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It is well established that MYBPC3 mutations are the most common cause of hypertrophic cardiomyopathy, accounting for about half of identified mutations. However, when compared with mutations in other myofibrillar proteins that cause hypertrophic cardiomyopathy, MYBPC3 mutations seem to be the odd one out. The most striking characteristic of HCM mutations in MYBPC3 is that many are within introns and are predicted to cause aberrant splicing leading to a frameshift and a premature chain termination, yet the truncated peptides have never been identified in human heart tissue carrying these mutations. Instead of expression of a poison peptide we consistently observe haploinsufficiency of MyBP-C in MYBPC3 mutant human heart muscle. In this review we investigate the mechanism for MyBP-C haploinsufficiency and consider how this haploinsufficiency could cause hypertrophic cardiomyopathy.

Original publication

DOI

10.1007/s10974-011-9268-3

Type

Journal article

Journal

J Muscle Res Cell Motil

Publication Date

05/2012

Volume

33

Pages

75 - 80

Keywords

Animals, Calcium, Cardiomyopathy, Hypertrophic, Carrier Proteins, Codon, Nonsense, Exons, Frameshift Mutation, Haploinsufficiency, Humans, Myocardium, Nonsense Mediated mRNA Decay, Peptide Chain Termination, Translational, RNA Splicing, RNA, Messenger