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Pesquisa : D08.811.913.555.500.100 [Categoria DeCS]
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[PMID]:28198154
[Au] Autor:Rajiv C; Sanjita Devi H; Mondal G; Devi SD; Khan ZA; Yumnamcha T; Bharali R; Chattoraj A
[Ad] Endereço:Biological Rhythm Laboratory, Animal Resources Programme, Department of Biotechnology, Institute of Bioresources and Sustainable Development, Imphal, India.
[Ti] Título:Daily and Seasonal Expression Profile of Serum Melatonin and Its Biosynthesizing Enzyme Genes (tph1, aanat1, aanat2, and hiomt) in Pineal Organ and Retina: A Study under Natural Environmental Conditions in a Tropical Carp, Catla catla.
[So] Source:J Exp Zool A Ecol Genet Physiol;325(10):688-700, 2016 Dec.
[Is] ISSN:1932-5231
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The tropical carp Catla catla is gaining importance for the studies of the impact of environmental changes on aquatic animals due to its surface dwelling habitat. To date, no information is available on the transcriptional profile of melatonin biosynthesizing enzyme genes in any tropical carp under either natural or artificial photothermal conditions in pineal and retina. The present study is an attempt to demonstrate the temporal pattern of expression of melatonin biosynthesizing enzyme genes, tryptophan hydroxylase 1 (tph1), arylalkylamine N-acetyltransferase (aanat1 and aanat2), and hydroxyindole-O-methyltransferase (hiomt) collectively and simultaneously in pineal organ and retina in tropical fish, C. catla, on a daily and seasonal basis under natural environmental conditions along with the serum melatonin levels. Depending upon the changes of the natural photothermal conditions, in four phases of an annual cycle, the variation and/or shifting of the rhythm parameters of different melatonin biosynthesizing enzyme genes in these two organs are different. Moreover, relative expression of these genes varies based on tissue and season. The serum melatonin levels correspond to the expression pattern of pineal aanat2 and hiomt. This finding indicates a possible organization of melatonin biosynthesizing enzyme genes with reproductive phases differently in these two photoreceptive organs for maintaining its physiological functions.
[Mh] Termos MeSH primário: Acetilserotonina O-Metiltransferasa/metabolismo
Arilalquilamina N-Acetiltransferase/metabolismo
Carpas/fisiologia
Melatonina/biossíntese
Triptofano Hidroxilase/metabolismo
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/genética
Animais
Arilalquilamina N-Acetiltransferase/genética
Ritmo Circadiano
Meio Ambiente
Regulação Enzimológica da Expressão Gênica/fisiologia
Glândula Pineal/enzimologia
Retina/enzimologia
Estações do Ano
Clima Tropical
Triptofano Hidroxilase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.14.16.4 (Tryptophan Hydroxylase); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1002/jez.2061


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[PMID]:27484733
[Au] Autor:Xu W; Cai SY; Zhang Y; Wang Y; Ahammed GJ; Xia XJ; Shi K; Zhou YH; Yu JQ; Reiter RJ; Zhou J
[Ad] Endereço:Department of Horticulture, Zhejiang University, Hangzhou, China.
[Ti] Título:Melatonin enhances thermotolerance by promoting cellular protein protection in tomato plants.
[So] Source:J Pineal Res;61(4):457-469, 2016 Nov.
[Is] ISSN:1600-079X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Melatonin is a pleiotropic signaling molecule that provides physiological protection against diverse environmental stresses in plants. Nonetheless, the mechanisms for melatonin-mediated thermotolerance remain largely unknown. Here, we report that endogenous melatonin levels increased with a rise in ambient temperature and that peaked at 40°C. Foliar pretreatment with an optimal dose of melatonin (10 µmol/L) or the overexpression of N-acetylserotonin methyltransferase (ASMT) gene effectively ameliorated heat-induced photoinhibition and electrolyte leakage in tomato plants. Both exogenous melatonin treatment and endogenous melatonin manipulation by overexpression of ASMT decreased the levels of insoluble and ubiquitinated proteins, but enhanced the expression of heat-shock proteins (HSPs) to refold denatured and unfolded proteins under heat stress. Meanwhile, melatonin also induced expression of several ATG genes and formation of autophagosomes to degrade aggregated proteins under the same stress. Proteomic profile analyses revealed that protein aggregates for a large number of biological processes accumulated in wild-type plants. However, exogenous melatonin treatment or overexpression of ASMT reduced the accumulation of aggregated proteins. Aggregation responsive proteins such as HSP70 and Rubisco activase were preferentially accumulated and ubiquitinated in wild-type plants under heat stress, while melatonin mitigated heat stress-induced accumulation and ubiquitination of aggregated proteins. These results suggest that melatonin promotes cellular protein protection through induction of HSPs and autophagy to refold or degrade denatured proteins under heat stress in tomato plants.
