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The enzymatic activities of brain catechol-O-methyltransferase (COMT) and methionine sulphoxide reductase are correlated in a COMTVal/Metallele-dependent fashion

Authors :
Consuelo Walss-Bass
Dianne A. Cruz
Marco Bortolato
Peter M. Thompson
Jackob Moskovitz
Jenaqua Hairston
Source :
Neuropathology and Applied Neurobiology. 41:941-951
Publication Year :
2015
Publisher :
Wiley, 2015.

Abstract

Aims The enzyme catechol-O-methyl transferase (COMT) plays a primary role in the metabolism of catecholamine neurotransmitters and is implicated in the modulation of cognitive and emotional responses. The best-characterized single nucleotide polymorphism (SNP) of the COMT gene consists of a valine (Val)-to-methionine (Met) substitution at codon 108/158. The Met-containing variant confers a marked reduction in COMT catalytic activity. We recently showed that the activity of recombinant COMT is positively regulated by the enzyme Met sulfoxide reductase (MSR), which counters the oxidation of Met residues of proteins. The current study was designed to assess whether brain COMT activity may be correlated to MSR in an allele-dependent fashion.

Details

ISSN :
03051846
Volume :
41
Database :
OpenAIRE
Journal :
Neuropathology and Applied Neurobiology
Accession number :
edsair.doi...........ad2129b0d639627fb65f32af73d228da