用于成像配体-受体结合的分裂型高斯荧光素酶。
Split Gaussia luciferase for imaging ligand-receptor binding.
作者信息
Luker Kathryn E, Luker Gary D
机构信息
Center for Molecular Imaging, Department of Radiology, University of Michigan, Ann Arbor, MI, USA.
出版信息
Methods Mol Biol. 2014;1098:59-69. doi: 10.1007/978-1-62703-718-1_5.
Abstract
Ligand binding to cell surface receptors activates signaling pathways in normal and pathologic conditions, and internalized ligand-receptor complexes may continue to signal from endosomes. Accessibility of cell surface receptors and the central function of ligand-receptor binding in signal transduction make ligand binding a prime target for therapeutic agents. We describe a Gaussia luciferase complementation method for imaging ligand-receptor binding in cell-based assays and living mice. While we illustrate this imaging method for chemokine ligand CXCL12 and its receptors CXCR4 and CXCR7, this imaging strategy can be generalized to a large number of ligand-receptor interactions.
摘要
在正常和病理条件下，配体与细胞表面受体的结合会激活信号通路，内化的配体 - 受体复合物可能会在内体中继续发出信号。细胞表面受体的可及性以及配体 - 受体结合在信号转导中的核心作用，使得配体结合成为治疗药物的主要靶点。我们描述了一种用于在基于细胞的检测和活体小鼠中成像配体 - 受体结合的高斯荧光素酶互补方法。虽然我们以趋化因子配体CXCL12及其受体CXCR4和CXCR7为例说明了这种成像方法，但这种成像策略可以推广到大量的配体 - 受体相互作用。
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