A novel mutation in the HCN4 gene causes symptomatic sinus bradycardia in Moroccan Jews - PubMed
Case Reports
A novel mutation in the HCN4 gene causes symptomatic sinus bradycardia in Moroccan Jews
Avishag Laish-Farkash et al. J Cardiovasc Electrophysiol. 2010 Dec.
Abstract
Objectives: to conduct a clinical, genetic, and functional analysis of 3 unrelated families with familial sinus bradycardia (FSB).
Background: mutations in the hyperpolarization-activated nucleotide-gated channel (HCN4) are known to be associated with FSB.
Methods and results: three males of Moroccan Jewish descent were hospitalized: 1 survived an out-of-hospital cardiac arrest and 2 presented with weakness and presyncopal events. All 3 had significant sinus bradycardia, also found in other first-degree relatives, with a segregation suggesting autosomal-dominant inheritance. All had normal response to exercise and normal heart structure. Sequencing of the HCN4 gene in all patients revealed a C to T transition at nucleotide position 1,454, which resulted in an alanine to valine change (A485V) in the ion channel pore found in most of their bradycardiac relatives, but not in 150 controls. Functional expression of the mutated ion channel in Xenopus oocytes and in human embryonic kidney 293 cells revealed profoundly reduced function and synthesis of the mutant channel compared to wild-type.
Conclusions: we describe a new mutation in the HCN4 gene causing symptomatic FSB in 3 unrelated individuals of similar ethnic background that may indicate unexplained FSB in this ethnic group. This profound functional defect is consistent with the symptomatic phenotype.
Figures

A–C. Family trees suggesting autosomal-dominant inheritance. Solid symbols represent affected family members. Open symbols indicate family members not carrying the mutant gene. Gray symbols represent patients whose clinical and genetic status is unknown. (Patients A-III-11, H-II-4, V-I-2, V-II-4, and V-II-5 were considered affected based only on a history of bradycardia without genetic screening due to lack of cooperation. Patients A-I-2 and A-I-6 died at 28y from unknown causes). D. This chart compares age with heart rate of carrier- and noncarrier family members. It demonstrates clear separation of two groups: affected and nonaffected family members, regarding minimal and mean heart rate on Holter recordings, independently of patient age. Low heart rate segregates near completely with positive genotype. Two exceptions are discussed in the text. Family member A-II-9 was not included in the graph due to technically unreadable Holter recordings. She was asymptomatic and was found to be a noncarrier.

A. Top: In this patient a C to T heterozygote change resulted in an alanine to valine amino acid change in position 485. Bottom: Control showing normal sequence. B. Multiple alignment of the A485V mutation region, showing the conserved alanine in position 485 in 3 different species (human, rat and mouse). The multiple alignment was done using the ClustalW software.

Expression of HCN4 wild-type, HCN4 A485V homotetramer and HCN4 WT/A485V heterotetramer in Xenopus oocytes. A. Currents recorded from oocytes injected with RNAs of HCN4 WT, A485V, or WT and A485V together. The extracellular solution contained 24 mM K+. B. Enlargement of traces of WT tail currents shown in A, recorded during the voltage step to 30 mV. Right, the voltage protocol. Holding potential was −40 mV and currents were elicited by 5-s hyperpolarizing voltage steps between −30 and −130 mV in 10-mV increments, followed by a 3-s step to 30 mV. C. I–V relationship of WT (full circles, n=4), A485V (empty circles, n=4) and HCN4 WT/A485V (full reverse triangles, n=4) channels, recorded at the end of the voltage steps between −30 and −130 mV. D. Reversal potential measurement of the HCN4 currents of WT (full circles, n=4) and A485V (empty circles, n=3). The measurement shows tail current amplitude at the indicated voltages after a 5-second pre-pulse to −130 mV. (*P<0.05, same results obtained in two additional experiments).

Comparison between HCN4 channels with A485V and G480R point mutations expressed in Xenopus oocytes. The currents of the HCN4 WT and homotetramer mutants were recorded in two separate experiments. The graph compares the currents of WT HCN4 (black, n=4) and A485V homozygote (red, n=4) to the currents of WT HCN4 (green, n=5) and G480R homozygote (yellow, n=4) at −80 mV, as well as at −120 mV. At −120 mV, the current of the homozygote mutants relative to the WT at the same experiment is 2.5 % and 20 % for A485V and G480R, respectively. (* P<0.05, **P<0.01,***P<0.001).

