COMT (D4N6M) Rabbit mAb #14368

Catechol-O-methyltransferase (COMT) is an intracellular enzyme that catalyzes the O-methylation and inactivation of catecholamine neurotransmitters and hormones, including dopamine, epinephrine, and norepinephrine (1). Two distinct COMT proteins are generated from separate promoters in cells, including a 28 kDa, membrane-bound protein (mb-COMT), and a soluble protein (s-COMT) of 24 kDa (2,3). The soluble s-COMT is the predominant form of COMT found in peripheral organs, while the mb-COMT protein is more abundant in the central nervous system (4,5).
In addition to inactivating endogenous catecholamines, COMT can also inhibit catechol-based drugs used to treat a number of disorders, including Parkinson's disease and schizophrenia. Research studies using COMT inhibitors indicate that these reagents can prolong the bioavailability of psychoactive drugs such as levodopa by preventing O-methylation and subsequent degradation (6). A Val158Met polymorphism in the corresponding COMT gene reduces COMT enzymatic activity and leads to increased cortical dopamine levels (7). Several research studies suggest that this reduced COMT activity is associated with a large number of mental disorders, including schizophrenia, bipolar disorder, attention deficit hyperactivity disorder, obsessive-compulsive disorder, and anorexia nervosa (reviewed in 8).