Kaznacheyeva E, Lupu V D, Bezprozvanny I
Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9040, USA.
J Gen Physiol. 1998 Jun;111(6):847-56. doi: 10.1085/jgp.111.6.847.
The inositol (1,4,5)-trisphosphate receptor (InsP3R) mediates Ca2+ release from intracellular stores in response to generation of second messenger InsP3. InsP3R was biochemically purified and cloned, and functional properties of native InsP3-gated Ca2+ channels were extensively studied. However, further studies of InsP3R are obstructed by the lack of a convenient functional assay of expressed InsP3R activity. To establish a functional assay of recombinant InsP3R activity, transient heterologous expression of neuronal rat InsP3R cDNA (InsP3R-I, SI- SII+ splice variant) in HEK-293 cells was combined with the planar lipid bilayer reconstitution experiments. Recombinant InsP3R retained specific InsP3 binding properties (Kd = 60 nM InsP3) and were specifically recognized by anti-InsP3R-I rabbit polyclonal antibody. Density of expressed InsP3R-I was at least 20-fold above endogenous InsP3R background and only 2-3-fold lower than InsP3R density in rat cerebellar microsomes. When incorporated into planar lipid bilayers, the recombinant InsP3R formed a functional InsP3-gated Ca2+ channel with 80 pS conductance using 50 mM Ba2+ as a current carrier. Mean open time of recombinant InsP3-gated channels was 3.0 ms; closed dwell time distribution was double exponential and characterized by short (18 ms) and long (130 ms) time constants. Overall, gating and conductance properties of recombinant neuronal rat InsP3R-I were very similar to properties of native rat cerebellar InsP3R recorded in identical experimental conditions. Recombinant InsP3R also retained bell-shaped dependence on cytosolic Ca2+ concentration and allosteric modulation by ATP, similar to native cerebellar InsP3R. The following conclusions are drawn from these results. (a) Rat neuronal InsP3R-I cDNA encodes a protein that is either sufficient to produce InsP3-gated channel with functional properties identical to the properties of native rat cerebellar InsP3R, or it is able to form a functional InsP3-gated channel by forming a complex with proteins endogenously expressed in HEK-293 cells. (b) Successful functional expression of InsP3R in a heterologous expression system provides an opportunity for future detailed structure-function characterization of this vital protein.
肌醇(1,4,5)-三磷酸受体(InsP3R)介导细胞内钙库释放Ca2+,以响应第二信使肌醇三磷酸(InsP3)的生成。InsP3R已通过生化方法纯化并克隆,并且对天然InsP3门控Ca2+通道的功能特性进行了广泛研究。然而,由于缺乏对表达的InsP3R活性的便捷功能检测方法,InsP3R的进一步研究受到阻碍。为了建立重组InsP3R活性的功能检测方法,将大鼠神经元InsP3R cDNA(InsP3R-I,SI-SII+剪接变体)在HEK-293细胞中的瞬时异源表达与平面脂质双层重组实验相结合。重组InsP3R保留了特定的InsP3结合特性(Kd = 60 nM InsP3),并被抗InsP3R-I兔多克隆抗体特异性识别。表达的InsP3R-I的密度比内源性InsP3R背景至少高20倍,仅比大鼠小脑微粒体中的InsP3R密度低2-3倍。当整合到平面脂质双层中时,重组InsP3R使用50 mM Ba2+作为电流载体形成了一个具有80 pS电导的功能性InsP3门控Ca2+通道。重组InsP3门控通道的平均开放时间为3.0毫秒;关闭驻留时间分布是双指数的,其特征在于短(18毫秒)和长(130毫秒)时间常数。总体而言,重组大鼠神经元InsP3R-I的门控和电导特性与在相同实验条件下记录的天然大鼠小脑InsP3R的特性非常相似。重组InsP3R也保留了对胞质Ca2+浓度的钟形依赖性以及ATP的变构调节,类似于天然小脑InsP3R。从这些结果得出以下结论。(a)大鼠神经元InsP3R-I cDNA编码的蛋白质要么足以产生具有与天然大鼠小脑InsP3R特性相同的功能特性的InsP3门控通道,要么能够通过与HEK-293细胞中内源性表达的蛋白质形成复合物来形成功能性InsP3门控通道。(b)InsP3R在异源表达系统中的成功功能表达为该重要蛋白质未来详细的结构-功能表征提供了机会。