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哺乳动物血浆胺氧化酶的起源。

The origin of mammalian plasma amine oxidases.

作者信息

Schwelberger H G

机构信息

Labor für Theoretische Chirurgie, Universitätsklinik für Chirurgie, Medizinische Universität Innsbruck, Innsbruck, Austria.

出版信息

J Neural Transm (Vienna). 2007;114(6):757-62. doi: 10.1007/s00702-007-0684-x. Epub 2007 Mar 26.

Abstract

Mammalian blood plasma contains considerable activity of soluble copper-containing amine oxidase (AOC) referred to as plasma or serum amine oxidase (SAO). The identity and origin of SAO was investigated based on the recent characterization of four porcine AOC genes with AOC1 encoding diamine oxidase (DAO), AOC2 retina-specific amine oxidase (RAO), AOC3 vascular adhesion protein-1 (VAP-1), and AOC4 a VAP-1 homologue that is expressed mainly in the liver and has a signal peptide sequence instead of a transmembrane domain at its N-terminus. Purification and characterization of the major amine oxidase activity from porcine serum showed that it is the product of the AOC4 gene. Intriguingly, all mammals possessing a functional AOC4 gene exhibit high plasma amine oxidase activity. Humans and rodents lack a functional AOC4 gene and have comparably low plasma amine oxidase activity that is probably derived from partial proteolytic release of the membrane-associated AOC3 gene product VAP-1.

摘要

哺乳动物血浆中含有相当高活性的可溶性含铜胺氧化酶(AOC),即血浆或血清胺氧化酶(SAO)。基于最近对四个猪AOC基因的特征描述,对SAO的身份和来源进行了研究,其中AOC1编码二胺氧化酶(DAO),AOC2是视网膜特异性胺氧化酶(RAO),AOC3是血管黏附蛋白-1(VAP-1),AOC4是VAP-1的同源物,主要在肝脏中表达,其N端有信号肽序列而非跨膜结构域。对猪血清中主要胺氧化酶活性的纯化和表征表明,它是AOC4基因的产物。有趣的是,所有拥有功能性AOC4基因的哺乳动物血浆胺氧化酶活性都很高。人类和啮齿动物缺乏功能性AOC4基因,血浆胺氧化酶活性相对较低,这可能源于膜相关AOC3基因产物VAP-1的部分蛋白水解释放。

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