288, no. 31 (June 10, 2013): 22451–59. http://dx.doi.org/10.1074/jbc.m113.485227.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Castaño Casas, Juan, Juan Barona, Flavio Betancourth, and Doris Salazar. "Altered 3D Structure of Human Tryptophan Hydroxylase-2 Caused by Change in the amino acid 341: In Silico Analysis." Journal of Morphological Sciences 35, no. 03 (September 2018): 198–202. http://dx.doi.org/10.1055/s-0038-1675830.

Full text

Abstract:

Introduction Neuropsychiatric syndromes have an important connection with disorders in the regulation of serotonin, with human tryptophan hydroxylase-2 being one of the related biosynthetic enzymes of this neurotransmitter. Evidence-based genetic studies suggest a possible involvement of this enzyme in neuropsychiatric disorders caused by abnormalities in the synthesis and regulation of serotonin. Objective To analyze the structural effects of single nucleotide polymorphism (SNP) in the enzyme tryptophan hydroxylase-2 and the changes that lead to functional alterations. Materials and Methods In this study, we performed an in silico analysis of SNPs associated with abnormal folding of the tryptophan hydroxylase-2 protein. Different programs were used to identify amino acid changes evidencing pathogenic effects and possible functional impairments. Results A change in the amino acid 341 (lysine [L]for phenylalanine [F]) (L341F) of the protein chain affects the total enthalpy of the protein. The enthalpy turned positive due to the energy required for the amino acid to return to its original condition. The protein function is also affected negatively because of the altered structured. Conclusion The change in the L341F leads to serious structural defects in the tryptophan hydroxylase-2. Those defects can be further related with functional instability and associated to the etiology of neuropsychiatric diseases.

APA, Harvard, Vancouver, ISO, and other styles

13

Mangge, Harald, Wolfgang J. Schnedl, Sebastian Schröcksnadel, Simon Geisler, Christian Murr, and Dietmar Fuchs. "Immune activation and inflammation in patients with cardiovascular disease are associated with elevated phenylalanine-to-tyrosine ratios." Pteridines 24, no. 1 (June 1, 2013): 51–55. http://dx.doi.org/10.1515/pterid-2013-0002.

Full text

Abstract:

AbstractHigher serum neopterin concentrations and kynurenine-to-tryptophan (Kyn/Trp) ratios are associated with increased mortality in patients with coronary artery disease (CAD). Preferentially, Th1-type cytokine interferon-γ stimulates tryptophan breakdown and neopterin production by GTP cyclohydrolase I (GCH-I) in parallel in monocyte-derived macrophages and dendritic cells. In other cells, activation of GCH-I leads to the formation of 5,6,7,8-tetrahydrobiopterin (BH4), the necessary cofactor of amino acid hydroxylases such as phenylalanine 4-hydroxylase (PAH) and nitric oxide synthases. In 31 CAD patients (70.3±9.9 years; 21 males, 10 females), we determined serum concentrations of phenylalanine, tyrosine, and Kyn/Trp by HPLC, neopterin by ELISA, and nitrite by the colorimetric Griess assay. The phenylalanine-to-tyrosine ratio (Phe/Tyr) served as an estimate of PAH enzyme activity. Elevated Phe/Tyr concentrations were detected in a subgroup of CAD patients and correlated with Kyn/Trp (r=0.396, p<0.05) and neopterin (r=0.354, p<0.05) and inversely with nitrite (r=–0.371, p<0.05) concentrations. Higher Phe/Tyr in patients is associated with immune activation and indicates subnormal PAH activity that might be involved in the precipitation of neuropsychiatric symptoms in CAD patients.

APA, Harvard, Vancouver, ISO, and other styles

14

Boularand, Sylviane, Michèle C. Darmon, and Jacques Mallet. "The Human Tryptophan Hydroxylase Gene." Journal of Biological Chemistry 270, no. 8 (February 24, 1995): 3748–56. http://dx.doi.org/10.1074/jbc.270.8.3748.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Mockus, Susan M., Sean C. Kumer, and Kent E. Vrana. "A chimeric tyrosine/tryptophan hydroxylase." Journal of Molecular Neuroscience 9, no. 1 (June 1997): 35–48. http://dx.doi.org/10.1007/bf02789393.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Zhang, Jiantao, Chaochen Wu, Jiayuan Sheng, and Xueyang Feng. "Molecular basis of 5-hydroxytryptophan synthesis in Saccharomyces cerevisiae." Molecular BioSystems 12, no. 5 (2016): 1432–35. http://dx.doi.org/10.1039/c5mb00888c.

