A purified functional non-NMDA glutamate receptor reconstituted in artificial lipid bilayers

1990 ◽  
Vol 16 ◽  
pp. 26
Keyword(s):  
Lipid Bilayers ◽  
Glutamate Receptor ◽  
Artificial Lipid Bilayers ◽  
Nmda Glutamate Receptor

In vivo evaluation of [11C]CNS-5161 as a use-dependent ligand for the NMDA glutamate receptor channel

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S595-S595 ◽  
Author(s):  
Wynne K Schiffer ◽  
Deborah Pareto-Onghena ◽  
HaiTao Wu ◽  
Kuo-Shyan Lin ◽  
Andrew R Gibbs ◽  
...  
Keyword(s):  
Glutamate Receptor ◽  
In Vivo Evaluation ◽  
Nmda Glutamate Receptor ◽  
Receptor Channel

scholarly journals Formation of artificial lipid bilayers using droplet dielectrophoresis

Lab on a Chip ◽  
2008 ◽  
Vol 8 (10) ◽  
pp. 1617 ◽  
Author(s):  
Sara Aghdaei ◽  
Mairi E. Sandison ◽  
Michele Zagnoni ◽  
Nicolas G. Green ◽  
Hywel Morgan
Keyword(s):  
Lipid Bilayers ◽  
Artificial Lipid Bilayers

scholarly journals A synergy between mechanosensitive calcium- and membrane-binding mediates tension-sensing by C2-like domains

2021 ◽  
Vol 119 (1) ◽  
pp. e2112390119
Author(s):  
Zhouyang Shen ◽  
Kalina T. Belcheva ◽  
Mark Jelcic ◽  
King Lam Hui ◽  
Anushka Katikaneni ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Membrane Insertion ◽  
C2 Domain ◽  
Hydrophobic Membrane ◽  
Membrane Recruitment ◽  
Calcium Dependent ◽  
Nuclear Membranes ◽  
Cytosolic Phospholipase ◽  
Artificial Lipid Bilayers ◽  
Quantitative Basis

When nuclear membranes are stretched, the peripheral membrane enzyme cytosolic phospholipase A2 (cPLA2) binds via its calcium-dependent C2 domain (cPLA2-C2) and initiates bioactive lipid signaling and tissue inflammation. More than 150 C2-like domains are encoded in vertebrate genomes. How many of them are mechanosensors and quantitative relationships between tension and membrane recruitment remain unexplored, leaving a knowledge gap in the mechanotransduction field. In this study, we imaged the mechanosensitive adsorption of cPLA2 and its C2 domain to nuclear membranes and artificial lipid bilayers, comparing it to related C2-like motifs. Stretch increased the Ca2+ sensitivity of all tested domains, promoting half-maximal binding of cPLA2 at cytoplasmic resting-Ca2+ concentrations. cPLA2-C2 bound up to 50 times tighter to stretched than to unstretched membranes. Our data suggest that a synergy of mechanosensitive Ca2+ interactions and deep, hydrophobic membrane insertion enables cPLA2-C2 to detect stretched membranes with antibody-like affinity, providing a quantitative basis for understanding mechanotransduction by C2-like domains.

Functional reconstitution of receptors in artificial lipid bilayers

1987 ◽  
Vol 81 (1-2) ◽  
pp. 133-138 ◽  
Author(s):  
Vitaly Vodyanoy ◽  
Dominique Muller ◽  
Kathryn Kramer ◽  
Gary Lynch ◽  
Michel Baudry
Keyword(s):  
Lipid Bilayers ◽  
Artificial Lipid Bilayers

α-Actinin-2 in rat striatum: localization and interaction with NMDA glutamate receptor subunits

2000 ◽  
Vol 79 (1-2) ◽  
pp. 77-87 ◽  
Author(s):  
Anthone W Dunah ◽  
Michael Wyszynski ◽  
Deborah M Martin ◽  
Morgan Sheng ◽  
David G Standaert
Keyword(s):  
Glutamate Receptor ◽  
Rat Striatum ◽  
Nmda Glutamate Receptor
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