Higher order structure of aquaporin-4

Abstract Unlike other mammalian AQPs, multiple tetramers of AQP4 associate in the plasma membrane to form peculiar structures called Orthogonal Arrays of Particles (OAPs), that are observable by freeze-fracture electron microscopy (FFEM). However, FFEM cannot give information about the composition o...

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Bibliographic Details
Published in:Neuroscience 2010-07, Vol.168 (4), p.903-914
Main Authors: Nicchia, G.P, Rossi, A, Mola, M.G, Pisani, F, Stigliano, C, Basco, D, Mastrototaro, M, Svelto, M, Frigeri, A
Format: Article
Language:English
Subjects:
Animals
AQP4
Aquaporin 4 - chemistry
Aquaporin 4 - metabolism
aquaporins
Astrocytes - metabolism
Autoantibodies - chemistry
Autoantibodies - metabolism
BN–SDS/PAGE
Brain - metabolism
Cell Membrane - chemistry
Cell Membrane - metabolism
Cells, Cultured
Dystrophin - chemistry
Dystrophin - genetics
Dystrophin - metabolism
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Mice
Mice, Knockout
Neurology
Neuromyelitis Optica - immunology
NMO
NMO-IgG
OAPs
Protein Isoforms - chemistry
Protein Isoforms - metabolism
Protein Multimerization
Protein Structure, Quaternary
Rats
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Summary:Abstract Unlike other mammalian AQPs, multiple tetramers of AQP4 associate in the plasma membrane to form peculiar structures called Orthogonal Arrays of Particles (OAPs), that are observable by freeze-fracture electron microscopy (FFEM). However, FFEM cannot give information about the composition of OAPs of different sizes, and due to its technical complexity is not easily applicable as a routine technique. Recently, we employed the 2D gel electrophoresis BN–SDS/PAGE that for the first time enabled the biochemical isolation of AQP4-OAPs from several tissues. We found that AQP4 protein is present in several higher-order complexes (membrane pools of supra-structures) which contain different ratios of M1/M23 isoforms corresponding to AQP4-OAPs of different size. In this paper, we illustrate in detail the potentiality of 2D BN/SDS-PAGE for analyzing AQP4 supra-structures, their relationship with the dystrophin glycoprotein complex and other membrane proteins, and their role as a specific target of Neuromyelitis Optica autoantibodies.
ISSN:0306-4522
1873-7544
DOI:10.1016/j.neuroscience.2010.02.008