Full text

Abstract:

We report for the first time that 5-hydroxytryptophan can be synthesized in Saccharomyces cerevisiae by heterologously expressing prokaryotic phenylalanine 4-hydroxylase or eukaryotic tryptophan 3/5-hydroxylase, together with enhanced synthesis of MH4 or BH4 cofactors.

APA, Harvard, Vancouver, ISO, and other styles

17

Yohrling, G. J., G. C. T. Jiang, S. M. Mockus, and K. E. Vrana. "Intersubunit binding domains within tyrosine hydroxylase and tryptophan hydroxylase." Journal of Neuroscience Research 61, no. 3 (2000): 313–20. http://dx.doi.org/10.1002/1097-4547(20000801)61:3<313::aid-jnr9>3.0.co;2-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Mockus, Susan M., George J. Yohrling, and Kent E. Vrana. "Tyrosine hydroxylase and tryptophan hydroxylase do not form heterotetramers." Journal of Molecular Neuroscience 10, no. 1 (February 1998): 45–51. http://dx.doi.org/10.1007/bf02737084.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Grenett, H. E., F. D. Ledley, L. L. Reed, and S. L. Woo. "Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases." Proceedings of the National Academy of Sciences 84, no. 16 (August 1, 1987): 5530–34. http://dx.doi.org/10.1073/pnas.84.16.5530.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Walther, Diego J., and Michael Bader. "A unique central tryptophan hydroxylase isoform." Biochemical Pharmacology 66, no. 9 (November 2003): 1673–80. http://dx.doi.org/10.1016/s0006-2952(03)00556-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Serretti, Alessandro, Roberta Lilli, Cristina Lorenzi, Enrico Lattuada, Cristina Cusin, and Enrico Smeraldi. "Tryptophan hydroxylase gene and major psychoses." Psychiatry Research 103, no. 1 (August 2001): 79–86. http://dx.doi.org/10.1016/s0165-1781(01)00269-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Roberts, Kenneth M., and Paul F. Fitzpatrick. "Mechanisms of tryptophan and tyrosine hydroxylase." IUBMB Life 65, no. 4 (February 26, 2013): 350–57. http://dx.doi.org/10.1002/iub.1144.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Bennett, P. J., W. M. McMahon, J. Watabe, J. Achilles, M. Bacon, H. Coon, T. Grey, et al. "Tryptophan hydroxylase polymorphisms in suicide victims." Psychiatric Genetics 10, no. 1 (March 2000): 13–17. http://dx.doi.org/10.1097/00041444-200010010-00003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Sawada, Makoto, and Toshiharu Nagatsu. "Tryptophan hydroxylase activity in brain slices." International Journal of Biochemistry 20, no. 10 (January 1988): 1033–38. http://dx.doi.org/10.1016/0020-711x(88)90247-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Betari, Nibal, Knut Teigen, Kristoffer Sahlholm, and Jan Haavik. "Synthetic corticosteroids as tryptophan hydroxylase stabilizers." Future Medicinal Chemistry 13, no. 17 (September 2021): 1465–74. http://dx.doi.org/10.4155/fmc-2021-0068.

Full text

Abstract:

Background: Clinically, corticosteroids are used mainly for their immune-modulatory properties but are also known to influence mood. Despite evidence of a role in regulating tryptophan hydroxylases (TPH), key enzymes in serotonin biosynthesis, a direct action of corticosteroids on these enzymes has not been systematically investigated. Methodology & results: Corticosteroid effects on TPHs were tested using an in vitro assay. The compound with the strongest modulatory effect, beclomethasone dipropionate, activated TPH1 and TPH2 with low micromolar potency. Thermostability assays suggested a stabilizing mechanism, and computational docking indicated that beclomethasone dipropionate interacts with the TPH active site. Conclusion: Beclomethasone dipropionate is a stabilizer of TPHs, acting as a pharmacological chaperone. Our findings may inspire further development of steroid scaffolds as putative antidepressant drugs.

APA, Harvard, Vancouver, ISO, and other styles

26

Izikki, M., N. Hanoun, E. Marcos, L. Savale, A. M. Barlier-Mur, F. Saurini, S. Eddahibi, M. Hamon, and S. Adnot. "Tryptophan hydroxylase 1 knockout and tryptophan hydroxylase 2 polymorphism: effects on hypoxic pulmonary hypertension in mice." American Journal of Physiology-Lung Cellular and Molecular Physiology 293, no. 4 (October 2007): L1045—L1052. http://dx.doi.org/10.1152/ajplung.00082.2007.

