Research in Japan Has Contributed to the Understanding of GPI Anchor Deficiency

2009 ◽  
pp. 323-325
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Taroh Kinoshita
Keyword(s):  
Glycobiology ◽  
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Vol 8 (8) ◽  
pp. 761-770 ◽  
Author(s):  
E. Canivenc-Gansel ◽  
I. Imhof ◽  
F. Reggiori ◽  
P. Burda ◽  
A. Conzelmann ◽  
...  
Keyword(s):  

Glycobiology ◽  
2006 ◽  
Vol 16 (10) ◽  
pp. 969-980 ◽  
Author(s):  
Franck Chevalier ◽  
Javier Lopez-Prados ◽  
Patrick Groves ◽  
Serge Perez ◽  
Manuel Martín-Lomas ◽  
...  

2004 ◽  
Vol 339 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Zuchao Ma ◽  
Jianjun Zhang ◽  
Fanzuo Kong
Keyword(s):  

2011 ◽  
Vol 286 (12) ◽  
pp. 10618-10627 ◽  
Author(s):  
Ekaterina N. Lyukmanova ◽  
Zakhar O. Shenkarev ◽  
Mikhail A. Shulepko ◽  
Konstantin S. Mineev ◽  
Dieter D'Hoedt ◽  
...  

Discovery of proteins expressed in the central nervous system sharing the three-finger structure with snake α-neurotoxins provoked much interest to their role in brain functions. Prototoxin LYNX1, having homology both to Ly6 proteins and three-finger neurotoxins, is the first identified member of this family membrane-tethered by a GPI anchor, which considerably complicates in vitro studies. We report for the first time the NMR spatial structure for the water-soluble domain of human LYNX1 lacking a GPI anchor (ws-LYNX1) and its concentration-dependent activity on nicotinic acetylcholine receptors (nAChRs). At 5–30 μm, ws-LYNX1 competed with 125I-α-bungarotoxin for binding to the acetylcholine-binding proteins (AChBPs) and to Torpedo nAChR. Exposure of Xenopus oocytes expressing α7 nAChRs to 1 μm ws-LYNX1 enhanced the response to acetylcholine, but no effect was detected on α4β2 and α3β2 nAChRs. Increasing ws-LYNX1 concentration to 10 μm caused a modest inhibition of these three nAChR subtypes. A common feature for ws-LYNX1 and LYNX1 is a decrease of nAChR sensitivity to high concentrations of acetylcholine. NMR and functional analysis both demonstrate that ws-LYNX1 is an appropriate model to shed light on the mechanism of LYNX1 action. Computer modeling, based on ws-LYNX1 NMR structure and AChBP x-ray structure, revealed a possible mode of ws-LYNX1 binding.


2021 ◽  
pp. 101153
Author(s):  
Samuel M. Duncan ◽  
Rupa Nagar ◽  
Manuela Damerow ◽  
Dmitry V. Yashunsky ◽  
Benedetta Buzzi ◽  
...  

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