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Acetylserotonin O-methyltransferase

hydroxyindole-O-methyltransferase, HIOMT, Acetylserotonin N-Methyltransferase, ASMT
This gene belongs to the methyltransferase superfamily, and is located in the pseudoautosomal region (PAR) at the end of the short arms of the X and Y chromosomes. The encoded enzyme catalyzes the final reaction in the synthesis of melatonin, and is abundant in the pineal gland. Alternatively spliced transcript variants have been noted for this gene. [provided by RefSeq, Jan 2010] (from NCBI)
Top mentioned proteins: Arylamine N-Acetyltransferase, serotonin N-acetyltransferase, HAD, ACID, STEP
Papers on hydroxyindole-O-methyltransferase
Evidence of melatonin synthesis in the ram reproductive tract.
Casao et al., Zaragoza, Spain. In Andrology, Feb 2016
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.
Adenosine triphosphate (ATP) inhibits melatonin synthesis in the rat pineal gland.
Ferreira et al., São Paulo, Brazil. In J Pineal Res, Feb 2016
Nevertheless, the biotransformation of NAS into melatonin, which occurs due to the subsequent methylation by acetylserotonin O-methyltransferase (ASMT; EC,
Melatonergic system-based two-gene index is prognostic in human gliomas.
Fernandes et al., São Paulo, Brazil. In J Pineal Res, Jan 2016
Using The Cancer Genome Atlas RNAseq data of 351 glioma patients, we designed a predictive model of the content of melatonin in the tumor microenvironment, the ASMT:CYP1B1 index, combining the gene expression levels of melatonin synthesis and metabolism enzymes.
Cloning and functional characterization of the Arabidopsis N-acetylserotonin O-methyltransferase responsible for melatonin synthesis.
Back et al., Kwangju, South Korea. In J Pineal Res, Nov 2015
UNASSIGNED: The N-acetylserotonin O-methyltransferase (ASMT) gene encodes the enzyme that catalyzes the conversion of N-acetylserotonin to melatonin as the last step in melatonin biosynthesis.
Melatonin in the thyroid gland: regulation by thyroid-stimulating hormone and role in thyroglobulin gene expression.
Martin-Lacave et al., Sevilla, Spain. In J Physiol Pharmacol, Oct 2015
Our results show that the key enzymes for melatonin biosynthesis (AANAT and ASMT) are regulated by thyroid-stimulating hormone.
Genetic variations of the melatonin pathway in patients with attention-deficit and hyperactivity disorders.
Bourgeron et al., Paris, France. In J Pineal Res, 2011
Data found a splice site mutation in ASMT (IVS5+2T>C) and one stop mutation in MTNR1A (Y170X) - detected exclusively in patients with ADHD - for which biochemical analyses indicated that they abolish the activity of ASMT and MTNR1A.
Melatonin exerts by an autocrine loop antiproliferative effects in cholangiocarcinoma: its synthesis is reduced favoring cholangiocarcinoma growth.
Alpini et al., Tempe, United States. In Am J Physiol Gastrointest Liver Physiol, 2011
There is dysregulation of the AANAT/ASMT/melatonin --> melatonin receptor axis in cholangiocarcinoma, which inhibited melatonin secretion and subsequently enhanced CCA growth.
Evidence of melatonin synthesis in the cumulus oocyte complexes and its role in enhancing oocyte maturation in vitro in cattle.
Nagai et al., Tsukuba, Japan. In Mol Reprod Dev, 2011
The study revealed that ASMT and MTNR1A genes were expressed in cumulus-oocyte complexes (COCs).
Expression and cellular localizaion of melatonin-synthesizing enzymes in rat and human salivary glands.
Satomura et al., Yokohama, Japan. In Histochem Cell Biol, 2011
The expression of HIOMT in epithelial cells of striated ducts in rat submandibular glands.
Mutation screening of ASMT, the last enzyme of the melatonin pathway, in a large sample of patients with intellectual disability.