Full text

Abstract:

Serotonin [5-hydroxytryptamine (5-HT)] biosynthesis depends on two rate-limiting tryptophan hydroxylases (Tph): Tph1, which is expressed in peripheral organs, and Tph2, which is expressed in neurons. Because 5-HT is involved in pulmonary hypertension (PH), we investigated whether genetic variations in Tph1 and/or Tph2 affected PH development in mice. To examine the functional impact of peripheral Tph1 deficiency on hypoxic PH, we used Tph1−/− mice characterized by very low 5-HT synthesis rates and contents in the gut and lung and increased 5-HT synthesis in the forebrain. With chronic hypoxia, 5-HT synthesis in the forebrain increased further. Hypoxic PH, right ventricular hypertrophy, and distal pulmonary artery muscularization were less severe ( P < 0.001) than in wild-type controls. The Tph inhibitor p-chlorophenylalanine (100 mg·kg−1·day−1) further improved these parameters. We then investigated whether mouse strains harboring the C1473G polymorphism of the Tph2 gene showed different PH phenotypes during hypoxia. Forebrain Tph activity was greater and hypoxic PH was more severe in C57Bl/6 and 129X1/SvJ mice homozygous for the 1473C allele than in DBA/2 and BALB/cJ mice homozygous for the 1473G allele. p-Chlorophenylalanine reduced PH in all groups and abolished the difference in PH severity across mouse strains. Hypoxia increased 5-hydroxytryptophan accumulation but decreased 5-HT contents in the forebrain and lung, suggesting accelerated 5-HT turnover during hypoxia. These results provide evidence that dysregulation of 5-HT synthesis is closely linked to the hypoxic PH phenotype in mice and that Tph1 and Tph2 may contribute to PH development.

APA, Harvard, Vancouver, ISO, and other styles

27

Porter, Richard J., Roger T. Mulder, Peter R. Joyce, Allison L. Miller, and Martin Kennedy. "Tryptophan hydroxylase gene (TPH1) and peripheral tryptophan levels in depression." Journal of Affective Disorders 109, no. 1-2 (July 2008): 209–12. http://dx.doi.org/10.1016/j.jad.2007.11.010.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Nowak, Elizabeth C., Victor C. de Vries, Anna Wasiuk, Cory Ahonen, Kathryn A. Bennett, Isabelle Le Mercier, Dae-Gon Ha, and Randolph J. Noelle. "Tryptophan hydroxylase-1 regulates immune tolerance and inflammation." Journal of Experimental Medicine 209, no. 11 (September 24, 2012): 2127–35. http://dx.doi.org/10.1084/jem.20120408.

Full text

Abstract:

Nutrient deprivation based on the loss of essential amino acids by catabolic enzymes in the microenvironment is a critical means to control inflammatory responses and immune tolerance. Here we report the novel finding that Tph-1 (tryptophan hydroxylase-1), a synthase which catalyses the conversion of tryptophan to serotonin and exhausts tryptophan, is a potent regulator of immunity. In models of skin allograft tolerance, tumor growth, and experimental autoimmune encephalomyelitis, Tph-1 deficiency breaks allograft tolerance, induces tumor remission, and intensifies neuroinflammation, respectively. All of these effects of Tph-1 deficiency are independent of its downstream product serotonin. Because mast cells (MCs) appear to be the major source of Tph-1 and restoration of Tph-1 in the MC compartment in vivo compensates for the defect, these experiments introduce a fundamentally new mechanism of MC-mediated immune suppression that broadly impacts multiple arms of immunity.

APA, Harvard, Vancouver, ISO, and other styles

29

HEYES, Melvyn P., Cai Y. CHEN, Eugene O. MAJOR, and Kuniaki SAITO. "Different kynurenine pathway enzymes limit quinolinic acid formation by various human cell types." Biochemical Journal 326, no. 2 (September 1, 1997): 351–56. http://dx.doi.org/10.1042/bj3260351.

