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The COMT Val158Met polymorphism might not be associated with PE in Chinese women.
COMT Val158Met polymorphism plays critical roles in self-related processes, specifically social acceptance.
The assay was established using membranes expressing human membrane-bound COMT and was optimized for protein and time to give an acceptable signal window, good potency for tolcapone, and a high degree of translation between data in fluorescence ratio and data in terms of [SAH (show ACSM3 Proteins)] produced
Study shoes an interaction between COMT Val(158)Met polymorphism and childhood adversity affects reward processing in adulthood. Results identify convergent genetic and environmental effects on reward processing in a prospective study.
COMT gene-linked locus that was associated with premature ejaculation symptoms.
Meta-analysing data results from 11 studies and 7225 subjects show that COMT Val158Met polymorphism is not associated with Eating Disorders.
Results support possible involvement of the COMT (Val(158)-Met) polymorphism in the treatment response to methylphenidate in children with attention-deficit/hyperactivity disorder.
Results showed that genetic variants of COMT modulate the association of age and brain morphology of the dorsal visual pathway and basal ganglia that are dopaminergically rich. Additionally, COMT shows an antagonistic pleiotropy phenomenon that confers a differential impact of COMT on an aging brain.
Our findings indicate that the effects of the COMT genotype on language ability and cortical language processing may change in a narrow age window of 6-10 years.
Study used a data-driven method to search brain regions that showed a significant interaction between COMT rs4680 and BDNF (show BDNF Proteins) rs6265 on the global functional connectivity density in healthy young adults; and repeatedly found a significant COMT x BDNF (show BDNF Proteins) interaction in the left frontal eye field of the dorsal attention network.
Miroestrol restored uterine COMT expression in beta-naphthoflavone-treated mice.
This study report that genetically driven reduction in COMT enzyme activity increased cortical thickness in the prefrontal cortex (PFC (show CFP Proteins)) and postero-parieto-temporal cortex of male, but not female adult mice.
COMT expression in the hippocampus was significantly reduced by high E2 replacement, implying increased catecholamine levels in the hippocampus of high E2 mice.
COMT overexpressing mice display an increase in dopamine release capacity in the striatum, suggesting increased COMT activity may affect dopamine signaling by enhancing synaptic clearance in the cortex and changes in striatal presynaptic dopamine function
These data confirm at the level of mouse working memory and human working memory-associated physiology a genetic interaction between COMT and DTNBP1 (show DTNBP1 Proteins).
The results of this study suggest that individual differences in COMT activity do not affect primary reinforcing effects of cocaine in mice.
Inhibition of COMT via serotonin binding contributes to pain hypersensitivity.
COMT knockout mice were more impulsive compared with wild-type littermates.
Data show that in male catechol-O-methyltransferase COMT(-/-)-mice, the total number of T-, and B-lymphocytes from spleen increased but the T-cell proliferative response decreased.
decreased COMT activity was associated with some changes in feeding microstructure in rats and mice
An analysis of polymorphisms of the COMT gene as a preliminary step in evaluating the role of the gene in behavior is reported.
Catechol-O-methyltransferase catalyzes the transfer of a methyl group from S-adenosylmethionine to catecholamines, including the neurotransmitters dopamine, epinephrine, and norepinephrine. This O-methylation results in one of the major degradative pathways of the catecholamine transmitters. In addition to its role in the metabolism of endogenous substances, COMT is important in the metabolism of catechol drugs used in the treatment of hypertension, asthma, and Parkinson disease. COMT is found in two forms in tissues, a soluble form (S-COMT) and a membrane-bound form (MB-COMT). The differences between S-COMT and MB-COMT reside within the N-termini. Several transcript variants are formed through the use of alternative translation initiation sites and promoters.
, catechol-O-methyltransferase 1
, catechol O-methyltransferase, soluble form
, catechol O-methyltransferase, membrane-bound form