[Mh] Termos MeSH primário: Resposta ao Choque Térmico/efeitos dos fármacos
Temperatura Alta
Lycopersicon esculentum/metabolismo
Melatonina/farmacologia
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/metabolismo
Proteínas de Choque Térmico HSP70/metabolismo
Ribulose-Bifosfato Carboxilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HSP70 Heat-Shock Proteins); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 4.1.1.39 (Ribulose-Bisphosphate Carboxylase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170330
[Lr] Data última revisão:
170330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160804
[St] Status:MEDLINE
[do] DOI:10.1111/jpi.12359


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[PMID]:27366756
[Au] Autor:Cataldo LR; Mizgier ML; Busso D; Olmos P; Galgani JE; Valenzuela R; Mezzano D; Aranda E; Cortés VA; Santos JL
[Ad] Endereço:Departamento de Nutrición, Diabetes y Metabolismo, Escuela de Medicina, Pontificia Universidad Católica de Chile, 8331150 Santiago, Chile; Facultad de Medicina, Universidad de los Andes, 7620001 Santiago, Chile.
[Ti] Título:Serotonin- and Dopamine-Related Gene Expression in db/db Mice Islets and in MIN6 ß-Cells Treated with Palmitate and Oleate.
[So] Source:J Diabetes Res;2016:3793781, 2016.
[Is] ISSN:2314-6753
[Cp] País de publicação:Egypt
[La] Idioma:eng
[Ab] Resumo:High circulating nonesterified fatty acids (NEFAs) concentration, often reported in diabetes, leads to impaired glucose-stimulated insulin secretion (GSIS) through not yet well-defined mechanisms. Serotonin and dopamine might contribute to NEFA-dependent ß-cell dysfunction, since extracellular signal of these monoamines decreases GSIS. Moreover, palmitate-treated ß-cells may enhance the expression of the serotonin receptor Htr2c, affecting insulin secretion. Additionally, the expression of monoamine-oxidase type B (Maob) seems to be lower in islets from humans and mice with diabetes compared to nondiabetic islets, which may lead to increased monoamine concentrations. We assessed the expression of serotonin- and dopamine-related genes in islets from db/db and wild-type (WT) mice. In addition, the effect of palmitate and oleate on the expression of such genes, 5HT content, and GSIS in MIN6 ß-cell was determined. Lower Maob expression was found in islets from db/db versus WT mice and in MIN6 ß-cells in response to palmitate and oleate treatment compared to vehicle. Reduced 5HT content and impaired GSIS in response to palmitate (-25%; p < 0.0001) and oleate (-43%; p < 0.0001) were detected in MIN6 ß-cells. In conclusion, known defects of GSIS in islets from db/db mice and MIN6 ß-cells treated with NEFAs are accompanied by reduced Maob expression and reduced 5HT content.
