| Literature DB >> 29730419 |
Hua Wei1, Xiao-Hua Zhang1, Cassandra Clift1, Naohiro Yamaguchi2, Martin Morad3.
Abstract
Type-2 ryanodine receptors (RyR2s) play a pivotal role in cardiac excitation-contraction coupling by releasing Ca2+ from sarcoplasmic reticulum (SR) via a Ca2+ -induced Ca2+ release (CICR) mechanism. Two strategies have been used to study the structure-function characteristics of RyR2 and its disease associated mutations: (1) heterologous cell expression of the recombinant mutant RyR2s, and (2) knock-in mouse models harboring RyR2 point mutations. Here, we establish an alternative approach where Ca2+ signaling aberrancy caused by the RyR2 mutation is studied in human cardiomyocytes with robust CICR mechanism. Specifically, we introduce point mutations in wild-type RYR2 of human induced pluripotent stem cells (hiPSCs) by CRISPR/Cas9 gene editing, and then differentiate them into cardiomyocytes. To verify the reliability of this approach, we introduced the same disease-associated RyR2 mutation, F2483I, which was studied by us in hiPSC-derived cardiomyocytes (hiPSC-CMs) from a patient biopsy. The gene-edited F2483I hiPSC-CMs exhibited longer and wandering Ca2+ sparks, elevated diastolic Ca2+ leaks, and smaller SR Ca2+ stores, like those of patient-derived cells. Our CRISPR/Cas9 gene editing approach validated the feasibility of creating myocytes expressing the various RyR2 mutants, making comparative mechanistic analysis and pharmacotherapeutic approaches for RyR2 pathologies possible.Entities:
Keywords: CPVT; CRISPR/Cas9; Human induced pluripotent stem cells; Ryanodine receptor mutation
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Year: 2018 PMID: 29730419 PMCID: PMC5993620 DOI: 10.1016/j.ceca.2018.04.009
Source DB: PubMed Journal: Cell Calcium ISSN: 0143-4160 Impact factor: 6.817