Substrate Selectivity of Monoamine Oxidase A, Monoamine Oxidase B, Diamine Oxidase, and Semicarbazide-Sensitive Amine Oxidase in COS-1 Expression Systems
-
- Ochiai Yoshinori
- Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
-
- Itoh Kunio
- Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
-
- Adachi Mayuko
- Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
-
- Tanaka Yorihisa
- Department of Drug Metabolism and Pharmacokinetics, Tohoku Pharmaceutical University
この論文をさがす
抄録
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 β-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.
収録刊行物
-
- Biological & Pharmaceutical Bulletin
-
Biological & Pharmaceutical Bulletin 29 (12), 2362-2366, 2006
公益社団法人 日本薬学会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1390282679603464576
-
- NII論文ID
- 110006148653
-
- NII書誌ID
- AA10885497
-
- ISSN
- 13475215
- 09186158
-
- NDL書誌ID
- 8548568
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可