Department of Pharmacy, Zhongnan Hospital of Wuhan University, Wuhan, Hubei 430071, P.R. China.
Department of Cardiovascular Biology, Meharry Medical College, Nashville, TN 37208, USA.
Int J Mol Med. 2014 Feb;33(2):462-8. doi: 10.3892/ijmm.2013.1566. Epub 2013 Nov 26.
Individuals carrying mutations at both ataxia telangiectasia mutated (ATM) gene alleles reportedly have increased plasma cholesterol and triglyceride levels. Previous studies have demonstrated that defective ATM function promotes atherosclerosis. We previously demonstrated that ATM facilitates the clearance of plasma apolipoprotein (Apo)E-deficient, ApoB48-containing (E(-)/B(48)) lipoproteins in ApoE-deficient mice (ApoE(-/-) mice). However, to date there is no exact explanation available as to the mechanism(s) through which ATM is involved in the removal of E(-)/B(48) lipoprotein in ApoE(-/-) mice. In this study, to our knowledge, we demonstrate for the first time that heterozygous ATM mutation reduces the hepatocyte uptake of E(-)/B(48) lipoproteins in ApoE(-/-) mice; however, heterozygous ATM mutation did not affect hepatocyte binding to E(-)/B(48) lipoproteins. Moreover, our results revealed that ATM proteins were localized in the nucleus, early endosomes and late endosomes, but not in the plasma membrane in the hepatocytes of ApoE(-/-) mice. In addition, following treatment with the ATM activator, chloroquine, and E(-)/B(48) lipoproteins, ATM interacted with class III phosphatidylinositol-3-kinases (PI3Ks) and the activated ATM protein enhanced class III PI3K activity. Furthermore, treatment with a class III PI3K inhibitor (LY290042 and 3-MA) attenuated the intracellular total cholesterol accumulation induced by ATM activation. These results provide insight into the mechanisms behind the involvment of ATM in the process of endocytosis of E(-)/B(48) lipoprotein in ApoE(-/-) mice, demonstrating the role of class III PI3K protein.
据报道,携带两种共济失调毛细血管扩张突变基因(ATM)突变的个体血浆胆固醇和甘油三酯水平升高。先前的研究表明,有缺陷的 ATM 功能会促进动脉粥样硬化的形成。我们之前的研究表明,ATM 有助于清除载脂蛋白 E 缺乏的血浆载脂蛋白(Apo)E-缺陷、载脂蛋白 B48 包含(E(-)/B(48))脂蛋白在载脂蛋白 E 缺陷的小鼠(ApoE(-/-) 小鼠)中。然而,迄今为止,尚无确切的解释说明 ATM 是如何参与清除 ApoE(-/-) 小鼠中 E(-)/B(48)脂蛋白的。在这项研究中,据我们所知,我们首次证明杂合 ATM 突变可减少 ApoE(-/-) 小鼠中肝细胞对 E(-)/B(48)脂蛋白的摄取;然而,杂合 ATM 突变并不影响肝细胞对 E(-)/B(48)脂蛋白的结合。此外,我们的结果表明,ATM 蛋白定位于 ApoE(-/-) 小鼠肝细胞的细胞核、早期内体和晚期内体,而不是质膜。此外,在用 ATM 激活剂氯喹和 E(-)/B(48)脂蛋白处理后,ATM 与 III 类磷酸肌醇-3-激酶(PI3Ks)相互作用,激活的 ATM 蛋白增强了 III 类 PI3K 活性。此外,用 III 类 PI3K 抑制剂(LY290042 和 3-MA)处理可减弱 ATM 激活引起的细胞内总胆固醇积累。这些结果为阐明 ATM 在 ApoE(-/-) 小鼠 E(-)/B(48)脂蛋白内吞过程中的作用机制提供了深入了解,表明了 III 类 PI3K 蛋白的作用。