Lectin-like oxidized low-density lipoprotein receptor (LOX-1) is a scavenger receptor that binds oxidized low-density lipoprotein (OxLDL) and has a role in atherosclerosis development. The N-terminus intracellular region (cytoplasmic domain) of LOX-1 mediates receptor internalization and trafficking, potentially through intracellular protein interactions. Using affinity isolation, we identified 6 of the 8 components of the chaperonin-containing TCP-1 (CCT) complex bound to LOX-1 cytoplasmic domain, which we verified by coimmunoprecipitation and immunostaining in human umbilical vein endothelial cells. We found that the interaction between CCT and LOX-1 is direct and ATP-dependent and that OxLDL suppressed this interaction. Understanding the association between LOX-1 and the CCT complex may facilitate the design of novel therapies for cardiovascular disease.

中文翻译：

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含有伴侣蛋白的 TCP-1 复合物直接与 LOX-1 受体的细胞质结构域结合。

凝集素样氧化低密度脂蛋白受体 (LOX-1) 是一种清道夫受体，可结合氧化低密度脂蛋白 (OxLDL) 并在动脉粥样硬化发展中发挥作用。LOX-1 的 N 端细胞内区域（细胞质域）可能通过细胞内蛋白质相互作用介导受体内化和运输。使用亲和分离，我们确定了包含伴侣蛋白的 TCP-1 (CCT) 复合物的 8 种成分中的 6 种与 LOX-1 细胞质域结合，我们通过人脐静脉内皮细胞中的共免疫沉淀和免疫染色进行了验证。我们发现 CCT 和 LOX-1 之间的相互作用是直接的且依赖于 ATP，而 OxLDL 抑制了这种相互作用。