Full text

Abstract:

Substantial increases in the tryptophan–kynurenine pathway metabolites, L-kynurenine and the neurotoxin quinolinic acid, occur in human brain, blood and systemic tissues during immune activation. Studies in vitrohave shown that not all human cells are capable of synthesizing quinolinate. To investigate further the mechanisms that limit L-kynurenine and quinolinate production, the activities of kynurenine pathway enzymes and the ability of different human cells to convert pathway intermediates into quinolinate were compared. Stimulation with interferon γ substantially increased indoleamine 2,3-dioxygenase activity and L-kynurenine production in primary peripheral blood macrophages and fetal brains (astrocytes and neurons), as well as cell lines derived from macrophage/monocytes (THP-1), U373MG astrocytoma, SKHEP1 liver and lung (MRC-9). High activities of kynurenine 3-hydroxylase, kynureninase or 3-hydroxyanthranilate 3,4-dioxygenase were found in interferon-γ-stimulated macrophages, THP-1 cells and SKHEP1 cells, and these cells made large amounts of quinolinate when supplied with L-tryptophan, L-kynurenine, 3-hydroxykynurenine or 3-hydroxyanthranilate. Quinolinate production by human fetal brain cultures and U373MG cells was restricted by the low activities of kynurenine 3-hydroxylase, kynureninase and 3-hydroxyanthranilate 3,4-dioxygenase, and only small amounts of quinolinate were synthesized when cultures were supplied with L-tryptophan or 3-hydroxyanthranilate. In MRC-9 cells, quinolinate was produced only from 3-hydroxykynurenine and 3-hydroxyanthranilate, consistent with their low kynurenine 3-hydroxylase activity. The results are consistent with the notion that indoleamine 2,3-dioxygenase is an important regulatory enzyme in the production of L-kynurenine and quinolinate. Kynurenine 3-hydroxylase and, in some cells, kynureninase and 3-hydroxyanthranilate 3,4-dioxygenase are important determinants of whether a cell can make quinolinate.

