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Speciated Human High-Density Lipoprotein Protein Proximity Profiles

机译：特定的人类高密度脂蛋白蛋白质邻近特征

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It is expected that the attendant structural heterogeneity of human high-density lipoprotein (HDL)ncomplexes is a determinant of its varied metabolic functions. To determine the structural heterogeneity ofnHDL, we determinedmajor apolipoprotein stoichiometry profiles in human HDL. First, HDL was separatedninto twomain populations, with and without apolipoprotein (apo) A-II, LpA-I and LpA-I/A-II, respectively.nEach main population was further separated into six individual subfractions using size exclusion chroma-ntography (SEC). Protein proximity profiles (PPPs) of major apolipoproteins in each individual subfrac-ntion was determined by optimally cross-linking apolipoproteins within individual particles with bis-n(sulfosuccinimidyl) suberate (BS3n), a bifunctional cross-linker, followed by molecular mass determination bynMALDI-MS. The PPPs of LpA-I subfractions indicated that the number of apoA-I molecules increased fromntwo to three to four with an increase in the LpA-I particle size. On the other hand, the entire population ofnLpA-I/A-II demonstrated the presence of only two proximal apoA-I molecules per particle, while the numbernof apoA-II molecules varied from one dimeric apoA-II to two and then to three. For most of the PPPsndescribed above, an additional population that contained a single molecule of apoC-III in addition to apoA-Inand/or apoA-II was detected. Upon composition analyses of individual subpopulations, LpA-I/A-IInexhibited comparable proportions for total protein (∼58%), phospholipids (∼21%), total cholesteroln(∼16%), triglycerides (∼5%), and free cholesterol (∼4%) across subfractions. LpA-I components, on thenother hand, showed significant variability. This novel information about HDL subfractions will form a basisnfor an improved understanding of particle-specific functions of HDL.
机译：预期人类高密度脂蛋白（HDL）复合物伴随的结构异质性是其各种代谢功能的决定因素。为了确定nHDL的结构异质性，我们确定了人类HDL中主要的载脂蛋白化学计量分布。首先，将HDL分为两个主要种群，分别有和没有载脂蛋白（apo）A-II，LpA-I和LpA-I / A-II.n使用大小排阻色谱法将每个主要种群进一步分为6个单独的亚组分（ SEC）。通过将单个颗粒中的载脂蛋白与双功能正辛二酸双正辛酯（BS3n）最佳交联，然后通过nMALDI进行分子质量测定，可确定每个单个亚片段中主要载脂蛋白的蛋白质接近谱（PPPs） -多发性硬化症。 LpA-I子级的PPPs表明，随着LpA-I粒径的增加，apoA-I分子的数量从两个增加到三个到四个。另一方面，整个nLpA-I / A-II群体显示每个粒子仅存在两个近端apoA-I分子，而apoA-II分子的数量从一个二聚apoA-II变为两个，然后变为三个。对于上述大多数PPPs，检测到除apoA-Inand /或apoA-II外还包含单分子apoC-III的其他种群。根据各个亚群的组成分析，LpA-I / A-IIn的可比比例为总蛋白（〜58％），磷脂（〜21％），总胆固醇（〜16％），甘油三酸酯（〜5％）和游离胆固醇（〜4％）。另一方面，LpA-I组分显示出显着的可变性。有关HDL子级分的新颖信息将为更好地理解HDL的特定粒子功能奠定基础。

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  • 来源
    《Biochemistry》 |2010年第50期|p.10656-10665|共10页
  • 作者

    Kekulawalage Gauthamadasa Corina Rosales Henry J. Pownall Stephen Macha W. Gray Jerome Rong Huang and R. A. Gangani D. Silva;

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    ‡Department of Pathology and Laboratory Medicine, University of Cincinnati, Cincinnati, Ohio 45237, United States,§Section ofAtherosclerosis and VascularMedicine, Department ofMedicine, Baylor College ofMedicine, Houston, Texas 77030, United States,) Mass Spectrometry Services, Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221, United States, and^Department of Pathology, Vanderbilt University Medical Center, Nashville, Tennessee 37232, United States;

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