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：

---

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，我们鉴定了与 LOX-1 细胞质结构域结合的含伴侣蛋白 TCP-1 (CCT) 复合物的 8 种成分中的 6 种，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和 ATP 依赖性的，而 OxLDL 抑制了这种相互作用。