APA, Harvard, Vancouver, ISO, and other styles

30

Rotondo, A., K. E. Schuebel, D. A. Nielsen, S. Michelini, A. Lezza, E. Coli, S. Bouanani, et al. "Tryptophan hydroxylase promoter polymorphisms and anorexia nervosa." Biological Psychiatry 42, no. 1 (July 1997): 99S. http://dx.doi.org/10.1016/s0006-3223(97)87285-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Kuhn, Donald M., and Timothy J. Geddes. "Peroxynitrite Inactivates Tryptophan Hydroxylase via Sulfhydryl Oxidation." Journal of Biological Chemistry 274, no. 42 (October 15, 1999): 29726–32. http://dx.doi.org/10.1074/jbc.274.42.29726.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Slominski, Andrzej, Alexander Pisarchik, Olle Johansson, Chen Jing, Igor Semak, George Slugocki, and Jacobo Wortsman. "Tryptophan hydroxylase expression in human skin cells." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1639, no. 2 (October 2003): 80–86. http://dx.doi.org/10.1016/s0925-4439(03)00124-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Mockus, Susan M., Sean C. Kumer, and Kent E. Vrana. "Carboxyl terminal deletion analysis of tryptophan hydroxylase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1342, no. 2 (October 1997): 132–40. http://dx.doi.org/10.1016/s0167-4838(97)00069-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Popova, Nina K., and Alexander V. Kulikov. "Targeting tryptophan hydroxylase 2 in affective disorder." Expert Opinion on Therapeutic Targets 14, no. 11 (September 29, 2010): 1259–71. http://dx.doi.org/10.1517/14728222.2010.524208.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Abbar, M., P. Courtet, F. Bellivier, M. Leboyer, J. P. Boulenger, D. Castelhau, M. Ferreira, et al. "Suicide attempts and the tryptophan hydroxylase gene." Molecular Psychiatry 6, no. 3 (April 27, 2001): 268–73. http://dx.doi.org/10.1038/sj.mp.4000846.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Boularand, Sylviane, Michèle C. Darmon, Yves Ganem, Jean-Marie Launay, and Jacques Mallet. "Complete coding sequence of human tryptophan hydroxylase." Nucleic Acids Research 18, no. 14 (1990): 4257. http://dx.doi.org/10.1093/nar/18.14.4257.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Lerman, Caryn, Neil E. Caporaso, Angelita Bush, Yun-Ling Zheng, Janet Audrain, David Main, and Peter G. Shields. "Tryptophan hydroxylase gene variant and smoking behavior." American Journal of Medical Genetics 105, no. 6 (2001): 518–20. http://dx.doi.org/10.1002/ajmg.1476.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Abbar, Mocrane. "Suicidal Behaviors and the Tryptophan Hydroxylase Gene." Archives of General Psychiatry 52, no. 10 (October 1, 1995): 846. http://dx.doi.org/10.1001/archpsyc.1995.03950220056011.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Kirov, George, Michael J. Owen, Ian Jones, Fiona McCandless, and Nick Craddock. "Tryptophan Hydroxylase Gene and Manic-Depressive Illness." Archives of General Psychiatry 56, no. 1 (January 1, 1999): 98. http://dx.doi.org/10.1001/archpsyc.56.1.98.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Moran, Graham R., Agnes Derecskei-Kovacs, Patrick J. Hillas, and Paul F. Fitzpatrick. "On the Catalytic Mechanism of Tryptophan Hydroxylase." Journal of the American Chemical Society 122, no. 19 (May 2000): 4535–41. http://dx.doi.org/10.1021/ja994479a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Rahman, Md Saydur, Izhar A. Khan, and Peter Thomas. "Tryptophan Hydroxylase: A Target for Neuroendocrine Disruption." Journal of Toxicology and Environmental Health, Part B 14, no. 5-7 (July 2011): 473–94. http://dx.doi.org/10.1080/10937404.2011.578563.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Zhang, X. "Tryptophan Hydroxylase-2 Controls Brain Serotonin Synthesis." Science 305, no. 5681 (July 9, 2004): 217. http://dx.doi.org/10.1126/science.1097540.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Reed, Grant E., Jeffrey E. Kirchner, and Lucinda G. Carr. "NF-Y activates mouse tryptophan hydroxylase transcription." Brain Research 682, no. 1-2 (June 1995): 1–12. http://dx.doi.org/10.1016/0006-8993(95)00284-w.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Moran, Graham R., and Paul F. Fitzpatrick. "A Continuous Fluorescence Assay for Tryptophan Hydroxylase." Analytical Biochemistry 266, no. 1 (January 1999): 148–52. http://dx.doi.org/10.1006/abio.1998.2956.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Calvo, Ana C., Tanja Scherer, Angel L. Pey, Ming Ying, Ingeborg Winge, Jeffrey McKinney, Jan Haavik, Beat Thöny, and Aurora Martinez. "Effect of pharmacological chaperones on brain tyrosine hydroxylase and tryptophan hydroxylase 2." Journal of Neurochemistry 114, no. 3 (June 11, 2010): 853–63. http://dx.doi.org/10.1111/j.1471-4159.2010.06821.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Rocha, Felipe Filardi da, Nathália Bueno Alvarenga, Naira Vassalo Lage, Marco Aurélio Romano-Silva, Luiz Armando de Marco, and Humberto Corrêa. "Associations between polymorphic variants of the tryptophan hydroxylase 2 gene and obsessive-compulsive disorder." Revista Brasileira de Psiquiatria 33, no. 2 (March 11, 2011): 176–80. http://dx.doi.org/10.1590/s1516-44462011005000003.

Full text

Abstract:

OBJECTIVE: A substantial body of evidence suggests that obsessive-compulsive disorder has a genetic component, and substantial candidate genes for the disorder have been investigated through association analyses. A particular emphasis has been placed on genes related to the serotonergic system, which is likely to play an important role in the pathogenesis of obsessive-compulsive disorder. The gene for tryptophan hydroxylase 2, which is a rate limiting enzyme in serotonin synthesis is considered an important candidate gene associated with psychiatric disorders. METHOD: Our sample consisted of 321 subjects (107 diagnosed with obsessive-compulsive disorder and 214 healthy controls), which were genotyped for eight tagSNPs (rs4448731, rs4565946, rs11179000, rs7955501, rs10506645, rs4760820, rs1487275 and rs10879357) covering the entire human tryptophan hydroxylase 2 gene. Statistical analyses were performed using UNPHASED, version 3.0.12, and Haploview ((R)). RESULTS: Single markers, genotype analysis did not show a significant genetic association with obsessive-compulsive disorder. A significant association between the T-C-T (rs4448731, rs4565946, rs10506645) and C-A-T (rs4565946, rs7955501, rs10506645) haplotypes and obsessive-compulsive disorder was observed, as well as a strong linkage disequilibrium between SNPs rs4448731 and rs4565946, and SNPs rs10506645 and 4760820. DISCUSSION: Our research has not demonstrated the existence of associations between the eight SNPs of TPH2 and obsessive-compulsive disorder. However, two LD and two haplotypes areas were demonstrated, thus suggesting that more studies in TPH2 are needed to investigate the role of tryptophan hydroxylase 2 variants in obsessive-compulsive disorder.