[Mh] Termos MeSH primário: Células Secretoras de Insulina/efeitos dos fármacos
Ilhotas Pancreáticas/metabolismo
Transcriptoma/genética
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/efeitos dos fármacos
Acetilserotonina O-Metiltransferasa/genética
Animais
Arilalquilamina N-Acetiltransferase/efeitos dos fármacos
Arilalquilamina N-Acetiltransferase/genética
Catecol O-Metiltransferase/efeitos dos fármacos
Catecol O-Metiltransferase/genética
Linhagem Celular
Dopa Descarboxilase/efeitos dos fármacos
Dopa Descarboxilase/genética
Proteínas da Membrana Plasmática de Transporte de Dopamina/efeitos dos fármacos
Proteínas da Membrana Plasmática de Transporte de Dopamina/genética
Dopamina beta-Hidroxilase/efeitos dos fármacos
Dopamina beta-Hidroxilase/genética
Insulina/metabolismo
Insulina/secreção
Células Secretoras de Insulina/metabolismo
Camundongos
Monoaminoxidase/efeitos dos fármacos
Monoaminoxidase/genética
Ácido Oleico/farmacologia
Ácido Palmítico/farmacologia
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Serotonina/metabolismo
Proteínas da Membrana Plasmática de Transporte de Serotonina/efeitos dos fármacos
Proteínas da Membrana Plasmática de Transporte de Serotonina/genética
Transcriptoma/efeitos dos fármacos
Triptofano Hidroxilase/efeitos dos fármacos
Triptofano Hidroxilase/genética
Tirosina 3-Mono-Oxigenase/efeitos dos fármacos
Tirosina 3-Mono-Oxigenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dopamine Plasma Membrane Transport Proteins); 0 (Insulin); 0 (Serotonin Plasma Membrane Transport Proteins); 0 (Slc6a3 protein, mouse); 0 (Slc6a4 protein, mouse); 2UMI9U37CP (Oleic Acid); 2V16EO95H1 (Palmitic Acid); 333DO1RDJY (Serotonin); EC 1.14.16.2 (Tyrosine 3-Monooxygenase); EC 1.14.16.4 (Tph1 protein, mouse); EC 1.14.16.4 (Tph2 protein, mouse); EC 1.14.16.4 (Tryptophan Hydroxylase); EC 1.14.17.1 (Dopamine beta-Hydroxylase); EC 1.4.3.4 (Monoamine Oxidase); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.1.1.6 (COMT protein, mouse); EC 2.1.1.6 (Catechol O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); EC 4.1.1.- (Dopa Decarboxylase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170609
[Lr] Data última revisão:
170609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160702
[St] Status:MEDLINE
[do] DOI:10.1155/2016/3793781


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[PMID]:27212805
[Au] Autor:Herman AP; Bochenek J; Król K; Krawczynska A; Antushevich H; Pawlina B; Herman A; Romanowicz K; Tomaszewska-Zaremba D
[Ad] Endereço:The Kielanowski Institute of Animal Physiology and Nutrition, Polish Academy of Sciences, Instytucka 3 Street, 05-110 Jablonna, Poland.
[Ti] Título:Central Interleukin-1ß Suppresses the Nocturnal Secretion of Melatonin.
[So] Source:Mediators Inflamm;2016:2589483, 2016.
[Is] ISSN:1466-1861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In vertebrates, numerous processes occur in a rhythmic manner. The hormonal signal reliably reflecting the environmental light conditions is melatonin. Nocturnal melatonin secretion patterns could be disturbed in pathophysiological states, including inflammation, Alzheimer's disease, and depression. All of these states share common elements in their aetiology, including the overexpression of interleukin- (IL-) 1ß in the central nervous system. Therefore, the present study was designed to determine the effect of the central injection of exogenous IL-1ß on melatonin release and on the expression of the enzymes of the melatonin biosynthetic pathway in the pineal gland of ewe. It was found that intracerebroventricular injections of IL-1ß (50 µg/animal) suppressed (P < 0.05) nocturnal melatonin secretion in sheep regardless of the photoperiod. This may have resulted from decreased (P < 0.05) synthesis of the melatonin intermediate serotonin, which may have resulted, at least partially, from a reduced expression of tryptophan hydroxylase. IL-1ß also inhibited (P < 0.05) the expression of the melatonin rhythm enzyme arylalkylamine-N-acetyltransferase and hydroxyindole-O-methyltransferase. However, the ability of IL-1ß to affect the expression of these enzymes was dependent upon the photoperiod. Our study may shed new light on the role of central IL-1ß in the aetiology of disruptions in melatonin secretion.
[Mh] Termos MeSH primário: Interleucina-1beta/farmacologia
Melatonina/secreção
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/metabolismo
Animais
Arilalquilamina N-Acetiltransferase/metabolismo
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Feminino
Fotoperíodo
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Interleukin-1beta); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160524
[St] Status:MEDLINE
[do] DOI:10.1155/2016/2589483


  5 / 448 MEDLINE  
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[PMID]:27179881
[Au] Autor:Khan ZA; Yumnamcha T; Rajiv C; Sanjita Devi H; Mondal G; Devi SD; Bharali R; Chattoraj A
[Ad] Endereço:Biological Rhythm Laboratory, Animal Resources Programme, Institute of Bioresources and Sustainable Development, Department of Biotechnology, Government of India, Takyelpat, Imphal 795 001, Manipur, India.
