The deamination of monoamines by pig dental pulp

Norqvist, Astrid; Fowler, Christopher J.; Oreland, Lars

doi:10.1016/0006-2952(81)90623-7

Cited by 27 publications

(11 citation statements)

References 28 publications

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“…This activity, which is not sensitive to inhibition by the acetylenic monoamine oxidase inhibitors, has been variously termed benzylamine oxidase,22 clorgyline-resistant amine ~x i d a s e ,~~ or semicarbazide-sensitive amine ~x i d a s e .~~ It has been found in the blood plasma from several species," in rat cardiovascular t i s s~e , '~ human vascular muscle,26 in rat brown adipose t i s s~e~~,~~ and intestine,'* and in pig dental pulp. 29 It is apparently not present in brain.…”

Section: Classification and Reaction Catalyzedmentioning

confidence: 98%

Interactions of monoamine oxidase with substrates and inhibitors

Dostert

Benedetti

Tipton

1989

Medicinal Research Reviews

143

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Section: Classification and Reaction Catalyzedmentioning

confidence: 98%

Interactions of monoamine oxidase with substrates and inhibitors

Dostert

Benedetti

Tipton

1989

Medicinal Research Reviews

143

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“…Tissue-bound SSAO has been described in many mammalian tissues, especially in those that are highly vascularized (Lyles 1996), and blood vessels (Precious and Lyles 1988). SSAO activity has also been found in nonvascular tissues, such as adipocytes (Barrand et al 1984;Morris et al 1997), odontoblasts (Norqvist et al 1981), and different parts of the bovine eye (Fernández de Arriba et al 1991) (see Lyles 1996 for review).…”

mentioning

confidence: 99%

Tissue Activity and Cellular Localization of Human Semicarbazide-sensitive Amine Oxidase

Andrés

Lizcano

Rodrı́guez

et al. 2001

J Histochem Cytochem.

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S U M M A R Y Semicarbazide-sensitive amine oxidase (SSAO), widely distributed in highly vascularized mammalian tissues, metabolizes endogenous and xenobiotic aromatic and aliphatic monoamines. To assess whether its physiological role in humans is restricted to oxidation, we used an immunohistochemical approach to examine the cellular localization of SSAO in human peripheral tissues (adrenal gland, duodenum, heart, kidney, lung, liver, pancreas, spleen, thyroid gland, and blood vessels) and also analyzed its subcellular localization. The results are in agreement with the specific activities also determined in the same samples and are discussed with reference to the tissue distribution of monoamine oxidase A and B. Together with the oxidative deamination of monoamines, SSAO cellular localization indicates that, in most human peripheral tissues, it might participate in the regulation of physiological processes via H 2 O 2 generation.

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“…Carbonyl reagents such as semicarbazide and isoniazid and a copper chelator , cuprizone, strongly inhibit pyridoxal phosphateand copper-containing amine oxidase(s), designated as BZO, clorgylineresistant amine oxidase or, more recently, semicarbazide-sensitive amine oxidase (24)(25)(26)(27)(28)(29)(30). However, these reagents do not inhibit the mitochondrial FAD-containing amine oxidase, MAO.…”

Section: Discussionmentioning

confidence: 99%

“…The present study showed that they did not significantly inhibit the activity of either carp preparation, even at the highest concentration used (10-3 M) (Table 4). Moreover, after complete inhibition of BZO, no inhibition of MAO by the carbonyl reagent isoniazid or the copper chelator cuprizone was observed (Table 4), suggesting that carp brain, like carp liver (5) and many mammalian tissues (24)(25)(26)(27)(28)(29)(30), may contain both MAO and BZO.…”

Section: Discussionmentioning

confidence: 99%