human α3β4 neuronal nicotinic receptors show different stoichiometry if they are expressed in xenopus oocytes or mammalian hek293 cells人类α3β4神经元烟碱受体显示不同化学计量学,如果他们在非洲爪蟾蜍卵母细胞或哺乳动物hek293细胞表达.pdfVIP

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human α3β4 neuronal nicotinic receptors show different stoichiometry if they are expressed in xenopus oocytes or mammalian hek293 cells人类α3β4神经元烟碱受体显示不同化学计量学,如果他们在非洲爪蟾蜍卵母细胞或哺乳动物hek293细胞表达.pdf

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human α3β4 neuronal nicotinic receptors show different stoichiometry if they are expressed in xenopus oocytes or mammalian hek293 cells人类α3β4神经元烟碱受体显示不同化学计量学,如果他们在非洲爪蟾蜍卵母细胞或哺乳动物hek293细胞表达

Human a3b4 Neuronal Nicotinic Receptors Show Different Stoichiometry if They Are Expressed in Xenopus Oocytes or Mammalian HEK293 Cells 1 1 2 1 3 Paraskevi Krashia , Mirko Moroni , Steven Broadbent , Giovanna Hofmann , Sebastian Kracun , Marco 1 4 1 Beato , Paul J. Groot-Kormelink , Lucia G. Sivilotti * 1 Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom, 2 Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne, United Kingdom, 3 Department of Physiology, University of California Los Angeles, Los Angeles, California, United States of America, 4 Novartis Horsham Research Centre, Novartis Institutes for Biomedical Research, Horsham, United Kingdom Abstract Background: The neuronal nicotinic receptors that mediate excitatory transmission in autonomic ganglia are thought to be formed mainly by the a3 and b4 subunits. Expressing this composition in oocytes fails to reproduce the properties of ganglionic receptors, which may also incorporate the a5 and/or b2 subunits. We compared the properties of human a3b4 neuronal nicotinic receptors expressed in Human embryonic kidney cells (HEK293) and in Xenopus oocytes, to examine the effect of the expression system and a:b subunit ratio. Methodology/Principal Findings: Two distinct channel forms were observed: these are likely to correspond to different stoichiometries of the receptor, with two or three copies of the a subunit, as reported for a4b2 channels. This interpretation is supported by the pattern of change in acetylcholine (ACh) sensitivity observed when a hydrophilic Leu to Thr mutation was in