[Ti] Título:Melatonin biosynthesizing enzyme genes and clock genes in ovary and whole brain of zebrafish (Danio rerio): Differential expression and a possible interplay.
[So] Source:Gen Comp Endocrinol;233:16-31, 2016 Jul 01.
[Is] ISSN:1095-6840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The present study on zebrafish (Danio rerio) is the first attempt to demonstrate the circadian mRNA expression of melatonin biosynthesizing enzyme genes (Tph1a, Aanat1, Aanat2 and Hiomt) and clock associated genes (Bmal1a, Clock1a, Per1b, Per2 and Cry2a) in the ovary with a comparison to whole brain in normal (LD=12h L:12h D) and altered photic conditions (continuous dark, DD; continuous light, LL). Moreover, the present study also confirmed the ability of zebrafish ovary to biosynthesize melatonin both in vivo and in vitro with a significant difference at day and night. qRT-PCR analysis of genes revealed a dark acrophase of Aanat2 in both organs while Tph1 is in whole brain in LD condition. On the contrary, Bmal1a and Clock1a giving their peak in light, thereby showing a negative correlation with Tph1a and Aanat2. In LD-ovary, the acrophase of Tph1a, Bmal1a and Clock1a is in light and thus display a positive correlation. This trend of relationship in respect to Tph1a is not changing in altered photic conditions in both organs (except in DD-ovary). On the other hand this association for Aanat2 is varying in ovary under altered photic conditions but only in DD-whole brain. Both in LD and LL the expression of Aanat2 in brain presenting an opposite acrophase with both Bmal1a and Clock1a of ovary and consequently displaying a strong negative correlation among them. Interestingly, all ovarian clock associated genes become totally arrhythmic in DD, representing a loss of correlation between the melatonin synthesizing genes in brain and clock associated genes in ovary. The result is also indicating the formation of two heterodimers namely Clock1a:Bmal1a and Per2:Cry2a in the functioning of clock genes in both organs, irrespective of photic conditions, as they are exhibiting a strong significant positive correlation. Collectively, our data suggest that ovary of zebrafish is working as peripheral oscillator having its own melatonin biosynthesizing machinery and signifying a possible correlation with central oscillating system in various photic conditions.
[Mh] Termos MeSH primário: Encéfalo/enzimologia
Encéfalo/metabolismo
Proteínas CLOCK/genética
Melatonina/biossíntese
Ovário/enzimologia
Ovário/metabolismo
Peixe-Zebra
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/genética
Acetilserotonina O-Metiltransferasa/metabolismo
Animais
Arilalquilamina N-Acetiltransferase/genética
Arilalquilamina N-Acetiltransferase/metabolismo
Ritmo Circadiano/genética
Feminino
Perfilação da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Luz
Masculino
Redes e Vias Metabólicas/genética
Triptofano Hidroxilase/genética
Triptofano Hidroxilase/metabolismo
Peixe-Zebra/genética
Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.14.16.4 (Tryptophan Hydroxylase); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.48 (CLOCK Proteins); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160516
[St] Status:MEDLINE


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[PMID]:26950199
[Au] Autor:Rath MF; Coon SL; Amaral FG; Weller JL; Møller M; Klein DC
[Ad] Endereço:Department of Neuroscience and Pharmacology (M.F.R., M.M.), Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark; and Section on Neuroendocrinology (M.F.R., S.L.C., F.G.A., J.L.W., D.C.K.), Program in Developmental Endocrinology and Genetics, Eunice Kennedy S
[Ti] Título:Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is Strongly Expressed in a Subpopulation of Pinealocytes in the Male Rat Pineal Gland.
[So] Source:Endocrinology;157(5):2028-40, 2016 May.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The rat pineal gland has been extensively used in studies of melatonin synthesis. However, the cellular localization of melatonin synthesis in this species has not been investigated. Here we focus on the localization of melatonin synthesis using immunohistochemical methods to detect the last enzyme in melatonin synthesis, acetylserotonin O-methyltransferase (ASMT), and in situ hybridization techniques to study transcripts encoding ASMT and two other enzymes in melatonin synthesis, tryptophan hydroxylase (TPH)-1 and aralkylamine N-acetyltransferase. In sections of the rat pineal gland, marked cell-to-cell differences were found in ASMT immunostaining intensity and in the abundance of Tph1, Aanat, and Asmt transcripts. ASMT immunoreactivity was localized to the cytoplasm in pinealocytes in the parenchyma of the superficial pineal gland, and immunopositive pinealocytes were also detected in the pineal stalk and in the deep pineal gland. ASMT was found to inconsistently colocalize with S-antigen, a widely used pinealocyte marker; this colocalization was seen in cells throughout the pineal complex and also in displaced pinealocyte-like cells of the medial habenular nucleus. Inconsistent colocalization between ASMT and TPH protein was also detected in the pineal gland. ASMT protein was not detected in extraepithalamic parts of the central nervous system or in peripheral tissues. The findings in this report are of special interest because they provide reason to suspect that melatonin synthesis varies significantly among individual pinealocytes.
