Substrate Selectivity of Monoamine Oxidase A, Monoamine Oxidase B, Diamine Oxidase, and Semicarbazide-Sensitive Amine Oxidase in COS-1 Expression Systems
| Autor: | Mayuko Adachi, Yoshinori Ochiai, Eiichi Sakurai, Yorihisa Tanaka, Kunio Itoh |
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| Rok vydání: | 2006 |
| Předmět: |
Pharmacology
Amine oxidase Base Sequence biology Chemistry Pharmaceutical Science Substrate (chemistry) General Medicine Tyramine Substrate Specificity chemistry.chemical_compound Benzylamine Biochemistry COS Cells Chlorocebus aethiops biology.protein Animals Amine gas treating Amine Oxidase (Copper-Containing) Monoamine oxidase B Diamine oxidase Monoamine oxidase A Monoamine Oxidase DNA Primers |
| Zdroj: | Biological & Pharmaceutical Bulletin. 29:2362-2366 |
| ISSN: | 1347-5215 0918-6158 |
| Popis: | The substrate selectivity of monoamine oxidase A (MAO-A), monoamine oxidase B (MAO-B), diamine oxidase (DAO), and semicarbazide-sensitive amine oxidase (SSAO) was investigated in the absence of chemical inhibitors using the COS-1 cells expressed with respective amine oxidase. Serotonin (5-hydroxytryptamine), 1-methylhistamine, and histamine were preferentially oxidized by MAO-A, SSAO, and DAO, respectively, at a low substrate concentration. In contrast, benzylamine, tyramine, and beta-phenylethylamine served as substrates for all of MAO-A, MAO-B, and SSAO. Each amine oxidase showed broad substrate selectivity at a high substrate concentration. The cross-inhibition was remarkable in MAO-A and MAO-B, especially in MAO-A, but not in SSAO and DAO. A study of the substrate selectivity of amine oxidases should include consideration of the effects of substrate concentration and specific chemical inhibitors. |
| Databáze: | OpenAIRE |
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