Words similar to myosin
Example sentences for: myosin
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Myosin II is the conventional myosin, which was discovered 60 years ago [ 8].
Sixteen unique sequences were obtained that contain a myosin motor domain as identified by the SMART (Smart Modular Architecture Research Tool) program [ 56].
is expressed in skeletal muscle, with a less abundant ~7 kb transcript expressed in both skeletal and cardiac muscle [ 8 ] . Whereas tropomodulins or the Arp 2/3 complex cap the pointed end of actin filaments, the barbed end can be capped by CapZ, α, β, and γ adducins as well as gelsolin [ 9 10 11 ] . Control of thin filament length is critical for maintaining proper sarcomere function and length [ 12 ] . Inhibition of Tmod1's capping activity - either by using an antibody to its C-terminal end or by decreasing expression using an antisense Tmod1 transcript - results in elongated thin filaments and decreased cardiac contractility [ 13 14 ] . Tmod1 overexpression in rat cardiomyocytes causes shortening of the thin filaments and sarcomere disorganization, resulting in myofibril degeneration [ 14 ] . Likewise, mice overexpressing TMOD1 in the heart show disrupted sarcomere organization with shortened thin filaments, leading to myofibril degeneration and dilated cardiomyopathy [ 15 ] . Recently, Littlefield and colleagues showed that overexpression of GFP-Tmod1 in chick cardiac myocytes results in shortening of thin filaments; the authors proposed that excess Tmod1 decreases the affinity between actin monomers and pointed ends, leading to monomer dissociation and filament shortening [ 42 ] . Mutations in many proteins making up the cardiac sarcomere have been shown to cause cardiac hypertrophy [ 16 17 18 19 ] :mutations in the TPM1 gene, for example, cause type 3 familial hypertrophic cardiomyopathy (CMH3), and a transgenic mouse expressing a CMH3 mutation develops ventricular myocyte disarray and hypertrophy [ 20 ] . Mutations in myosin heavy chain 7 are estimated to account for 40-50% of the cases of hypertrophic cardiomyopathy [ 21 ] .
The pTX-MKC2 plasmid was therefore transfected into 3xALA myosin II cells, which are resistant to myosin filament hyperphosphorylation and disassembly due to elimination of phosphorylation target sites in the myosin tail [ 24 ] . The resultant 3xALA/pTX-MKC2 cells could be propagated in suspension culture even after selection for elevated expression in 40 μg/ml G418.
If FLAG-MHCK-C was not subjected to a pre-autophosphorylation step, 32P incorporation into the peptide displayed a similar lag phase as observed for myosin II phosphorylation (Figure 4Aand 4B, open symbols).