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首页> 外文期刊>Molecular biology of the cell >Association of ABCA1 with syntaxin 13 and flotillin-1 and enhanced phagocytosis in Tangier cells
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Association of ABCA1 with syntaxin 13 and flotillin-1 and enhanced phagocytosis in Tangier cells

机译：ABCA1与syntaxin 13和flotillin-1的关联以及丹吉尔细胞吞噬作用增强

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The ATP-binding cassette transporter A1 (ABCA1) facilitates the cellular release of cholesterol and choline-phospholipids to apolipoprotein A-I (apoA-I) and several studies indicate that vesicular transport is associated with ABCA1 function. Syntaxins play a major role in vesicular fusion and have also been demonstrated to interact with members of the ABC-transporter family. Therefore, we focused on the identification of syntaxins that directly interact with ABCA1 The expression of syntaxins and ABCA1 in cultured human monocytes during M-CSF differentiation and cholesterol loading was investigated and syntaxins 3. 6, and 13 were found induced in foam cells together with ABCA1 Immunoprecipitation experiments revealed a direct association of syntaxin 13 and full-length ABCA1, whereas syntaxin 3 and 6 failed to interact with ABCA1. The colocalization of ABCA1 and syntaxin 13 was also shown by immunofluorescence microscopy. Silencing of syntaxin 13 by small interfering RNA (siRNA) led to reduced ABCA1 protein levels and hence to a significant decrease in apoA-I- dependent choline-phospholipid efflux. ABCA1 is localized in Lubrol WX- insoluble raft microdomains in macrophages and syntaxin 13 and flotillin-1 were also detected in these detergent resistant microdomains along with ABCA1 Syntaxin 13, flotillin-1, and ABCA1 were identified as phagosomal proteins, indicating the involvement of the phagosomal compartment in ABCA1-mediated lipid efflux. In addition, the uptake of latex phagobeads by fibroblasts with mutated ABCA1 was enhanced when compared with control cells and the recombinant expression of functional ABCA1 normalized the phagocytosis rate in Tangier fibroblasts. It is concluded that ABCA1 forms a complex with syntaxin 13 and flotillin-1, residing at the plasma membrane and in phagosomes that are partially located in raft microdomains.
机译：ATP结合盒转运蛋白A1（ABCA1）促进胆固醇和胆碱磷脂向载脂蛋白A-1（apoA-1）的细胞释放，一些研究表明囊泡转运与ABCA1功能相关。语法素在水泡融合中起主要作用，并且还被证明与ABC转运蛋白家族成员相互作用。因此，我们着重于与ABCA1直接相互作用的语法素的鉴定。研究了在培养的人单核细胞中M-CSF分化和胆固醇加载过程中语法素和ABCA1的表达，并发现了泡沫细胞中诱导了语法素3、6和13。 ABCA1免疫沉淀实验表明语法13和全长ABCA1直接相关，而语法3和6无法与ABCA1相互作用。免疫荧光显微镜检查还显示了ABCA1和Syntaxin 13的共定位。小干扰RNA（siRNA）对syntaxin 13的沉默导致ABCA1蛋白水平降低，并因此导致apoA-I依赖性胆碱-磷脂外排显着降低。 ABCA1位于巨噬细胞的Lubrol WX不溶性筏微结构域中，并且在这些耐洗涤剂的微结构域中还检测到了句法素13和flotillin-1以及ABCA1语法蛋白13，flortillin-1和ABCA1被鉴定为吞噬体蛋白，表明它们参与了噬菌体蛋白的表达。 ABCA1介导的脂质外流中的吞噬区室。此外，与对照细胞相比，具有突变的ABCA1的成纤维细胞对乳胶吞噬珠的吸收增加，并且功能性ABCA1的重组表达使丹吉尔成纤维细胞的吞噬率正常化。结论是ABCA1与syntaxin 13和flotilin-1形成复合物，存在于质膜和部分位于筏微区中的吞噬体中。

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