Expression of HCN4 WT and HCN4 A485V homotetramers in HEK293T cells. A, Western blot of total protein using anti-HCN4 (top) or anti-Calnexin (bottom) antibodies in WT HCN4 transfected HEK293T cells, A485V HCN4 transfected cells and pCDNA3 transfected cells. Blot exposure time was 1 min. The area of each band was estimated using the Scion software, and was estimated as following: 11356 and 5716 for total HCN4 WT (*) and total A485V HCN4 (**), respectively. B, Currents recorded from cells transfected with DNA of HCN4 WT (n=4) or A485V (n=5). The extracellular solution contained 54 mM Na+ and 90 mM K+. Right, voltage protocol. Holding potential was −10 mV and currents were elicited by 5-s hyperpolarizing voltage steps between 0 and −140 mV in 20-mV increments.
Comment in
-
The slow pace of the heart and the objectives of molecular cardiology.
Napolitano C. Napolitano C. J Cardiovasc Electrophysiol. 2010 Dec;21(12):1373-4. doi: 10.1111/j.1540-8167.2010.01879.x. Epub 2010 Aug 30. J Cardiovasc Electrophysiol. 2010. PMID: 20807277 No abstract available.
Similar articles
-
Nof E, Luria D, Brass D, Marek D, Lahat H, Reznik-Wolf H, Pras E, Dascal N, Eldar M, Glikson M. Nof E, et al. Circulation. 2007 Jul 31;116(5):463-70. doi: 10.1161/CIRCULATIONAHA.107.706887. Epub 2007 Jul 23. Circulation. 2007. PMID: 17646576
-
The slow pace of the heart and the objectives of molecular cardiology.
Napolitano C. Napolitano C. J Cardiovasc Electrophysiol. 2010 Dec;21(12):1373-4. doi: 10.1111/j.1540-8167.2010.01879.x. Epub 2010 Aug 30. J Cardiovasc Electrophysiol. 2010. PMID: 20807277 No abstract available.
-
Familial sinus bradycardia associated with a mutation in the cardiac pacemaker channel.
Milanesi R, Baruscotti M, Gnecchi-Ruscone T, DiFrancesco D. Milanesi R, et al. N Engl J Med. 2006 Jan 12;354(2):151-7. doi: 10.1056/NEJMoa052475. N Engl J Med. 2006. PMID: 16407510
-
Pacemaker channels and sinus node arrhythmia.
Stieber J, Hofmann F, Ludwig A. Stieber J, et al. Trends Cardiovasc Med. 2004 Jan;14(1):23-8. doi: 10.1016/j.tcm.2003.09.006. Trends Cardiovasc Med. 2004. PMID: 14720471 Review.
-
The Contribution of HCN4 to normal sinus node function in humans and animal models.
Nof E, Antzelevitch C, Glikson M. Nof E, et al. Pacing Clin Electrophysiol. 2010 Jan;33(1):100-6. doi: 10.1111/j.1540-8159.2009.02563.x. Epub 2009 Oct 1. Pacing Clin Electrophysiol. 2010. PMID: 19796353 Free PMC article. Review.
Cited by
-
Funny channel gene mutations associated with arrhythmias.
DiFrancesco D. DiFrancesco D. J Physiol. 2013 Sep 1;591(17):4117-24. doi: 10.1113/jphysiol.2013.253765. Epub 2013 Mar 18. J Physiol. 2013. PMID: 23507880 Free PMC article. Review.
-
An evolutionarily conserved pacemaker role for HCN ion channels in smooth muscle.
Yang L, Arbona RJR, Smith CS, Banks KM, Thomas VK, Palmer L, Evans T, Hurtado R. Yang L, et al. J Physiol. 2023 Apr;601(7):1225-1246. doi: 10.1113/JP283701. Epub 2023 Mar 17. J Physiol. 2023. PMID: 36930567 Free PMC article.
-
Characterization of drug binding within the HCN1 channel pore.
Tanguay J, Callahan KM, D'Avanzo N. Tanguay J, et al. Sci Rep. 2019 Jan 24;9(1):465. doi: 10.1038/s41598-018-37116-2. Sci Rep. 2019. PMID: 30679654 Free PMC article.
-
Keaney JJ, Groarke JD, Galvin Z, McGorrian C, McCann HA, Sugrue D, Keelan E, Galvin J, Blake G, Mahon NG, O'Neill J. Keaney JJ, et al. BMJ. 2013 Dec 12;347:f6627. doi: 10.1136/bmj.f6627. BMJ. 2013. PMID: 24336304 Free PMC article.
-
Biology of the Sinus Node and its Disease.
Choudhury M, Boyett MR, Morris GM. Choudhury M, et al. Arrhythm Electrophysiol Rev. 2015 May;4(1):28-34. doi: 10.15420/aer.2015.4.1.28. Epub 2015 May 30. Arrhythm Electrophysiol Rev. 2015. PMID: 26835096 Free PMC article.
References
-
- DiFrancesco D, Tortora P. Direct activation of cardiac pacemaker channels by intracellular cyclic AMP. Nature. 1991;351:145–147. - PubMed
-
- DiFrancesco D. Pacemaker mechanisms in cardiac tissue. Annu Rev Physiol. 1993;55:455–472. - PubMed
-
- Baruscotti M, Bucchi A, DiFrancesco D. Physiology and pharmacology of the cardiac pacemaker (“funny”) current. Pharmacol Ther. 2005;107:59–79. - PubMed
-
- Ludwig A, Zong X, Jeglitsch M, Hofmann F, Biel M. A family of hyperpolarization-activated mammalian cation channels. Nature. 1998;393(6685):587–91. - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases