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Cardiac Myosin Heavy Chain - Crossref

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Last Updated: 16 August 2022

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α-Cardiac-like myosin heavy chain as an intermediate between MHCIIa and MHCIβ in transforming rabbit muscle

To clarify the sequence of myosin heavy chain shifts in fast-to-slow transforming rabbit muscle, a direct reverse transcriptase-polymerase chain reaction was used to determine mRNAs specific to five MHC isoforms in single fibers from control and low-frequency stimulation of tibialis anterior muscles. MHCIIa, + MHCIIa, + MHCIIa, MHCIIa+ MHCIIa, MHCIIa + MHCIIa, MHCIIa+ MHCIIa + MHCIIa + MHCIIa + MHCIIa + MHCIIa, MHCIIa+ MHCIIa + MHCIIa + MHCIIa + MHCIIa + MHCIIa + MHCIIa + MHCIIa + MHCIIa+ MHCIIa + MHCIIa + MHCIIa + MHCIIa + MHCIIa+ MHCIIa + MHCIIa + MHCI.

Source link: https://doi.org/10.1152/ajpcell.1998.274.3.c595


An α-cardiac myosin heavy chain gene mutation impairs contraction and relaxation function of cardiac myocytes

Myocytes in comparison to WT myocytes had fewer type I cells and more type III cells than those in type III. In mutant cells, contraction was depressed in mutant cells, but not in type II and III cells than in type I cells. The depressability of relaxation was also depressed in type II and III cells more than in type I cells. We found that the amplitude of the Ca 2+ signal during contraction was unchanged in u03b1-MHC 403+ myocytes, but that the time required for decay of the signal to decrease 70% from its maximum was long shortened dramatically. The altered cardiac function of u03b1-MHC 403/+ myocytes is primarily due to defective myocyte function rather than to second-order global cardiac function and/or loading conditions, according to these results.

Source link: https://doi.org/10.1152/ajpheart.1999.276.5.h1780


Cardiac myosin heavy chains lacking the light chain binding domain cause hypertrophic cardiomyopathy in mice

More than 40 researchers missed significant mutations in the cardiac myosin heavy chain gene and several variations in the two myosin light chains, leading to a prevalently inherited heart disease called familial hypertrophic cardiomyopathy. We tested the likelihood that such a mutant MHC would occur as a dominant mutation in cardiac muscle by the removal of the light chain binding domain in MHC's lever arm but not its catalytic function. After flash photolysis of diazo 2, skinned myocytes and multicellular preparations from transgenic hearts displayed reduced Ca 2+ sensitivity and reduced relaxation rates.

Source link: https://doi.org/10.1152/ajpheart.1999.276.6.h2148


Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species

In eight mammalian species, a protocol for sample preparation and gel electrophoresis is described as demonstrating reproducible results in the separation of cardiac myosin heavy chain u03b1- and u03b2-isoforms. MHC isoforms were detected in samples at least 1 gram of urine at least 1 u03bcg. The protocol's sensitivity is sufficient for the detection of MHC isoforms in samples that are not as small as 1 u03bcg. In myocardial samples from different species, the glycerol level in the separation gel is a key factor for successfully distinguishing MHC-u03b1 and MHC-u03b2. The effect of sample load on MHC-u03b1 and MHC-u03b2 band resolutions is shown. The inclusion of a homogenization step during sample preparation has also increased the amount of MHC detected on the gel for cardiac samples to a much higher degree than on skeletal muscle samples.

Source link: https://doi.org/10.1152/ajpheart.1998.274.3.h1048


Double heterozygosity for mutations in the β-myosin heavy chain and in the cardiac myosin binding protein C genes in a family with hypertrophic cardiomyopathy

With the u03b2-myosin heavy chain and the cardiac myosin binding protein C genes being the most prevalent, seven genes have been identified with the disease so far, with the u03b2-myosin heavy chain and the cardiac myosin binding protein C genes being the most prevalent. In 15 people with hypertrophic cardiomyopathy from a French Caribbean family, we performed electrocardiography and echocardiography. Genetic analyses of genomic DNA were performed on genomic DNA by haplotype analysis with microsatellite markers at each locus involved and mutation testing by single strand conformation polymorphism analysis. Two new mutations cosegregating with the disease were discovered, one in the MYH7 gene exon 15 and the other in the MYBPC3 gene exon 30. Both patients were MYH7 gene mutation, two MYBPC3 gene mutations, and two were doubly heterozygous for the two mutations. We reveal for the first time the simultaneous occurrence of two pathological mutations in two separate genes in the context of familial hypertrophic cardiomyopathy.

Source link: https://doi.org/10.1136/jmg.36.7.542

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions