Monoamine oxidase inhibitor efficacy in depression and the ‘cheese effect’

Sandler, M.

doi:10.1017/s0033291700052764

Cited by 26 publications

(4 citation statements)

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“…The main role of intestinal MAO is the degradation of dietary amines, some of which are potentially toxic, e.g. tyramine (Sandler 1981). This role is played by mucosal MAO and the presence of both MAO-A and MAO-B in these cells might provide a better defence mechanism by covering a broader spectrum of substrates.…”

Section: Discussionmentioning

confidence: 99%

Cellular localization of monoamine oxidase A and B in human tissues outside of the central nervous system

Rodrı́guez

Saura

Billett

et al. 2001

Cell and Tissue Research

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We studied the localization of monoamine oxidase (MAO) A and B in human heart, liver, duodenum, blood vessels and kidney by immunohistochemistry. The primary antibodies used were mouse monoclonal anti-human MAO-A (6G11/E1) and anti-human MAO-B (3F12/G10/2E3). Samples were obtained from six routine autopsy cases and fixed in 2% paraformaldehyde. All cardiomyocytes and hepatocytes showed MAO-A and MAO-B immunoreactivity. In the duodenum, both immunoreactivities were present in all cells of the villi, Lieberkühn crypts, muscularis mucosae and muscular layers, whereas Brunner glands were devoid of MAO-A and MAO-B staining. Endothelial cells of lymphatic vessels showed MAO-A but no MAO-B immunoreactivity, whereas arteries and veins presented MAO-A and MAO-B staining in muscular layers and fibroblasts but not in endothelial cells. In the kidney, renal tubuli showed MAO-A and MAO-B immunoreactivities, whereas collecting ducts and the Bowman's capsule showed only MAO-A staining. These data represent the first study of the cellular distribution of MAO-A and MAO-B in these human tissues. They show that both enzymes have a widespread distribution in the human body with a matching pattern in many, but not all tissues, and with strong differences from the pattern of distribution in rodents.

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Section: Discussionmentioning

confidence: 99%

Cellular localization of monoamine oxidase A and B in human tissues outside of the central nervous system

Rodrı́guez

Saura

Billett

et al. 2001

Cell and Tissue Research

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“…Based on a better understanding of the biochemical and catalytic properties of MAO, recent research efforts have focused on selective and reversible inhibitors of MAO-A or MAO-B. [1][2][3][4][5][6][7][8] Pyridazine derivatives are currently an object of sustained interest due to the vast range of their potential activities as chemotherapeutics, antithrombotics, cardiovascular agents, antisecretory and antiulcer agents, analgetic and antiinflammatory agents, and central nervous system (CNS) stimulants or depressants.910 In a previous paper, we reported the synthesis and activity of a series of novel 5If-indeno[l,2-c]pyridazin-5-ones (IPs) acting as competitive inhibitors of MAO and mainly Such IPs have a structural analogy (the endocyclic N-N functionality) with 2-aryl-l,3,4-oxadiazines and 5-aryl-l,3,4-oxadiazoles which have been described as selective and competitive MAO-B inhibitors.1014 '15 In order to improve the MAO inhibitory activity of IPs and gain an understanding of their structure-activity relationships, we designed, prepared, and tested a large congeneric series of 3-and 4-substituted indeno[l,2-c]pyridazine derivatives. Their synthesis, MAO inhibitory activities, and structureactivity relationships are described in this paper.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Monoamine Oxidase-B by 5H-Indeno[1,2-c]pyridazines: Biological Activities, Quantitative Structure-Activity Relationships (QSARs) and 3D-QSARs

Kneubühler¹,

Thull²,

Altomare³

et al. 1995

J. Med. Chem.

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A large series (66 compounds) of indeno[1,2-c]pyridazin-5-ones (IPs) were synthesized and tested on their monoamine oxidase-A (MAO-A) and MAO-B inhibitory activity. All of the tested compounds acted preferentially on MAO-B displaying weak (nonmeasurable IC50 values) to high (submicromolar IC50 values) activities. The most active compound was p-CF3-3-phenyl-IP (IC50 = 90 nM). Multiple linear regression analysis of the substituted 3-phenyl-IPs yielded good statistical results (q2 = 0.74; r2 = 0.86) and showed the importance of lipophilic, electronic, and steric properties of the substituents in determining inhibitory potency. Various comparative molecular field analysis studies were performed with different alignments and including the molecular lipophilicity potential. This led to a model including the steric, electrostatic and lipophilicity fields and having a good predictive value (q2 = 0.75; r2 = 0.93).

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“…phenelzine (Youdim & Paykel, 1981). This may well be because MAO-A inhibition is necessary for any antidepressant efficacy of MAO inhibitors (Pickar, Cohen, Jimerson, Lake & Murphy, 1981); however, it is also a possibility that facilitated release of NA by tyramine, a central counterpart of the 'cheese effect', is responsible for any therapeutic benefit achieved with these drugs (Sandler, 1981), rather than mere enzyme inhibition as such. Should MAO-A inhibition eventually prove essential, however, it remains to be determined whether the combination of a selective MAO-A or non-selective MAO inhibitor, to-gether with a low dose of (-)-deprenyl, will provide a safe and effective antidepressant.…”

Section: Discussionmentioning

confidence: 99%

Tyramine‐induced noradrenaline release from rat brain slices: prevention by (‐)‐deprenyl

Glover

Pycock

Sandler

1983

British J Pharmacology

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Clorgyline (1 and 10 μM) and (+)‐deprenyl (10 μM) both significantly potentiated the tyramine (100 μM)‐induced release of [3H]‐noradrenaline from rat cerebral cortex slices. (‐)‐Deprenyl (50 μM) significantly reduced it, while lower concentrations had no effect on noradrenaline release. However, in combination, 1 μM (‐)‐deprenyl blocked the release‐facilitating action of 1 μM clorgyline, and 10 μM (‐)‐deprenyl that of 10 μM (+)‐deprenyl. Low concentrations of (+)‐ and (‐)‐deprenyl (1 and 10 μM), both selectively inhibited phenylethylamine oxidation by monoamine oxidase B. Higher concentrations of (‐)‐deprenyl (20 and 50 μM) also inhibited 5‐hydroxytryptamine oxidation by monoamine oxidase A. Clorgyline (1 and 10 μM) inhibited both enzymes. Thus, the effects of these drugs on noradrenaline‐release cannot be explained solely in terms of irreversible inhibition of monoamine oxidase A and B, and other possible mechanisms are discussed. If the brain‐slice model faithfully mirrors the sequence of events manifesting peripherally as the tyramine hypertensive response (‘cheese effect”), then it is possible that low doses of (‐)‐deprenyl, administered with antidepressant monoamine oxidase inhibitors, can prevent this adverse reaction.

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Monoamine oxidase inhibitor efficacy in depression and the ‘cheese effect’

Cited by 26 publications

References 31 publications

Cellular localization of monoamine oxidase A and B in human tissues outside of the central nervous system

Cellular localization of monoamine oxidase A and B in human tissues outside of the central nervous system

Inhibition of Monoamine Oxidase-B by 5H-Indeno[1,2-c]pyridazines: Biological Activities, Quantitative Structure-Activity Relationships (QSARs) and 3D-QSARs

Tyramine‐induced noradrenaline release from rat brain slices: prevention by (‐)‐deprenyl

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