[Mh] Termos MeSH primário: Acetilserotonina O-Metiltransferasa/metabolismo
Melatonina/biossíntese
Glândula Pineal/metabolismo
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/genética
Animais
Arilalquilamina N-Acetiltransferase/genética
Arilalquilamina N-Acetiltransferase/metabolismo
Imuno-Histoquímica
Masculino
Glândula Pineal/citologia
Ratos
Ratos Sprague-Dawley
Triptofano Hidroxilase/genética
Triptofano Hidroxilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.14.16.4 (Tryptophan Hydroxylase); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160308
[St] Status:MEDLINE
[do] DOI:10.1210/en.2015-1888


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[PMID]:26919041
[Au] Autor:Byeon Y; Back K
[Ad] Endereço:Department of Biotechnology, Bioenergy Research Center, College of Agriculture and Life Sciences, Chonnam National University, Gwangju, South Korea.
[Ti] Título:Low melatonin production by suppression of either serotonin N-acetyltransferase or N-acetylserotonin methyltransferase in rice causes seedling growth retardation with yield penalty, abiotic stress susceptibility, and enhanced coleoptile growth under anoxic conditions.
[So] Source:J Pineal Res;60(3):348-59, 2016 Apr.
[Is] ISSN:1600-079X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Serotonin N-acetyltransferase (SNAT) and N-acetylserotonin methyltransferase (ASMT) are the last two key enzymes for melatonin biosynthesis in living organisms. In this study, we demonstrated that transgenic rice (Oryza sativa L.) plants, in which expression of either endogenous SNAT or ASMT was suppressed, had reduced melatonin synthesis, confirming that both SNAT and ASMT are functionally involved in melatonin synthesis. The melatonin-deficient SNAT rice had retarded seedling growth, which was partially restored by exogenous melatonin application, suggesting melatonin's role in seedling growth. In addition, the plants were more sensitive to various abiotic stresses, including salt and cold, compared with the wild type. Melatonin-deficient SNAT rice had increased coleoptile growth under anoxic conditions, indicating that melatonin also inversely regulates plant growth under anaerobic conditions with the concomitant high expression of alcohol dehydrogenase genes. Similarly, the melatonin-deficient ASMT rice exhibited accelerated senescence in detached flag leaves, as well as significantly reduced yield. These loss-of-function studies on the melatonin biosynthetic genes confirmed most previous pharmacological reports that melatonin not only promotes plant growth but also mitigates various abiotic stresses.
[Mh] Termos MeSH primário: Acetilserotonina O-Metiltransferasa/metabolismo
Arilalquilamina N-Acetiltransferase/metabolismo
Cotilédone/crescimento & desenvolvimento
Melatonina/metabolismo
Oryza/metabolismo
Proteínas de Plantas/metabolismo
Plântulas/crescimento & desenvolvimento
Estresse Fisiológico
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/genética
Arilalquilamina N-Acetiltransferase/genética
Cotilédone/genética
Melatonina/genética
Oryza/genética
Proteínas de Plantas/genética
Plântulas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160227
[St] Status:MEDLINE
[do] DOI:10.1111/jpi.12317


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[PMID]:26873742
[Au] Autor:Muñoz-Pérez JL; López-Patiño MA; Álvarez-Otero R; Gesto M; Soengas JL; Míguez JM
[Ad] Endereço:Laboratorio de Fisioloxía Animal, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, 36310, Vigo, Spain.
[Ti] Título:Characterization of melatonin synthesis in the gastrointestinal tract of rainbow trout (Oncorhynchus mykiss): distribution, relation with serotonin, daily rhythms and photoperiod regulation.
