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首页> 外文期刊>Cellular Physiology and Biochemistry >T1 alpha/Podoplanin Shows Raft-Associated Distribution in Mouse Lung Alveolar Epithelial E10 Cells
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T1 alpha/Podoplanin Shows Raft-Associated Distribution in Mouse Lung Alveolar Epithelial E10 Cells

机译：T1 alpha / Podoplanin在小鼠肺泡上皮E10细胞中显示筏相关的分布

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Aims: T1 alpha/(podoplanin) is abundantly expressed in the alveolar epithelial type I cells (ATI) of rodent and human lungs. Caveolin-1 is a classical primary structural protein of plasmalemal invaginations, so-called caveolae, which represent specialized lipid rafts, and which are particularly abundant in ATI cells. The biological functions of T1 alpha in the alveolar epithelium are unknown. Here we report on the characteristics of raft domains in the microplicae/microvillar protrusions of ATI cells, which contain T1 alpha. Methods: Detergent resistant membranes (DRMs) from cell lysates of the mouse epithelial ATI-like cell line E10 were prepared using different detergents followed by flotation in a sucrose gradient and tested by Western and dot blots with raft markers (caveolin-1, GM1) and nonraft markers (transferrin receptor, PDI and beta-Cop). Immunocytochemistry was employed for the localization of T1 alpha in E10 cells and in situ in rat lungs. Results: Our biochemical results showed that the solubility or insolubility of T1 alpha and caveolin-1 differs in Triton X-100 and Lubrol WX, two distinct non-ionic detergents. Caveolin-1 was unsoluble in both detergents, whereas T1 alpha was Triton X-100 soluble but Lubrol WX insoluble. Immunofluorescence double stainings revealed that both proteins were colocalized with GM1, while caveolin-1 and T1 alpha were not colocalized in the plasma membrane. Cholesterol depletion modified the segregation of T1 alpha in Lubrol WX DRMs. Cellular processes in ultrathin sections of cultured mouse E10 cells were immunogold positive. Immunoelectron microscopy (postembedding) of rat lung tissue revealed the preferential localization of T1 alpha on apical microvillar protrusions of ATI cells. Conclusion: We conclude that T1 alpha and caveolin-1 are located in distinct plasma membrane microdomains, which differ in their protein-lipid interactions. The raft-associated distribution of T1 alpha may have an impact on a specific, not yet clarified function of this protein in the alveolar epithelium.
机译：目的：T1 alpha /（podoplanin）在啮齿动物和人肺的肺泡上皮I型细胞（ATI）中大量表达。 Caveolin-1是血浆缺陷内陷的经典主要结构蛋白，即所谓的caveolae，它代表专门的脂质筏，在ATI细胞中特别丰富。 T1α在肺泡上皮中的生物学功能尚不清楚。在这里，我们报告的ATI细胞的微孔/微绒毛突起中的筏域的特征，其中包含T1 alpha。方法：使用不同的去污剂制备小鼠上皮ATI样细胞E10的细胞裂解液的去污剂抗性膜（DRMs），然后在蔗糖梯度中浮选，并通过带有筏标记（caveolin-1，GM1）的Western和点印迹进行测试和非筏标记（运铁蛋白受体，PDI和β-Cop）。免疫细胞化学用于在E10细胞中和大鼠肺中原位定位T1α。结果：我们的生化结果表明，T1 alpha和Caveolin-1在两种不同的非离子型去污剂Triton X-100和Lubrol WX中的溶解度或不溶性不同。 Caveolin-1在两种洗涤剂中均不溶，而T1α在Triton X-100中可溶，而Lubrol WX不溶。免疫荧光双染色显示这两种蛋白均与GM1共定位，而小窝蛋白1和T1α在质膜中未共定位。胆固醇消耗改变了Lubrol WX DRM中T1α的分离。培养的小鼠E10细胞超薄切片中的细胞过程是免疫金阳性的。大鼠肺组织的免疫电子显微镜检查（包埋后）显示ATI细胞的顶端微绒毛突起中T1 alpha的优先定位。结论：我们得出结论，T1α和小窝蛋白1位于不同的质膜微区，它们的蛋白质-脂质相互作用不同。筏相关的T1α分布可能会影响该蛋白在肺泡上皮中的特定功能（尚未阐明）。

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