PMID: 15047694

Yan W, Samaha FF, Ramkumar M, Kleyman TR, Rubenstein RC
Cystic fibrosis transmembrane conductance regulator differentially regulates human and mouse epithelial sodium channels in Xenopus oocytes.
J Biol Chem. 2004 May 28;279(22):23183-92. Epub 2004 Mar 26., 2004-05-28 [PubMed]
Sentences
No. Mutations Sentence Comment
35 ABCC7 p.Thr663Ala
X
ABCC7 p.Thr663Ala 15047694:35:151
status: NEW
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We also tested the hypothesis that a naturally occurring polymorphism in the C terminus of ␣ hENaC, substitution of Ala at residue 663 for Thr (T663A), which we have recently shown to decrease the functional and surface expression of hENaC in oocytes,2 would influence regulatory interactions between CFTR and hENaC. Login to comment
79 ABCC7 p.Thr663Ala
X
ABCC7 p.Thr663Ala 15047694:79:138
status: NEW
view ABCC7 p.Thr663Ala details
Co-expression of CFTR and hENaC-We next assessed regulatory interactions between CFTR and hENaC as well as the potential influence of the T663A functional polymorphism of ␣ hENaC described recently by our group2 on these interactions. Login to comment
120 ABCC7 p.Thr663Ala
X
ABCC7 p.Thr663Ala 15047694:120:291
status: NEW
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We recently observed that the C-terminal 20 residues (residues 650-669) of ␣ hENaC, when expressed at the C terminus of a murine/human ␣ ENaC chimera in place of the 21 C-terminal amino acids of ␣ mENaC (residues 679-699), were sufficient to confer functionality of the T663A polymorphism of ␣ hENaC.2 Given that mENaC (Fig. 1 and Ref. Login to comment
134 ABCC7 p.Thr663Ala
X
ABCC7 p.Thr663Ala 15047694:134:249
status: NEW
view ABCC7 p.Thr663Ala details
As our data suggest differences between the interregulation of wild type CFTR and hENaC versus wild type CFTR and mENaC, we sought to characterize regulatory interactions between ⌬F508-CFTR and hENaC as well as the potential influence of the T663A functional polymorphism on these interactions (Fig. 7). Login to comment