APA, Harvard, Vancouver, ISO, and other styles

47

Hernández-Hernández, Olivia Tania, Lucía Martínez-Mota, José Jaime Herrera-Pérez, and Graciela Jiménez-Rubio. "Role of Estradiol in the Expression of Genes Involved in Serotonin Neurotransmission: Implications for Female Depression." Current Neuropharmacology 17, no. 5 (April 5, 2019): 459–71. http://dx.doi.org/10.2174/1570159x16666180628165107.

Full text

Abstract:

Background:In women, changes in estrogen levels may increase the incidence and/or symptomatology of depression and affect the response to antidepressant treatments. Estrogen therapy in females may provide some mood benefits as a single treatment or might augment clinical response to antidepressants that inhibit serotonin reuptake.Objective:We analyzed the mechanisms of estradiol action involved in the regulation of gene expression that modulates serotonin neurotransmission implicated in depression.Method:Publications were identified by a literature search on PubMed.Results:The participation of estradiol in depression may include regulation of the expression of tryptophan hydroxylase-2, monoamine oxidase A and B, serotonin transporter and serotonin-1A receptor. This effect is mediated by estradiol binding to intracellular estrogen receptor that interacts with estrogen response elements in the promoter sequences of tryptophan hydroxylase-2, serotonin transporter and monoamine oxidase-B. In addition to directly binding deoxyribonucleic acid, estrogen receptor can tether to other transcription factors, including activator protein 1, specificity protein 1, CCAAT/enhancer binding protein β and nuclear factor kappa B to regulate gene promoters that lack estrogen response elements, such as monoamine oxidase-A and serotonin 1A receptor.Conclusion:Estradiol increases tryptophan hydroxylase-2 and serotonin transporter expression and decreases the expression of serotonin 1A receptor and monoamine oxidase A and B through the interaction with its intracellular receptors. The understanding of molecular mechanisms of estradiol regulation on the protein expression that modulates serotonin neurotransmission will be helpful for the development of new and more effective treatment for women with depression.

APA, Harvard, Vancouver, ISO, and other styles

48

Salter, M., R. G. Knowles, and C. I. Pogson. "Quantification of the importance of individual steps in the control of aromatic amino acid metabolism." Biochemical Journal 234, no. 3 (March 15, 1986): 635–47. http://dx.doi.org/10.1042/bj2340635.

Full text

Abstract:

The quantitative importance of the individual steps of aromatic amino acid metabolism in rat liver was determined by calculation of the respective Control Coefficients (Strengths). The Control Coefficient of tryptophan 2,3-dioxygenase for tryptophan degradation was determined in a variety of physiological conditions and with a range of activities of tryptophan 2,3-dioxygenase. The Control Coefficient varied from 0.75 with basal enzyme activity to 0.25 after maximal induction of the enzyme by dexamethasone. The remainder of the control for tryptophan degradation was associated with the transport of the amino acid across the plasma membrane, with only very small contributions from kynureninase and kynurenine hydroxylase. The Control Coefficients of tyrosine aminotransferase for tyrosine degradation were approx. 0.70 and 0.20 with basal and dexamethasone-induced tyrosine aminotransferase activities respectively; the Control Coefficients of the transport of the amino acid into the cell were 0.22 and 0.58 respectively. Phenylalanine hydroxylase was found to have a Control Coefficient for the degradation of phenylalanine of approx. 0.50 under conditions of basal enzyme activity; after maximal activation by glucagon, the Control Coefficient decreased to 0.12. The transport of phenylalanine was responsible for the remaining control in the pathway. These results have important implications, directly for the regulation of aromatic amino acid metabolism in the liver, and indirectly for the regulation of neuroamine synthesis in the brain.

APA, Harvard, Vancouver, ISO, and other styles

49

Neckameyer, W. S., and K. White. "A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila." Journal of Biological Chemistry 267, no. 6 (February 1992): 4199–206. http://dx.doi.org/10.1016/s0021-9258(19)50648-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Hirata, Y., M. Sawada, M. Minami, H. Arai, R. Iizuka, and T. Nagatsu. "Tyrosine hydroxylase, tryptophan hydroxylase, biopterin, and neopterin in the brain of anorexia nervosa." Journal of Neural Transmission 80, no. 2 (June 1990): 145–50. http://dx.doi.org/10.1007/bf01257079.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!