Department of Physiology, Seoul National University College of Medicine, Seoul, Republic of Korea; Department of Physiology, Sungkyunkwan University School of Medicine, Suwon, Republic of Korea; Wide River Institute of Immunology, Seoul National University College of Medicine, Hongcheon, Republic of Korea.
Department of Physiology, Seoul National University College of Medicine, Seoul, Republic of Korea.
Biochem Biophys Res Commun. 2024 Mar 5;699:149561. doi: 10.1016/j.bbrc.2024.149561. Epub 2024 Jan 23.
In mouse B lymphocytes, an unidentified slow-activating voltage-dependent current resembling the characteristics of the Calhm family ion channel (I) was investigated. RT-PCR analysis revealed the presence of Calhm2 and 6 transcripts, with subsequent whole-cell patch-clamp studies indicating that the I is augmented by heat, alkaline pH, and low extracellular [Ca]. Overexpression of Calhm2, but not Calhm6, in N2A cells recapitulated I. Moreover, Calhm2 knockdown in Bal-17 cells abolished I. We firstly identify the voltage-dependent ion channel function of the Calhm2 in the mouse immune cells. ATP release assays in primary mouse B cells suggested a significant contribution of Calhm2 for purinergic signaling at physiological temperature.
在小鼠 B 淋巴细胞中,研究了一种未被识别的缓慢激活的电压依赖性电流,其特征类似于 Calhm 家族离子通道(I)。RT-PCR 分析显示存在 Calhm2 和 6 种转录本,随后的全细胞膜片钳研究表明,I 可被热、碱性 pH 值和低细胞外 [Ca] 增强。在 N2A 细胞中过表达 Calhm2,但不是 Calhm6,可重现 I。此外,Bal-17 细胞中 Calhm2 的敲低消除了 I。我们首次在小鼠免疫细胞中鉴定了 Calhm2 的电压依赖性离子通道功能。在原代小鼠 B 细胞中的 ATP 释放实验表明,Calhm2 对生理温度下的嘌呤能信号传递有重要贡献。