ABCMdb

ABCC7 p.Thr663Ala

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Publications

PMID: 15047694 [PubMed] Yan W et al: "Cystic fibrosis transmembrane conductance regulator differentially regulates human and mouse epithelial sodium channels in Xenopus oocytes."

No. Sentence Comment

35 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 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 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 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

PMID: 15746174 [PubMed] Nagel G et al: "CFTR fails to inhibit the epithelial sodium channel ENaC expressed in Xenopus laevis oocytes."

No. Sentence Comment

184 They found less than 35% inhibition of murine ENaC by activated CFTR (their Fig. 1A), only a modest 20% inhibition for wildtype α-hENaC and no change for T663A α-hENaC, where threonine 663 (wildtype) was replaced by alanine (their Fig. 2). Login to comment

PMID: 19462466 [PubMed] Azad AK et al: "Mutations in the amiloride-sensitive epithelial sodium channel in patients with cystic fibrosis-like disease."

No. Sentence Comment

137 Since p.T663A-SCNN1A is a frequent variant, each missense mutation was introduced on the p.T663A-SCNN1A background as found in the patient. Login to comment
138 When the cis or trans configuration of the p.T663A-SCNN1A background could not be determined, the missense mutation was generated on both the p.T663-SCNN1A and p.A663-SCNN1A background. Login to comment

PMID: 17766193 [PubMed] Bangel N et al: "Upregulated expression of ENaC in human CF nasal epithelium."

No. Sentence Comment

164 We found a similar situation for Table 2 Single nucleotide polymorphisms in the α-, β- and γ-hnENaC subunits from CF and non-CF tissue and appropriate references α-ENaC Reference β-ENaC Reference γ-ENaC Reference T663A [53,54] A314G [55] R178W P502A A614S [53,55,56] A336P [53,56] F339S A350T Y369S D375G S458R [55] Fig. 2. mRNA expression data for all three hnENaC subunits of CF patients. Login to comment
214 We identified a common T663A polymorphism within the C-terminus of the hnENaC α-subunit of CF and non-CF epithelia. Login to comment
170 We found a similar situation for Table 2 Single nucleotide polymorphisms in the b1;-, b2;- and b3;-hnENaC subunits from CF and non-CF tissue and appropriate references b1;-ENaC Reference b2;-ENaC Reference b3;-ENaC Reference T663A [53,54] A314G [55] R178W P502A A614S [53,55,56] A336P [53,56] F339S A350T Y369S D375G S458R [55] Fig. 2. Login to comment
221 We identified a common T663A polymorphism within the C-terminus of the hnENaC b1;-subunit of CF and non-CF epithelia. Login to comment

PMID: 25900089 [PubMed] Brennan ML et al: "Assessment of epithelial sodium channel variants in nonwhite cystic fibrosis patients with non-diagnostic CFTR genotypes."

No. Sentence Comment

44 Ethnicity # of subjectsa SCNN1 subunit Genotype/clinical characteristicsb Sequence variantc Caucasian (France) [26] 56 B Two CFTR mutations; Classic CF p.Thr313Met, p.Gly589Ser G p.Leu481Gln, p.Val546Ile Caucasian (Europe) [28] 29; 47 A One/no CFTR mutation; typical and atypical CF cases c.-760ANG, c.-717GNC, c.-68CNT, p.Pro33Pro p.Phe61Leu, p.Val114Ile, p.Leu180Leu, p.Arg181Trp, p.Ala334Thr, p.Trp493Arg, p.Thr663Ala B p.Ser82Cys, p.Pro93Pro, c.777-5TNC, p.Phe293Phe, p.Ile515Ile, p.Gly589Ser, p.Asp629Asp G p.Tyr129Tyr, p.Ile158Ile, p.Gly183Gly, p.Glu197Lys, c.1176+14ANG, c.1373+29TNC, c.1432-7GNA, p.Leu649Leu Unknown (USA) [23] 20 A No CFTR mutations p.Arg181Trp B Non-classic CF p.Glu539Lys, c.1543-2ANG African 5; 55 (Rwanda) [27] A One/no CFTR mutation; CF-like c.-28TNC, p.Val573Ile B p.Val348Met, p.Gly442Val, p.Thr577Thr, c.1346+28CNT G p.Ser212Ser, c.1176+30GNC Caucasian (Spain) [29] 10 A One/no CFTR mutation; CF and CF-like p.Val14Gly, p.Leu203Leu, p.Arg204Trp, p.Ala304Pro, p.Ala357Thr, p.Cys641Phe, c.875+35GNA B p.Phe293Phe, p.Arg563Gln, p.Pro574Pro G p.Gly183Gly Caucasian/African (France) [24] 20; 35 B One/no CFTR mutation p.Ser82Cys, p.Asn288Ser,p.Pro369Thr G Bronchiectasis p.Gly183Ser, p.Glu197Lys Caucasian (Italy) [35] 24; 15 A One/no CFTR mutation; CFTR-related disorders c.-760ANG, p.Ala334Thr, p.Thr663Ala B p.Pro93Pro, p.Phe293Phe G p.Tyr129Tyr, p.Ile158Ile, p.Gly183Gly, p.Leu649Leu, c.1176+14ANG, c.1373+29TNC, c.1432-7GNA a Listed as number of subjects per genotype (if known). Login to comment