研究特定细胞表面受体介导的细胞维生素A摄取的技术。
Techniques to study specific cell-surface receptor-mediated cellular vitamin A uptake.
作者信息
Kawaguchi Riki, Sun Hui
机构信息
Department of Physiology, Jules Stein Eye Institute, and Brain Research Institute, David Geffen School of Medicine, University of California, Los Angeles, CA 90095-1751, USA.
出版信息
Methods Mol Biol. 2010;652:341-61. doi: 10.1007/978-1-60327-325-1_20.
STRA6 is a multitransmembrane domain protein that was recently identified as the cell-surface receptor for plasma retinol-binding protein (RBP), the vitamin A carrier protein in the blood. STRA6 binds to RBP with high affinity and mediates cellular uptake of vitamin A from RBP. It is not homologous to any known receptors, transporters, and channels, and it represents a new class of membrane transport protein. Consistent with the diverse physiological functions of vitamin A, STRA6 is widely expressed in diverse adult organs and throughout embryonic development. Mutations in human STRA6 that abolish its vitamin A uptake activity cause severe pathological phenotypes in many human organs including the eye, brain, lung, and heart. This chapter describes functional assays for STRA6 in live cells and on cellular membranes. These assays can be employed to study the mechanism of this new membrane transport mechanism and its roles in the physiology and pathology of many organs.
STRA6是一种多跨膜结构域蛋白，最近被鉴定为血液中维生素A载体蛋白——血浆视黄醇结合蛋白（RBP）的细胞表面受体。STRA6与RBP具有高亲和力结合，并介导细胞从RBP摄取维生素A。它与任何已知的受体、转运蛋白和通道均无同源性，代表了一类新的膜转运蛋白。与维生素A的多种生理功能一致，STRA6在多种成年器官以及整个胚胎发育过程中广泛表达。人类STRA6中消除其维生素A摄取活性的突变会在包括眼睛、大脑、肺和心脏在内的许多人体器官中导致严重的病理表型。本章描述了在活细胞和细胞膜上对STRA6进行功能测定的方法。这些测定可用于研究这种新的膜转运机制及其在许多器官的生理和病理中的作用。
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