Methionine sulfoxide reductase regulates brain catechol-O-methyl transferase activity

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Methionine sulfoxide reductase regulates brain catechol-O-methyl transferase activity.

Catechol-O-methyl transferase (COMT) plays a key role in the degradation of brain dopamine (DA). Specifically, low COMT activity results in higher DA levels in the prefrontal cortex (PFC), thereby reducing the vulnerability for attentional and cognitive deficits in both psychotic and healthy individuals. COMT activity is markedly reduced by a non-synonymous single-nucleotide polymorphism (SNP) ...

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Catechol-O-methyl transferase (COMT) is an enzyme involved in the degradation of dopamine. The most commonly examined polymorphism within the COMT gene is Val108/158Met polymorphism, which results in three to fourfold difference in COMT enzyme activity. It is particularely important in prefrontal cortex, since COMT activity is the most important regulator of the prefrontal dopamine function. Gi...

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Catechol-o-methyl Transferase and Monoamine Oxidase Activity in the Ocular Tissues of Albino Rabbits.

The distribution of catechol-O-methyl transferase and monoamine oxidase activity in the ocular tissues of albino rabbits has been determined with a radioactive tracer assay. The distribution of the former varied in the different tissues within a restricted range whereas the distribution of monoamine oxidase activity exhibited larger variations. Sympathetic denervation did not appear to affect c...

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Selenium and the methionine sulfoxide reductase system.

Selenium is a chemical element participating in the synthesis of selenocysteine residues that play a pivotal role in the enzymatic activity efficiency of selenoproteines. The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, resp...

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Methionine sulfoxide reductase A is a stereospecific methionine oxidase.

Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide. The enzyme participates in defense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methionine. Because oxidation of methionine residues is reversible, this covalent modification could also functio...

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ژورنال

عنوان ژورنال: The International Journal of Neuropsychopharmacology

سال: 2014

ISSN: 1461-1457,1469-5111

DOI: 10.1017/s1461145714000467