Immunohistochemical demonstration of catechol-O-methyltransferase in mammalian brain

Kaplan, G; Hartman, Boyd K.; Creveling, Cyrus R.

doi:10.1016/0006-8993(79)90819-9

Cited by 136 publications

(57 citation statements)

References 25 publications

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“…This observation is in agreement with biochemical evidence that liver is the richest source of catecholestrogen (6,11,16,20,21). It is very interesting to note that catechol-0-methyltransferase (COMT) has been shown to be present in rat liver immunocytochemically (13,15) and that the liver also contains estrogen-2-hydroxylase, the biosynthesistic enzymes of catecholestrogen (5,11,19). Catecholestrogen is rapidly 0-methylated to 2-methoxyestrogen by COMT (8).…”

Section: Discussionsupporting

confidence: 80%

Immunocytochemical localization of catecholestrogen in the rat liver after using various fixatives.

Inoue

Yoshizawa

1985

Acta Histochem. Cytochem

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Section: Discussionsupporting

confidence: 80%

Immunocytochemical localization of catecholestrogen in the rat liver after using various fixatives.

Inoue

Yoshizawa

1985

Acta Histochem. Cytochem

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“…Since COMT proteins have been detected exclusively in the neuropil of the cerebral cortex (Kaplan et al, 1979;Karhunen et al, 1994;Lundstrom et al, 1995) and neurons are the primary cell population producing COMT mRNA, it is reasonable to assume that COMT is located at dendrites and/or spines in the prefrontal cortex (Matsumoto et al, 2003). Interestingly, the prefrontal cortex of patients with schizophrenia has been reported to show reduced cortical neuropil, particularly in layer II , and decreased somal size of pyramidal neurons in layer III (Pierri et al, 2001;Rajkowska et al, 1998), both of which could be related to reduced dendritic arborization.…”

Section: Discussionmentioning

confidence: 99%

Catechol O-Methyltransferase (COMT) mRNA Expression in the Dorsolateral Prefrontal Cortex of Patients with Schizophrenia

Matsumoto

Weickert

Beltaifa

et al. 2003

Neuropsychopharmacol

126

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Human prefrontal cortical neurons express catechol O-methyltransferase (COMT), an enzyme that inactivates the neurotransmitter dopamine. A functional polymorphism of COMT, Val 108/158 Met, affects prefrontal function, and the high-activity Val allele has been reported to be a genetic risk factor for schizophrenia. We used in situ hybridization histochemistry to measure mRNA levels of COMT in the dorsolateral prefrontal cortex (DLPFC) of patients with schizophrenia (N ¼ 14) and of normal controls (N ¼ 15). While the groups did not differ in terms of mean level of COMT mRNA, there was a significantly different laminar pattern of COMT mRNA expression in pyramidal neurons (F ¼ 2.68, df ¼ 4,108, Po0.04); patients with schizophrenia had relatively lower levels in the superficial (II/III) layers and higher levels in the intermediate/deep (IV/V) layers (Po0.01), while in controls, the expression was homogeneous across layers. Neither the mean level nor the laminar distribution of COMT mRNA was related to the Val 108/158 Met genotype, suggesting that the feedback regulation of mRNA level is not a compensation for the functional effect of the COMT polymorphism. The disease-related laminar difference of COMT expression may be involved in dysregulation of dopamine signaling circuits in the DLPFC of patients with schizophrenia.

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“…Since both catechol-O-methyltransferase (28,29) and MAO-B are present in glial cells that invest the brain capillaries and circumventricular organs, these enzymes may control in part the entrance of circulating biogenic amines into the brain. An additional role for MAO B may be related to the intimate association between astrocytic processes and synaptic terminals.…”

mentioning

confidence: 99%

Immunocytochemical demonstration of monoamine oxidase B in brain astrocytes and serotonergic neurons.

Levitt

Pintar

Breakefield

1982

Proc. Natl. Acad. Sci. U.S.A.

445

214

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An antiserum to monoamine oxidase B (MAO-B) was used to define the distribution of this metabolic enzyme in the adult rat brain immunocytochemically. MAO-B is specifically located in two major central nervous system cell classes, astrocytes and serotonin-containing neurons. Double-immunofluorescence experiments using antisera to glial fibrillary acidic protein and MAO-B showed that both protoplasmic and fibrillary astrocytes throughout the brain contain MAO-B, whereas oligodendrocytes do not contain the enzyme. Areas lacking a blood-brain barrier, such as the specialized circumventricular organs, also contain MAO-B-positive cells. A double-immunofluorescence experiment using antisera to serotonin and MAO-B enabled the positive identification of neurons containing both molecules. The catecholamine-containing neurons of the brain did not contain detectable amounts of MAO-B. The specific distribution of MAO-B (1,2). MAO activity has been subdivided on a pharmacological basis into two types: MAO-A has a higher affinity for the substrates norepinephrine and serotonin (5-HT) and the inhibitor clorgyline, and MAO-B has a higher affinity for the substrates phenylethylamine and benzylamine and the inhibitor deprenyl. Recent biochemical evidence indicates that these activities are mediated by two distinct mitochondrial proteins that have different molecular weights (3-5). Both types of MAO activity can be measured in all CNS regions, but it has been difficult to elucidate the cellular distribution of MAO with current pharmacological and biochemical methods because of the diversity of neuronal and nonneuronal cell types in the brain. By using an antiserum directed against MAO-B and immunocytochemical methods, we have localized MAO-B Immunocytochemistry. Every third section, 10 ,Lm thick, through the entire brain was collected on a gelatin-coated slide and immunostained by using rabbit preimmune serum or antiserum prepared against pure bovine ; unpublished data; MAO-B was obtained from James Salach and Walter Weyler). Sections on slides were incubated for 5 min with 1% sodium borohydride in 0.1 M sodium phosphate (pH 7.2) and then for 3 hr at 370C with either MAO-B antiserum or preimmune serum diluted 1: 100 in a staining buffer of0.45 M NaCl/ 20 mM sodium phosphate, pH 7.4/0.3% Triton X-100/10% normal swine serum. The sections were washed for 30 min with the staining buffer and exposed to rhodamine-conjugated swine anti-rabbit IgG (Dako, Accurate Scientific) diluted 1: 40 in the staining buffer. Sections were washed for 30 min and placed under a coverslip with a glycerol/0. 1 M sodium phosphate, pH 7.2 (3:1), solution. The slides were examined on a Zeiss photomicroscope equipped with epifluorescence and photographed on Kodak Plus-X film using 1-to 2-min exposures. Some tissue sections were processed by using the peroxidaseantiperoxidase procedure (8,9). The cell cultures (see below) were fixed with 4% paraformaldehyde in 0.1 M sodium borate buffer (pH 11.0) for 90 min at 4°C, rinsed extensively, and then st...

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Immunohistochemical demonstration of catechol-O-methyltransferase in mammalian brain

Cited by 136 publications

References 25 publications

Immunocytochemical localization of catecholestrogen in the rat liver after using various fixatives.

Immunocytochemical localization of catecholestrogen in the rat liver after using various fixatives.

Catechol O-Methyltransferase (COMT) mRNA Expression in the Dorsolateral Prefrontal Cortex of Patients with Schizophrenia

Immunocytochemical demonstration of monoamine oxidase B in brain astrocytes and serotonergic neurons.

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