Novel KCNA5 mutation implicates tyrosine kinase signaling in human atrial fibrillation - PubMed (original) (raw)
Novel KCNA5 mutation implicates tyrosine kinase signaling in human atrial fibrillation
Tao Yang et al. Heart Rhythm. 2010 Sep.
Abstract
Background: Emerging evidence has strongly implicated hereditary determinants for atrial fibrillation (AF). Loss-of-function mutations in KCNA5 encoding the ultrarapid delayed rectifier potassium current I(Kur) have been identified in AF families.
Objective: The purpose of this study was to determine the clinical and biophysical phenotypes in a KCNA5 mutation with deletion of 11 amino acids in the N-terminus of the protein, which was identified in patients with lone AF.
Methods: Patients with AF confirmed by ECG were prospectively enrolled in the Vanderbilt AF Registry, which comprises clinical and genetic databases. A KCNA5 mutation was generated by mutagenesis for electrophysiologic characterization.
Results: We identified a novel 33-bp coding region deletion in two Caucasian probands. One proband was part of a kindred that included four other members with AF, and all were mutation carriers. The mutation results in deletion of 11 amino acids in the N-terminus of the protein, a proline-rich region as a binding site for Src homology 3 (SH3) domains associated with Src-family protein tyrosine kinase (TK) pathway. In transfected cells, the mutant caused approximately 60% decreased I(Kur) versus wild-type (WT) (75 +/- 8 pA/pF vs 180 +/- 15 pA/pF, P <.01) and dominant-negative effect on WT current (105 +/- 10 pA/pF, P <.01). Pretreatment with the Src inhibitor PP2 prevented v-Src TK from 90% suppressed WT current. In contrast, the mutant channel displayed no response to v-Src TK.
Conclusion: Our data implicate abnormal atrial repolarization control due to variable TK signaling as a mechanism in familial AF and thereby suggest a role for modulation of this pathway in AF and its treatment.
Keywords: KCNA5 channel; familial atrial fibrillation; genetics; tyrosine kinase; variants.
Copyright 2010 Heart Rhythm Society. Published by Elsevier Inc. All rights reserved.
Figures
Figure 1
A, family pedigree of Vanderbilt AF 579. Solid symbols denote AF, and open symbols individuals without a documented history of AF. Male subjects are shown as squares and female subjects as circles. The proband (arrow) and the presence (+) or absence (−) of the KCNA5 71-81del are indicated. B, location of the indel in the KCNA5 protein and a portion of the KCNA5 N-terminus amino acid showing the indel mutant sequence in red.
Figure 2
The 71-81del in the N-terminus of KCNA5 expressed a reduced current. Panels A, B and C show wild-type (WT), the 71-81del and the WT+71-81 del currents respectively with a dominant negative effect. Panels D and E summarize both steady-state and tail currents in the three groups.
Figure 3
A tyrosine kinase (TK) isoform v-Src coexpressed with KCNA5 suppressed WT current but had no effect on the mutant 71-81del expressed current. A, WT current; B, coexpression of v-Src with WT KCNA5 channel reduced the current; C, 71-81del expressed reduced the current; D, the 71-81del fail to respond to v-Src; E, current-voltage relationships in the four groups.
Figure 4
Suppression of KCNA5 current by Src is prevented by the selective Src inhibitor PP2 (10 μM). A, intracellular addition of v-Src (30 u/ml) progressively suppressed WT KCNA5 current elicited by repetitive pulses to +50 mV from −80 mV with the protocol shown. B, intracellular Src application did not affect the 71-81del expressed current. C, effects of intracellular Src application on WT and the 71-81del currents. D, pretreatment with PP2 (10 μM) for 30 minutes prevented the intracellular Src-induced suppression of WT current. E, intracellular Src addition did not alter the 71-81del expressed current. F, effects of intracellular Src application on WT and 71-81del currents in the presence PP2 pretreatment. The number of cells in each group was 6. Statistical differences among these groups are shown.
Comment in
- Alteration of tyrosine kinase signaling: another player in the arrhythmogenesis of atrial fibrillation?
Shinlapawittayatorn K, Deschênes I. Shinlapawittayatorn K, et al. Heart Rhythm. 2010 Sep;7(9):1253-4. doi: 10.1016/j.hrthm.2010.06.021. Epub 2010 Jun 17. Heart Rhythm. 2010. PMID: 20601156 No abstract available.
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