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Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors.

Authors :
Montenegro MF
Cabezas-Herrera J
Campoy FJ
Muñoz-Delgado E
Vidal CJ
Source :
FASEB journal : official publication of the Federation of American Societies for Experimental Biology [FASEB J] 2017 Feb; Vol. 31 (2), pp. 544-555. Date of Electronic Publication: 2016 Oct 25.
Publication Year :
2017

Abstract

The observation of acetylcholinesterase (AChE) type H (AChE <subscript>H</subscript> ), which is the predominant AChE variant in visceral organs and immune cells, in lipid rafts of muscle supports functional reasons for the raft targeting of glypiated AChE <subscript>H</subscript> The search for these reasons revealed that liver AChE activity is mostly confined to rafts and that the liver is able to make N-extended AChE variants and target them to rafts. These results prompted us to test whether AChE and muscarinic receptors existed in the same raft. Isolation of flotillin-2-rich raft fractions by their buoyancy in sucrose gradients, followed by immunoadsorption and matrix-assisted laser desorption ionization-time of flight-mass spectrometry application, gave the following results: 1) most hepatic AChE activity emanates from AChE-H mRNA, and its product, glypiated AChE <subscript>H</subscript> , accumulates in rafts; 2) N-extended N-AChE readthrough variant, nonglypiated N-AChE <subscript>H</subscript> , and N-AChE tailed variant were all identified in liver rafts; and 3) M3 AChRs were observed in rafts, and coprecipitation of raft-confined N-AChE and M3 receptors by using anti-M3 antibodies showed that enzyme and receptor reside in the same raft unit. A raft domain that harbors tightly packed muscarinic receptor and AChE may represent a molecular device that, by means of which, the intensity and duration of cholinergic inputs are regulated.-Montenegro, M. F., Cabezas-Herrera, J., Campoy, F. J., Muñoz-Delgado, E., Vidal, C. J. Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors.<br /> (© FASEB.)

Details

Language :
English
ISSN :
1530-6860
Volume :
31
Issue :
2
Database :
MEDLINE
Journal :
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Publication Type :
Academic Journal
Accession number :
28148778
Full Text :
https://doi.org/10.1096/fj.201600609R