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脂蛋白脂肪酶等电点异构体在人体中的研究。

Lipoprotein lipase isoelectric point isoforms in humans.

机构信息

Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, Barcelona, Spain.

CSIC/UAB Proteomics Laboratory, IIBB-CSIC-IDIBAPS, Barcelona, Spain.

出版信息

Biochem Biophys Res Commun. 2014 Mar 7;445(2):480-5. doi: 10.1016/j.bbrc.2014.02.028. Epub 2014 Feb 13.

DOI:10.1016/j.bbrc.2014.02.028
PMID:24530399
Abstract

Lipoprotein lipase (LPL) hydrolyzes circulating triacylglycerols (TAG) into free fatty acids and glycerol. It is present in almost all tissues and its tissue-specific regulation directs the flow of circulating TAG in the body. We demonstrated in a previous study that, in rat heart and post-heparin plasma (PHP), LPL consists of a pattern of more than 8 forms of the same apparent molecular weight, but different isoelectric point (pI). In the present study we describe, for the first time, the existence of at least nine LPL pI isoforms in human PHP, with apparent pI between 6.8 and 8.6. Separation and characterization of these forms was carried out by 2DE combined with Western blotting and mass spectrometry (MALDI-TOF/MS and LC-MS/MS). Further studies are needed to discover their molecular origin, the pattern of pI isoforms in human tissues, their possible physiological functions and possible modifications of their pattern in different pathologies.

摘要

脂蛋白脂肪酶 (LPL) 将循环三酰甘油 (TAG) 水解为游离脂肪酸和甘油。它几乎存在于所有组织中,其组织特异性调节决定了体内循环 TAG 的流动。我们之前的研究表明,在大鼠心脏和肝素后血浆 (PHP) 中,LPL 由超过 8 种相同表观分子量但不同等电点 (pI) 的形式组成。在本研究中,我们首次描述了人 PHP 中至少存在 9 种 LPL pI 同工型,其表观 pI 介于 6.8 和 8.6 之间。这些形式的分离和鉴定是通过 2DE 结合 Western 印迹和质谱法 (MALDI-TOF/MS 和 LC-MS/MS) 进行的。需要进一步的研究来发现它们的分子起源、人组织中 pI 同工型的模式、它们可能的生理功能以及不同病理状态下其模式的可能变化。

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