Molecular characteristics of tissue-bound semicarbazide-sensitive amine oxidase (SSAO) in guinea pig tissues

Various mammalian tissues contain a tissue-bound amine oxidizing enzyme distinct from mitochondrial outer membrane enzyme, monoamine oxidase (MAO, EC 1.4.3.4), termed semicarbazide-sensitive amine oxidase (SSAO, EC 1.4.3.6). An increase in SSAO activity was found in patients suffering from vascular...

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Veröffentlicht in:Life sciences (1973) 2002-02, Vol.70 (13), p.1519-1531
Hauptverfasser: Kobayashi, Naoyuki, Takahashi, Kazuya, Takayanagi, Kaori, Takahashi, Kaori, Masuko, Shin, Tadano, Takeshi, Kisara, Kensuke, Kinemuchi, Hiroyasu
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container_end_page 1531
container_issue 13
container_start_page 1519
container_title Life sciences (1973)
container_volume 70
creator Kobayashi, Naoyuki
Takahashi, Kazuya
Takayanagi, Kaori
Takahashi, Kaori
Masuko, Shin
Tadano, Takeshi
Kisara, Kensuke
Kinemuchi, Hiroyasu
description Various mammalian tissues contain a tissue-bound amine oxidizing enzyme distinct from mitochondrial outer membrane enzyme, monoamine oxidase (MAO, EC 1.4.3.4), termed semicarbazide-sensitive amine oxidase (SSAO, EC 1.4.3.6). An increase in SSAO activity was found in patients suffering from vascular disorders such as diabetes and diabetic complications. It has previously been shown that 2-bromoethylamine (2-BEA) is a potent, and selective suicidal inhibitor of tissue-bound SSAO. The aim of this study was to investigate the interaction of this suicidal SSAO inhibitor with the tissue-bound enzyme in guinea pig lung, kidney, stomach, and heart homogenates. The conditions necessary for this inhibitor to titrate the concentrations of this enzyme were also determined. 2-BEA appears to interact with SSAO, as reported previously for this enzyme from different sources, in a manner consistent with an irreversible, “suicide” reaction. Because of this property, 2-BEA could be used to titrate the concentrations of SSAO active centers in these tissues under the appropriate conditions employed. Although some possible non-specific binding of the inhibitor to sites other than the active center of the enzyme, metabolism of this inhibitor and/or presence of enzyme subtypes was hypothesized, the molecular characteristics of SSAO in these tissues (Km, Vmax values, enzyme efficiencies, approximate enzyme concentrations, and molecular turnover numbers) towards the substrate kynuramine (0.1 mM) at pH 7.4 and 37 °C have been estimated.
doi_str_mv 10.1016/S0024-3205(01)01523-5
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subjects 2-Bromoethylamine (2-BEA)
Amine Oxidase (Copper-Containing) - antagonists & inhibitors
Amine Oxidase (Copper-Containing) - metabolism
Animals
Dose-Response Relationship, Drug
Enzyme Inhibitors - pharmacology
Ethylamines - pharmacology
Guinea pig
Guinea Pigs
Heart - drug effects
Kidney - drug effects
Kidney - enzymology
Kinetics
Kynuramine - metabolism
Lung - drug effects
Lung - enzymology
Male
Molecular turnover number
Myocardium - enzymology
Semicarbazide-sensitive amine oxidase (SSAO)
Stomach - drug effects
Stomach - enzymology
Suicide inhibitor
Titration
title Molecular characteristics of tissue-bound semicarbazide-sensitive amine oxidase (SSAO) in guinea pig tissues
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