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Figure 2 M1 and M23 AQP4 isoforms compared by freeze-fracture electron microscopic and Western blot analyses M1 and M23 AQP4 isoforms compared by freeze-fracture.

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Presentation on theme: "Figure 2 M1 and M23 AQP4 isoforms compared by freeze-fracture electron microscopic and Western blot analyses M1 and M23 AQP4 isoforms compared by freeze-fracture."— Presentation transcript:

1 Figure 2 M1 and M23 AQP4 isoforms compared by freeze-fracture electron microscopic and Western blot analyses M1 and M23 AQP4 isoforms compared by freeze-fracture electron microscopic and Western blot analyses (A) Plasma membranes of HEK293 cells expressing recombinant M1-AQP4 or M23-AQP4 viewed by freeze-fracture electron microscopy. (B) Western blot analysis of the proportion of recombinant AQP4 expressed in higher-order arrays or as tetramers in HEK293 cells transfected with plasmids encoding M23 alone (lane 1), M1 alone (lane 5), or different ratios of each (lanes 2–4). Intramembranous particles in M1-AQP4 cells are predominantly singlet (A, left). Compare the large lattices of orthogonal array-like assemblies in M23-AQP4 cells (A, right). M1-AQP4 coexpression inhibits high-order array formation by M23-AQP4 (B). The y-axis indicates molecular weight (kDa) of AQP4 structures. Solubilized proteins, separated by Blue Native gel electrophoresis and transferred to PDF membrane, were probed with monoclonal AQP4-specific IgG. AQP4 immunoreactivity in largest-sized arrays (lane 1) diminishes with increasing M1:M23 ratio, and the proportion in tetrameric form increases (lane 5). AQP4 = aquaporin-4; Ig = immunoglobulin; HEK = human embryonic kidney. J.P. Fryer et al. Neurol Neuroimmunol Neuroinflamm 2014;1:e11 © 2014 American Academy of Neurology

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