[So] Source:J Comp Physiol B;186(4):471-84, 2016 May.
[Is] ISSN:1432-136X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Melatonin is synthesized in peripheral locations of vertebrates, including the gastrointestinal tract (GIT). In teleost, information regarding this topic is scarce. Here we studied the presence and synthesis of melatonin at the rainbow trout GIT. Different sections of trout GIT (from esophagus to hindgut) were dissected out and assayed for contents of melatonin, serotonin (5-HT) and its metabolite, 5-hydroxyindole acetic acid, as well as for aanat1, aanat2 and hiomt mRNA abundance. A trout group was pinealectomized to evaluate changes in plasma and gut melatonin content. Finally, the daily profile of melatonin and 5-HT content, and aanat1, aanat2 and hiomt mRNA abundance were analyzed in gut of trout kept under normal lighting, and then under constant darkness. Melatonin was detected in all GIT regions with higher concentrations in the muscular wall than in the mucosa, a similar trend to that of 5-HT. In contrast, transcripts of melatonin synthesis enzymes were more abundant in the mucosa. Pinealectomy did not affect melatonin levels in midgut and hindgut either at day or at night. Additionally, no daily rhythms could be defined for melatonin content in gut tissues but increases during late light phase and at midnight occurred. However, aanat1, aanat2 and hiomt mRNA abundance showed clear daily rhythms with peaks at night. These rhythms remained with a 3-h phase advanced peak in fish exposed to constant darkness. Our results provide clear evidence for a local synthesis of melatonin in trout GIT that might be influenced by the content of 5-HT in the tissue. The process is affected by environmental light cycle and is likely to be under circadian regulation.
[Mh] Termos MeSH primário: Trato Gastrointestinal/metabolismo
Melatonina/biossíntese
Oncorhynchus mykiss/metabolismo
Fotoperíodo
Serotonina/metabolismo
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/genética
Acetilserotonina O-Metiltransferasa/metabolismo
Animais
Arilalquilamina N-Acetiltransferase/genética
Arilalquilamina N-Acetiltransferase/metabolismo
Escuridão
Proteínas de Peixes/genética
Proteínas de Peixes/metabolismo
Trato Gastrointestinal/fisiologia
Regulação Enzimológica da Expressão Gênica
Melatonina/sangue
Melatonina/metabolismo
Oncorhynchus mykiss/fisiologia
Glândula Pineal/metabolismo
Glândula Pineal/cirurgia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fish Proteins); 333DO1RDJY (Serotonin); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160214
[St] Status:MEDLINE
[do] DOI:10.1007/s00360-016-0966-4


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[PMID]:26742835
[Au] Autor:Gonzalez-Arto M; Hamilton TR; Gallego M; Gaspar-Torrubia E; Aguilar D; Serrano-Blesa E; Abecia JA; Pérez-Pé R; Muiño-Blanco T; Cebrián-Pérez JA; Casao A
[Ad] Endereço:Grupo Biología y Fisiología de la Reproducción, Facultad de Veterinaria, Instituto de Investigación de Ciencias Ambientales de Aragón (IUCA), Universidad de Zaragoza, Zaragoza, Spain.
[Ti] Título:Evidence of melatonin synthesis in the ram reproductive tract.
[So] Source:Andrology;4(1):163-71, 2016 Jan.
[Is] ISSN:2047-2927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Melatonin is a ubiquitous molecule found in a wide range of fluids, one of them being ram seminal plasma, in which it can reach higher concentrations than those found in blood, suggesting an extrapineal secretion by the reproductive tract. In order to identify the source of the melatonin found in ram seminal plasma, we first tried to determine whether the melatonin levels were maintained during the day. For this purpose, melatonin concentrations were measured in seminal plasma obtained from first ejaculates of six rams at 6:00 a.m. in total darkness, at 10:00 a.m. and at 14:00 p.m. The melatonin concentration was higher (p < 0.05) in ejaculates collected at 6:00 a.m. than at 10:00 and 14:00. There was no statistical difference between the latter. To further corroborate an extrapineal secretion of melatonin, the presence of the two key enzymes involved in melatonin synthesis, arylalkylamine-N-acetyltransferase (AANAT) and N-acetylserotonin-O-methyltransferase (ASMT) was analyzed by RT-PCR, q-PCR and Western-blot in ram testes, epididymis, and accessory glands. The RT-PCR showed the presence of the m-RNA codifying both AANAT and ASTM in all the tissues under study, but the q-PCR and Western-blot revealed that gene expression of these enzymes was significantly higher in the testis (p < 0.05). Immunohistochemistry confirmed the presence of AANAT and ASMT in the testis and revealed that they were found in the Leydig cells, spermatocytes, and spermatids. Also, measurable levels of melatonin were found in testicular tissue and the tail of the epididymis. In conclusion, our study indicates that the testes are one of the likely sources of the high levels of melatonin found in ram seminal plasma, at least during the day.
