ABCMdb

ABCC7 p.Ala107Cys

None has been submitted yet.

Publications

PMID: 23442957 [PubMed] Gao X et al: "Cysteine scanning of CFTR's first transmembrane segment reveals its plausible roles in gating and permeation."

No. Sentence Comment

8 Interestingly, whole-cell A107C-CFTR currents were very sensitive to changes of bath pH as if the introduced cysteine assumes an altered pKa-like T338C in TM6. Login to comment
105 Further addition of a specific CFTR inhibitor, CFTRinh-172 (39,40), caused a minor decrease of the residual current, indicating a drastic reduction of I106C-CFTR currents by external MTSES. Similar results were obtained for A107C- and Y109C-CFTR except that the magnitude of inhibition for A107C-CFTR is significantly smaller (Fig. 3 C). Login to comment
113 The similarity between TM1 and TM6 was reinforced by the following results with A107C mutant channels. Login to comment
114 When recording whole-cell A107C-CFTR current with a chloride gradient (24 mM internal and 156 mM external [Cl ]), we found that instead of an expected outward rectified I-V curve due to this imposed concentration gradient, the observed I-V relationship shows significant inward rectification (Fig. 4 A). Login to comment
124 We next adopted the similar strategy used in Liu et al. (42) to test if A107C-CFTR can be modulated with baths of different pH. Login to comment
125 In Fig. 4 B, A107C-CFTR channel currents were first activated with forskolin in the bath solution with a pH of 7.4; after the current level stabilized, the bath was switched to forskolin-containing solution with a pH of 6 or 8. Login to comment
143 FIGURE 4 Effects of external MTSES and pH on A107C-CFTR. Login to comment
144 (A) Whole-cell A107C-CFTR currents in response to external MTSES (left) and I-V curves extracted from the whole-cell recording as marked. Login to comment
145 (B) Effects of acidic or alkaline pH on the whole-cell A107C-CFTR currents (left). Login to comment