Topographic immunocytochemical mapping of monoamine oxidase-A, monoamine oxidase-B and tyrosine hydroxylase in human post mortem brain stem

C, Konradi; Svoma, E.; Jellinger, K. A.; Riederer, Peter; Denney, Richard M.; Thibault, Jean

doi:10.1016/0306-4522(88)90099-1

Cited by 95 publications

(31 citation statements)

References 29 publications

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“…Similar results, moreover, were obtained immunohistochemically using monoclonal antibodies with human peripheral tissues and brain 1985, 1988Thorpe et al, 1987;Konradi et al, 1988) as well as with rat brain (Levitt et al, 1982). Although the cellular resolution of enzyme radioautography does not compare with that of enzyme histochemistry and immunohistochemistry, it is a quantitative and highly sensitive technique.…”

Section: Discussionsupporting

confidence: 63%

“…However, although the melanin-containing A9 cells appeared to contain more MAO-A than MAO-B, a hybridization signal for neither MAO-A nor MAO-B mRNA could be detected . Enzyme histochemical and immunohistochemical investigations have failed to demonstrate the presence of either enzyme in the majority of A9 cells (Konradi et al, 1988;Westlund et al, 1988;Moll et al, 1990). The functional implications of these findings are currently the subject of much speculation.…”

Section: Distribution and Abundance Of Mao-a And Mao-b In Human Brainmentioning

confidence: 99%

“…Efforts to determine the cellular localization and abundance of the enzymes have, to date, relied on enzyme histochemical and immunohistochemical investigations (Glenner et al, 1957;Graham and Karnovsky, 1965;Levitt et al, 1982;Westlund et al, 1985Arai et al, 1986;Thorpe et al, 1987;Konradi et al, 1988Konradi et al, , 1989Kirchgessner and Pintar, 1991). Although these techniques have revealed the cellular localization of MAO-A and MAO-B, enzyme radioautography using radiolabeled inhibitors as high-affinity substrates offers a highly sensitive and auantitative assay to determine the distribution and abundance of the enzymes in tissue sections of discrete regions of the CNS and peripheral organs.…”

Section: H-ro 19-6327mentioning

confidence: 99%

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Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19- 6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain

et al. 1992

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Monoamine oxidases A and B (MAO-A and MAO-B) oxidatively deaminate neurotransmitter and xenobiotic amines. Since the cellular localization of the isoenzymes in the CNS and peripheral organs determines to a large extent which substrate has access to which isoenzyme, knowledge of their tissue distribution and cellular localization is essential. Here we describe how reversible and selective inhibitors of MAO-A and MAO-B [Ro 41–1049 and Ro 19–6327 (lazabemide), respectively] can be used, as tritiated radioligands, to map the distribution and abundance of the enzymes in microscopic regions of the rat CNS and peripheral organs, and human brain by quantitative enzyme radioautography. The in vitro binding characteristics of both radiolabeled inhibitors revealed them to be selective, high-affinity ligands for the respective enzymes. KD and Bmax values for 3H-Ro 41–1049 in rat cerebral cortex were 10.7 nM and 7.38 pmol/mg protein, respectively, and for 3H-Ro 19–6327 were 18.4 nM and 3.45 pmol/mg protein, respectively. In accordance with their potencies as enzyme inhibitors, binding to MAO-A and MAO-B was competitively inhibited by clorgyline (IC50 = 1.4 nM) and L-deprenyl (selegiline; IC50 = 8.0 nM), respectively. The capacities of various rat and human tissues to bind the radioligands correlated extremely well with their corresponding enzyme activities. As revealed by the respective binding assays, the distribution and abundance of MAO-A and MAO-B in the tissues investigated differed markedly. MAO-A was most abundant in the locus coeruleus, paraventricular thalamus, bed nucleus of the stria terminalis, median habenular nucleus, ventromedial hypothalamus, raphe nuclei, solitary tract nucleus, inferior olives, interpeduncular nucleus, claustrum, and numerous peripheral tissues, including liver, vas deferens, heart, superior cervical ganglion, and exocrine and endocrine pancreas. In contrast, MAO-B was most abundant in the ependyma, circumventricular organs, olfactory nerve layer, periventricular hypothalamus, cingulum, hippocampal formation, raphe nuclei, paraventricular thalamus, mammillary nuclei, cerebellar Bergmann glia cells, liver, posterior pituitary, renal tubules, and endocrine pancreas. The cellular localization of the isoenzymes in both rat and human brain differs markedly and does not reflect the distribution of the presumed natural substrates, for example, absence of MAO-A in serotoninergic neurons. Indeed, the present evidence suggests that, whereas MAO-A is found in noradrenergic and adrenergic neurons, MAO-B occurs in astrocytes, serotoninergic neurons, as well as ventricular cells, including most circumventricular organs. The physiological roles of the enzymes are discussed in the light of these findings, some of which were unexpected.(ABSTRACT TRUNCATED AT 400 WORDS)

