A new type of mitochondrial monamine oxidase distinct from type-A and type-B

Kinemuchi, Hiroyasu; Sudo, Miyuki; Yoshino, Morihiko; Kawaguchi, Takamori; Sunami, Yumi; Kamijo, Keita

doi:10.1016/0024-3205(83)90146-7

Cited by 23 publications

(13 citation statements)

References 17 publications

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“…This MAO may be a classical mitochondrial MAO, presumably with FAD as its prosthetic group, since we also observed time dependent change in its mode of inhibition, which was first reversible and then irreversible, like that of mammalian MAO by clorgyline and deprenyl (6).…”

supporting

confidence: 52%

“…Although able to oxidize various amine substrates of both mammalian MAO-A and MAO-B, it appeared to be distinct from these two forms of MAO because it showed the same sensitivities to the inhibitors clorgyline and deprenyl (6,7). These findings suggested that this MAO might be useful in studies on the genesis of the two forms of mammalian MAO (6,7).…”

Section: Discussionmentioning

confidence: 94%

“…Knoll Carp liver mitochondrial preparation: The livers of carp weighing 900-1,200 g were rapidly removed, blotted on filter paper, weighed and cut into small pieces. Mito chondria in the heavy mitochondrial fractions were isolated by differential centrifugation as described previously (6). Briefly, the livers were promptly homogenized in 9 vol.…”

Section: Methodsmentioning

confidence: 99%

“…However, our recent studies on carp (Cyprinus carpio) liver mitochondria suggest the existence of a single form of MAO with the properties of both forms of mammalian MAO, but differing from both in showing the same sensitivity to clorgyline and deprenyl (6).…”

mentioning

confidence: 99%

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Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.

et al. 1983

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Abstract-The inhibitory effects of some detergents commonly used in biochemical research on carp liver mitochondrial monoamine oxidase were examined. Sodium dodecylsulfate, octyl-(3-D-glucopyranoside, sodium cholate and Triton X-100 at relatively low concentrations caused strong dose-dependent inhibition of the activity towards tyramine, but digitonin caused only weak inhibition. Sodium dodecylsulfate, octyl-Q D-glucopyranoside and sodium cholate caused almost complete inhibition of activity in the concentration ranges tested. The extent of inhibition by Triton X-100 was greater after preincubation at 37'C for 30 min than that without preincubation, but with or without preincubation, the inhibition was not substrate-selective and was not complete at a relatively high concentration (2%) of Triton X-1 00. Without preincubation, the mode of inhibition by Triton X-1 00 was competitive and reversible with respect to the oxidations of 5-HT, tyramine and PEA, but after preincubation (37°C for 30 min), it became non competitive and irreversible, depending on the concentration of detergent used. These findings suggest that it had different actions on the enzyme depending on preincubation. Triton X-100 also slightly changed enzyme sensitivity towards clorgyline and deprenyl, regardless of the preincubation time or the substrate used. Some possible mechanisms of the inhibitory effect of Triton X-100 are discussed. Many tissues of various species examined so far have been shown to contain both forms of MAO in different proportions or only one of these two forms of MAO (4, 5). However, our recent studies on carp (Cyprinus carpio) liver mitochondria suggest the existence of a single form of MAO with the properties of both forms of mammalian MAO, but differing from both in showing the same sensitivity to clorgyline and deprenyl (6).This MAO may be a classical mitochondrial MAO, presumably with FAD as its prosthetic group, since we also observed time dependent change in its mode of inhibition, which was first reversible and then irreversible, like that of mammalian MAO by clorgyline and deprenyl (6).The inhibitory effect of Triton X-100 on MAO activity was noticed during solubili zation of carp liver mitochondrial MAO with this non-ionic detergent (7). In the present study, we examined the inhibitory effects of various commonly used detergents on carp liver mitochondrial MAO. Special attention was paid to the inhibitory effects of Triton X-100.

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supporting

confidence: 52%

Section: Discussionmentioning

confidence: 94%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.

et al. 1983

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“…MAO in carp brain and liver seems to have similar enzymic and molecular characters to those of MAO in various mammals, except that it is equally sensitive to selective inhibitors of MAO-A and -B such as clorgyline and I-deprenyl. Our previous studies showed that the lipidenvironment in carp liver mitochondria probably does not play a role in the identical sensitivities of MAO to clorgyline and Ideprenyl (41). Thus carp brain and liver seem to contain a single MAO, which is apparently neither MAO-A nor MAO-B.…”

Section: Discussionmentioning

confidence: 92%

Enzymic and molecular characteristics of a new form of monoamine oxidase, distinct from form-A and form-B.

et al. 1984

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Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio)

Anichtchik

Sallinen

Peitsaro

et al. 2006

J of Comparative Neurology

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Monoamine oxidase (MAO) is a mitochondrial flavoprotein involved in the metabolism of, e.g., aminergic neurotransmitters and the parkinsonism-inducing neurotoxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine (MPTP). We have reported earlier MPTP-related alterations of brain catecholaminergic system in zebrafish (Danio rerio) brain. Here we describe the structural and functional properties of zebrafish MAO and the distribution of MAO mRNA and activity in zebrafish brain. The gene is located in chromosome 9 and consists of 15 exons. The amino acid composition of the active center resembles both human MAO-A and MAO-B. The enzyme displayed the highest substrate specificity for tyramine, followed by serotonin, phenylethylamine, MPTP, and dopamine; isoform-specific antagonists blocked the activity of the enzyme with equal potency. Zebrafish MAO mRNA, which was present in several tissues, and enzyme displayed differential distribution in the brain; dopaminergic cell clusters had low to moderate levels of MAO activity, whereas the highest levels of MAO activity were detected in noradrenergic and serotonergic cell groups and the habenulointerpeduncular pathway, including its caudal projection to the medial ventral rhombencephalon. The results of this study confirm the presence of functionally active MAO in zebrafish brain and other tissues and characterize the neural systems that express MAO and areas of intense activity in the brain. They also suggest that MPTP toxicity not related to MAO may affect the zebrafish brain.

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A new type of mitochondrial monamine oxidase distinct from type-A and type-B

Cited by 23 publications

References 17 publications

Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.

Inhibition of carp liver mitochondrial monoamine oxidase by some commonly-used detergents.

Enzymic and molecular characteristics of a new form of monoamine oxidase, distinct from form-A and form-B.

Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio)

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