The Molecular Biology and Pathophysiology of Hypertrophic Cardiomyopathy Due to Mutations in the Beta Myosin Heavy Chains and the Essential and Regulatory Light Chains

1998 ◽  
pp. 105-115 ◽  
Author(s):  
Neal D. Epstein
Keyword(s):  
Hypertrophic Cardiomyopathy ◽  
Molecular Biology ◽  
Light Chains ◽  
Myosin Heavy Chains ◽  
Regulatory Light Chains ◽  
Heavy Chains

scholarly journals Relative synthesis of cardiac contractile proteins. Evidence for synthesis from the same precursor pool

1981 ◽  
Vol 194 (3) ◽  
pp. 673-678 ◽  
Author(s):  
C D Evans ◽  
S S Schreiber ◽  
M Oratz ◽  
M A Rothschild
Keyword(s):  
Light Chain ◽  
Contractile Proteins ◽  
Light Chains ◽  
Myosin Heavy Chains ◽  
Perfused Heart ◽  
Precursor Pool ◽  
Heavy Chains ◽  
Cardiac Contractile ◽  
Specific Activities ◽  
Cardiac Contractile Proteins

The relative molar synthesis of cardiac contractile proteins has been measured in the perfused heart under control haemodynamic conditions. This synthesis, of myosin heavy chains, individual light chains (1 and 2), actin and tropomyosin, was determined from isolated guinea-pig hearts perfused for 3h simultaneously with constant specific radioactivities and concentrations of [3H]lysine and [3H]phenylalanine.The data strongly suggest that all of the proteins studied were synthesized from the same precursor pools of lysine and phenylalanine, since the ratio of the specific activities of the two labels was the same in all of the proteins. Measurement of molar synthesis of each contractile protein was the same with either labelled amino acid. Under control haemodynamic-perfusion conditions, the relative molar synthesis of the contractile proteins was actin greater than heavy chains greater than light chain 2 greater than light chain 1 greater than tropomyosin.

Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains

1993 ◽  
Vol 127-128 (1) ◽  
pp. 219-227 ◽  
Author(s):  
Robabeh S. Moussavi ◽  
Christine A. Kelley ◽  
Robert S. Adelstein
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Light Chains ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Muscle Myosin

A Complete Absence of Missense Mutation in Myosin Regulatory and Essential Light Chain Genes of South Indian Hypertrophic and Dilated Cardiomyopathies

Cardiology ◽  
2018 ◽  
Vol 141 (3) ◽  
pp. 156-166
Author(s):  
Deepa Selvi Rani ◽  
Pratibha Nallari ◽  
Jhansi Rani ◽  
Sheikh Nizamuddin ◽  
Thulasamma Seelamneni ◽  
...  
Keyword(s):  
South India ◽  
Myosin Head ◽  
Light Chains ◽  
Healthy Controls ◽  
Missense Mutations ◽  
Regulatory Light Chains ◽  
Heavy Chains ◽  
Essential Light Chain ◽  
South Indian ◽  
First Time

Background: Myosin is a hexameric contractile protein composed of 2 heavy chains associated with 4 light chains of 2 distinct classes – 2 regulatory light chains (MYL2) and 2 essential light chains (MYL3). The myosin light chains stabilize the long alpha helical neck of the myosin head and regulate the myosin ATPase activities. Objectives: Mutations in MYL2 and MYL3 are reported to be associated with cardiomyopathies. However, there is no study available on these genes in Indian cardiomyopathies, and therefore we planned to study them. Method: For the first time we sequenced MYL2 and MYL3 genes in a total of 248 clinically well-characterized cardiomyopathies consisting of 101 hypertrophic and 147 dilated cases along with 207 healthy controls from south India. Results: Our study revealed a total of 10 variations – 7 in MYL2 and 3 in MYL3, of which 3 are novel variations observed exclusively in cases. However, the 15 causative missense mutations previously reported are totally absent in our study, which showed that the sequences of MYL2 and MYL3 are highly conserved in Indian cases/controls. Conclusions: MYL2 and MYL3 mutations are rare and the least cause of cardiomyopathies in Indians.

scholarly journals Allele-Specific Silencing of MutantMyh6Transcripts in Mice Suppresses Hypertrophic Cardiomyopathy

Science ◽  
2013 ◽  
Vol 342 (6154) ◽  
pp. 111-114 ◽  
Author(s):  
Jianming Jiang ◽  
Hiroko Wakimoto ◽  
J. G. Seidman ◽  
Christine E. Seidman
Keyword(s):  
Rna Interference ◽  
Hypertrophic Cardiomyopathy ◽  
Clinical Phenotype ◽  
Therapeutic Benefit ◽  
Myosin Heavy Chains ◽  
Specific Expression ◽  
Adeno Associated Virus ◽  
Heavy Chains ◽  
Allele Specific ◽  
Sarcomere Proteins

Dominant mutations in sarcomere proteins such as the myosin heavy chains (MHC) are the leading genetic causes of human hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy. We found that expression of the HCM-causing cardiac MHC gene (Myh6) R403Q mutation in mice can be selectively silenced by an RNA interference (RNAi) cassette delivered by an adeno-associated virus vector. RNAi-transduced MHC403/+mice developed neither hypertrophy nor myocardial fibrosis, the pathologic manifestations of HCM, for at least 6 months. Because inhibition of HCM was achieved by only a 25% reduction in the levels of the mutant transcripts, we suggest that the variable clinical phenotype in HCM patients reflects allele-specific expression and that partial silencing of mutant transcripts may have therapeutic benefit.

scholarly journals Epitopes of streptococcal M proteins shared with cardiac myosin.

1985 ◽  
Vol 162 (2) ◽  
pp. 583-591 ◽  
Author(s):  
J B Dale ◽  
E H Beachey
Keyword(s):  
Acute Rheumatic Fever ◽  
M Protein ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Poststreptococcal Glomerulonephritis ◽  
Heavy Chains ◽  
M Proteins ◽  
Group A

We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis.

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