Bourgeron et al., Paris, France. In Bmc Med Genet, 2010
study of genetic variability of ASMT in a cohort of patients with intellectual disability (ID)and controls; identifed patients with deleterious ASMT mutations and decreased ASMT activity; however, study does not support ASMT as a causative gene for ID
Role of melatonin in upper gastrointestinal tract.
Bubenik et al., Kraków, Poland. In J Physiol Pharmacol, 2007
The biosynthetic steps of melatonin with two major rate limiting enzymes, arylalkylamine-N-acetyltransferase (AA-NAT) and hydroxyindole-O-methyltransferase (HIOMT), transforming tryptophan to melatonin, originally identified in pinealocytes have been also detected in entero-endocrine (EE) cells of GIT wall, where this indole may act via endocrine, paracrine and/or luminal pathway through G-protein coupled receptors.
Molecular aspects of avian oogenesis and fertilisation.
Stepinska et al., Warsaw, Poland. In Int J Dev Biol, 2007
Melatonin and the two enzymes engaged in its synthesis (AA-NAT and HIOMT) have been found in the egg yolk; their transcripts and the transcripts of the melatonin receptors mel-1a,b and c are present in RNA from the germinal discs.
Localization and biological activities of melatonin in intact and diseased gastrointestinal tract (GIT).
Pawlik et al., Kraków, Poland. In J Physiol Pharmacol, 2007
These biosynthetic steps of MT, including two major rate limiting enzymes; arylalkylamine-N-acetyltransferase (AA-NAT) and hydroxyindole-O-methyltransferase (HIOMT), transforming L-tryptophan (Trp), originally identified in pinealocytes, have been also detected in entero-endocrine (EE) cells of GIT, where this indole appears to act in endocrine, paracrine and/or luminal pathway directly or through G-protein coupled MT receptors.
Melatonin and its metabolites: new findings regarding their production and their radical scavenging actions.
Czarnocki et al., San Antonio, United States. In Acta Biochim Pol, 2006
New evidence from several different laboratories indicates that hydroxyindole-O-methyltransferase, which O-methylates N-acetylserotonin to melatonin may be rate-limiting in some cases.
On the role of melatonin in skin physiology and pathology.
Tobin et al., Memphis, United States. In Endocrine, 2005
Existence of the biosynthetic pathway was confirmed by detection of the corresponding genes and proteins with actual demonstration of enzymatic activities for tryptophan hydroxylase, serotonin N-acetyl-transferase, and hydroxyindole-O-methyltransferase in extracts from skin and skin cells.
Diurnal variation in mRNA encoding serotonin N-acetyltransferase in pineal gland.
Snyder et al., Baltimore, United States. In Nature, 1996
Melatonin is synthesized from serotonin by an initial N-acetylation followed by methylation of the 5-hydroxy moiety by hydroxyindole-O-methyltransferase.
Harderian gland: influence on pineal hydroxyindole-O-methyltransferase activity in neonatal rats.
Wallace et al., In Science, 1970
A circadian rhythm has been found in hydroxyindole-O-methyltransferase activity of the pineal gland of blinded 12-day-old rats.
Visual pathway mediating pineal response to environmental light.
Axelrod et al., In Science, 1967
Activity of the melatoninforming enzyme, hydroxyindole-O-methyltransferase, in rat pineal is increased when the animal is exposed to continuous darkness, and it is decreased by exposure to continuous light.
Light-induced changes in pineal hydroxyindole-O-methyltransferase: abolition by lateral hypothalamic lesions.
Moore et al., In Science, 1966
The activity of hydroxyindole-O-methyltransferase, the melatoninforming enzyme in the pineal gland, is several times greater in rats kept in continuous darkness than in those kept in continuous light.
TAYLOR et al., In Science, 1965
Pineal hydroxyindole-O-methyltransferase, with S-adenosylmethionine, converts 5-hydroxytryptophol to 5-methoxytryptophol.
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