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 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 20 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.
Autore Pugliese
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FRIGERI A.;PISANI F.;NICCHIA G.P.;SVELTO M.
Titolo volume/Rivista
Non Disponibile
Anno di pubblicazione
2010
ISSN
0306-4522
ISBN
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Nessuna citazione
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Numero di citazioni Scopus
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Settori ERC
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Codici ASJC
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