[Mh] Termos MeSH primário: Acetilserotonina O-Metiltransferasa/metabolismo
Arilalquilamina N-Acetiltransferase/metabolismo
Epididimo/metabolismo
Melatonina/metabolismo
Sêmen/metabolismo
Testículo/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Intersticiais do Testículo/metabolismo
Masculino
Melatonina/biossíntese
Ovinos
Espermátides/metabolismo
Espermatócitos/metabolismo
Testículo/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase); JL5DK93RCL (Melatonin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161231
[Lr] Data última revisão:
161231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160109
[St] Status:MEDLINE
[do] DOI:10.1111/andr.12117


  10 / 448 MEDLINE  
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[PMID]:26732366
[Au] Autor:Souza-Teodoro LH; Dargenio-Garcia L; Petrilli-Lapa CL; Souza Eda S; Fernandes PA; Markus RP; Ferreira ZS
[Ad] Endereço:Laboratory of Chronopharmacology, Biosciences Institute, University of São Paulo, São Paulo, Brazil.
[Ti] Título:Adenosine triphosphate inhibits melatonin synthesis in the rat pineal gland.
[So] Source:J Pineal Res;60(2):242-9, 2016 Mar.
[Is] ISSN:1600-079X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Adenosine triphosphate (ATP) is released onto the pinealocyte, along with noradrenaline, from sympathetic neurons and triggers P2Y1 receptors that enhance ß-adrenergic-induced N-acetylserotonin (NAS) synthesis. Nevertheless, the biotransformation of NAS into melatonin, which occurs due to the subsequent methylation by acetylserotonin O-methyltransferase (ASMT; EC 2.1.1.4), has not yet been evaluated in the presence of purinergic stimulation. We therefore evaluated the effects of purinergic signaling on melatonin synthesis induced by ß-adrenergic stimulation. ATP increased NAS levels, but, surprisingly, inhibited melatonin synthesis in an inverse, concentration-dependent manner. Our results demonstrate that enhanced NAS levels, which depend on phospholipase C (PLC) activity (but not the induction of gene transcription), are a post-translational effect. By contrast, melatonin reduction is related to an ASMT inhibition of expression at both the gene transcription and protein levels. These results were independent of nuclear factor-kappa B (NF-kB) translocation. Neither the P2Y1 receptor activation nor the PLC-mediated pathway was involved in the decrease in melatonin, indicating that ATP regulates pineal metabolism through different mechanisms. Taken together, our data demonstrate that purinergic signaling differentially modulates NAS and melatonin synthesis and point to a regulatory role for ATP as a cotransmitter in the control of ASMT, the rate-limiting enzyme in melatonin synthesis. The endogenous production of melatonin regulates defense responses; therefore, understanding the mechanisms involving ASMT regulation might provide novel insights into the development and progression of neurological disorders since melatonin presents anti-inflammatory, neuroprotective, and neurogenic effects.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/farmacologia
Melatonina/biossíntese
Glândula Pineal/metabolismo
[Mh] Termos MeSH secundário: Acetilserotonina O-Metiltransferasa/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Feminino
Masculino
NF-kappa B/metabolismo
Ratos
Ratos Wistar
Receptores Purinérgicos P2Y1/metabolismo
Serotonina/análogos & derivados
Serotonina/metabolismo
Fosfolipases Tipo C/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NF-kappa B); 0 (Receptors, Purinergic P2Y1); 333DO1RDJY (Serotonin); 8L70Q75FXE (Adenosine Triphosphate); EC 2.1.1.4 (Acetylserotonin O-Methyltransferase); EC 3.1.4.- (Type C Phospholipases); JL5DK93RCL (Melatonin); P4TO3C82WV (N-acetylserotonin)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160107
[St] Status:MEDLINE
[do] DOI:10.1111/jpi.12309



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