Cloning of two rainbow trout nucleotide-binding oligomerization domain containing 2 (NOD2) splice variants and functional characterization of the NOD2 effector domains

2011 ◽  
Vol 30 (1) ◽  
pp. 118-127 ◽  
Author(s):  
Mingxian Chang ◽  
Tiehui Wang ◽  
Pin Nie ◽  
Jun Zou ◽  
Christopher J. Secombes
2017 ◽  
Vol 74 ◽  
pp. 82-89 ◽  
Author(s):  
Huilin Li ◽  
Hui Jin ◽  
Yaqian Li ◽  
Dejian Liu ◽  
Mohamed Frahat Foda ◽  
...  

2008 ◽  
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Masanori Tohno ◽  
Wataru Ueda ◽  
Yuko Azuma ◽  
Tomoyuki Shimazu ◽  
Shinichiro Katoh ◽  
...  

2014 ◽  
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pp. 10350-10364 ◽  
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María Teresa-Rodrigo ◽  
Juliane Eckhold ◽  
Beatriz Puisac ◽  
Andreas Dalski ◽  
María Gil-Rodríguez ◽  
...  

2002 ◽  
Vol 283 (2) ◽  
pp. C587-C598 ◽  
Author(s):  
Annette Hambrock ◽  
Regina Preisig-Müller ◽  
Ulrich Russ ◽  
Anke Piehl ◽  
Peter J. Hanley ◽  
...  

ATP-sensitive K+ (KATP) channels are composed of pore-forming Kir6.x subunits and regulatory sulfonylurea receptor (SUR) subunits. SURs are ATP-binding cassette proteins with two nucleotide-binding folds (NBFs) and binding sites for sulfonylureas, like glibenclamide, and for channel openers. Here we report the identification and functional characterization of four novel splice forms of guinea pig SUR1. Three splice forms originate from alternative splicing of the region coding for NBF1 and lack exons 17 (SUR1Δ17), 19 (SUR1Δ19), or both (SUR1Δ17Δ19). The fourth (SUR1C) is a COOH-terminal SUR1-fragment formed by exons 31–39 containing the last two transmembrane segments and the COOH terminus of SUR1. RT-PCR analysis showed that these splice forms are expressed in several tissues with strong expression of SUR1C in cardiomyocytes. Confocal microscopy using enhanced green fluorescent protein-tagged SUR or Kir6.x did not provide any evidence for involvement of these splice forms in the mitochondrial KATP channel. Only SUR1 and SUR1Δ17 showed high-affinity binding of glibenclamide ( K d≈ 2 nM in the presence of 1 mM ATP) and formed functional KATPchannels upon coexpression with Kir6.2.


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