How do MYBPC3 mutations cause hypertrophic cardiomyopathy?
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How do MYBPC3 mutations cause hypertrophic cardiomyopathy? / Marston, Steven; Copeland, O'Neal; Gehmlich, Katja; Schlossarek, Saskia; Carrier, Lucie.
in: J MUSCLE RES CELL M, Jahrgang 33, Nr. 1, 1, 2012, S. 75-80.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - How do MYBPC3 mutations cause hypertrophic cardiomyopathy?
AU - Marston, Steven
AU - Copeland, O'Neal
AU - Gehmlich, Katja
AU - Schlossarek, Saskia
AU - Carrier, Lucie
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
M3 - SCORING: Journal article
VL - 33
SP - 75
EP - 80
JO - J MUSCLE RES CELL M
JF - J MUSCLE RES CELL M
SN - 0142-4319
IS - 1
M1 - 1
ER -