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Section: Discussionsupporting

confidence: 63%

Section: Distribution and Abundance Of Mao-a And Mao-b In Human Brainmentioning

confidence: 99%

Section: H-ro 19-6327mentioning

confidence: 99%

See 1 more Smart Citation

Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19- 6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain

et al. 1992

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“…These results are consistent with those previously obtained with the two-step double-labeling localization process (Albanese and Butcher 1979;de la Torre and Surgeon 1976) and with previous studies of the distribution of AChE by enzyme histochemical techniques (Caffe 1994;Ennis and Shipley 1992;Mizukawa et al 1986;Paxinos and Watson 1986;Butcher and Woolf 1984;Mesulam et al 1984;Satoh et al 1983;Albanese and Butcher 1979;Lewis and Schon 1975), and of MAO-A by enzyme histochemical (Kitahama et al 1986(Kitahama et al ,1994Konradi et al 1989;Willoughby et al 1988;Arai et al 1986) and immunohistochemical (Kitahama et al 1994;Konradi et al 1988;Thorpe et al 1987;Westlund et al 1985Westlund et al ,1988Westlund et al ,1993 techniques. The distinct color and nature of the reaction products produced by the present double-labeling technique allow both markers to be simultaneously co-localized within individual neurons.…”

Section: Discussionsupporting

confidence: 82%

A Simple Enzyme Histochemical Method for the Simultaneous Demonstration of Acetylcholinesterase and Monoamine Oxidase in Fixed-Frozen Sections

Dunning

McHaffie

Stein

1997

J Histochem Cytochem.

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SUMMARYWe describe an enzyme histochemical technique for the simultaneous demonstration of acetylcholinesterase (AChE) and monoamine oxidase (MAO) (Types A, B, or A ϩB) in fixed-frozen sections. Several regions in the mesencephalon and brainstem were examined for both somatic and neuropil labeling. The results obtained are equivalent or superior to those obtained using previous methods for the individual localization of these enzymes. The simultaneous visualization of AChE and MAO in the same section allows the relationship of the two enzymes to be easily assessed with brightfield microscopy.

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“…MAO A is found predominantly in the substantia nigra (a region rich in dopaminergic neurons), the locus coeruleus, the striatum, and other areas containing catecholaminergic neurons (36,37). MAO B is expressed at a lower level in the same brain regions as MAO A and is most abundant in the raphe nuclei and glial cells (35,38). MAO A and B differ in their substrate preferences.…”

Section: Gene Expression Is Required For Ngf Withdrawal-induced Apoptmentioning

confidence: 99%

Pro-apoptotic gene expression mediated by the p38 mitogen-activated protein kinase signal transduction pathway

Zutter

Davis

2001

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

116

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Neurotrophic factor deprivation causes apoptosis by a mechanism that requires macromolecular synthesis. This fact suggests that gene expression is necessary to achieve cell death. To identify mRNA that is expressed in apoptotic cells we used subtractive hybridization with cDNA prepared from neuronal pheochromocytoma cells. Monoamine oxidase (MAO) expression was increased in cells during nerve growth factor withdrawal-induced apoptosis. The increased apoptosis and induction of MAO was prevented by inhibition of the p38 mitogen-activated protein (MAP) kinase pathway. MAO may contribute to the apoptotic process because inhibition of MAO activity suppressed cell death. Together, these data indicate that MAO may be a target of pro-apoptotic signal transduction by the p38 MAP kinase pathway.

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Topographic immunocytochemical mapping of monoamine oxidase-A, monoamine oxidase-B and tyrosine hydroxylase in human post mortem brain stem

Cited by 95 publications

References 29 publications

Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19- 6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain

Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19- 6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain

A Simple Enzyme Histochemical Method for the Simultaneous Demonstration of Acetylcholinesterase and Monoamine Oxidase in Fixed-Frozen Sections

Pro-apoptotic gene expression mediated by the p38 mitogen-activated protein kinase signal transduction pathway

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