Myosin heavy

NFAT proteins are expressed in skeletal, cardiac, and smooth muscle and play important roles in the regulation of the development and differentiation of these tissues. In skeletal muscle, NFAT isoforms are expressed at different stages of development and regulate progression from early muscle cell precursors to mature myocytes. NFAT proteins have also been shown to control the expression of the myosin heavy chain and positively regulate muscle growth [1, 2]. 

Nonmuscle/smooth muscle myosins-Il are structurally similar to striated muscle myosin-II, but they have slower rates of ATP hydrolysis than do their striated muscle counterparts. Nonmuscle/smooth muscle myosin-II is also regulated differently than striated muscle myosin-II. Nonmuscle myosin-II is divided into the invertebrate and vertebrate branches (Cheney et al., 1993). This group is ubiquitous because it is present in most lower organisms, such as slime molds, amoeba, sea urchins, etc., and in virtually all mammalian nonmuscle cells. Smooth muscle myosin-II is also somewhat heterogeneous in that at least three separate forms of smooth muscle heavy chains, with molecular weights of 196,000, 200,000, and 204,000 have been identified (Kawamoto and Adelstein, 1987). The physiological properties of these separate myosin heavy chains are not yet known. 

De Lozanne, A. Spudich, J.A. (1987). Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236, 1086-1091. 

Geisterfer-Lowrance, A.A., Kass, S., Tanigawa, G., Vosberg, H.-P., McKenna, W., Seidman, C.E., Seidman, J.G. (1990). A molecular basis for familial hypertrophic cardiomyopathy a p-cardiac myosin heavy chain gene missense mutation. Cell 62, 999-1006,... 

Kawamoto, S. Adelstein, R.S. (1987), Characterization of myosin heavy chains in cultured aorta smooth muscle cells. A comparative study. J. Biol. Chem. 262, 7282-7288. 

Knecht, D.A., Loomis, W.F. (1987). Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science 236, 1081-1086. 

The crystal structure of myosin S-1 shows how the three subdomains (20K, 50K and 27K) of the myosin heavy chain (produced by further enzymatic digestion of... 

Abnormalities of myocardial contractile and structural proteins P-Myosin heavy chains, troponin, tropomyosin, dystrophin... 

Mutations in the Cardiac (i-Myosin Heavy Chain Gene Are One Cause of Familial Hypertrophic Cardiomyopathy... 

Figure 49-13. Simplified scheme of the causation of familial hypertrophic cardiomyopathy (MIM 192600) due to mutations in the gene encoding fi-myosin heavy chain. Mutations in genes encoding other proteins, such as the troponins, tropomyosin, and cardiac myosin-binding protein C can also cause this condition. Mutations in genes encoding yet other proteins (eg, dystrophin) are involved in the causation of dilated cardiomyopathy.

Some cases of famifial hypertrophic cardiomyopathy are due to missense mutations in the gene coding for p-myosin heavy chain. 

W - Dominant spotting SI = Steel a = nonagouti, d = dilute c - albino , p = pink-eyed dilution MHC = myosin heavy chain. 

Mercer, J. A., Seperack, P. K., Strobel, M. C Copeland, N. G., and Jenkins, N. A. (1991). Novel myosin heavy chain encoded by murine dilute coat colour locus. Nature 349 709-713. 

Liu P, Hajra A et al. Fusion between transcription factor CBF beta/PEBP2 beta and a myosin heavy chain in acute myeloid leukemia. Science 1993 261 1041-1044. 

Because myoepithelial cells are not always readily identifiable on routine hematoxylin- and eosin-stained sections, many immunohistochemical methods have been used to highlight an intact myoepithelial cells layer. Recent studies have reported CD10 and smooth muscle myosin heavy chain (SMMHC) expression in... 

Kalof AN, Tam D, Beatty B, Cooper K (2004) Immunostaining patterns of myoepithelial cells in breast lesions a comparison of CD10 and smooth muscle myosin heavy chain. J Clin Pathol 57 625 629... 

Li X, Zhou L, and Gorodeski GI [2006] Estrogen regulates epithelial cell deformability by modulation of cortical acto-myosin through phosphorylation of non-muscle myosin-heavy-chain II-B filaments. Endocrinology 147 5236-5248... 

Itoh K and Adelstein RS [1995] Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B. J Biol Chem 270 14533-14540... 

Shohet RV, Conti MA, Kawamoto S, Preston YA, Brill DA, and Adelstein RS [1989] Cloning of the cDNA encoding the myosin heavy chain of a vertebrate cellular myosin. Proc Natl Acad Sci USA 86 7726-7730... 

Simon H-G, Oppenheimer S. 1996. Advanced mRNA differential display isolation of a new differentially regulated myosin heavy chain-encoding gene in amphibian limb regeneration. Gene 172 175. 

Voluntary muscles contain a variety of fibre types which are specialized for particular tasks. Most muscles contain a mixture of fibre types although one type may predominate. All human skeletal muscles are composed of several different muscle fibre types. Up to seven different fibre types have been identified histochemically based on the pH stability of myofibrillar adenosine triphosphatase and on the myosin heavy chain profile. Innumerable fibre type transients exist due to continuing adaptation processes. However, three main... 

Immunohistochemical analyses were performed using antibodies recognizing smooth muscle actin (SMA), troponin-T (Trop-T), troponin T-C (Trop T-C), myosin heavy chain (MHC), muscle actin (MA), a-actinin, a-SR-1, desmin, connexin-43, fibroblasts (all antibodies from Dako, Denmark). For fluorescent immunohistochemistry the AlexaFluor 594 goat anti mouse secondary antibody (Molecular Probes, Leiden, The Netherlands) was used. In addition, cell nuclei were stained using DAPI. 

Durst, KL., Lutterbach, B., Kummalue, T., Friedman, A.D. and Hiehert, S.W. (2003) The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain. Molecular and Cellular Biology, 23, 607-619. 

A modified version of the ECVAM-approved embryonic stem cell test (EST) (52) was recently developed by Hunter and coworkers in NHEERL (31). This assay is capable of quantitatively assessing cytotoxicity and cardiomyocyte differentiation and was used to test the ToxCast Phase I chemical library (32). Briefly, male murine J1 mES cells were seeded onto gelatin-coated 96-well plates at a known density in differentiation media on day 0. On day 1, cells were treated with chemicals ranging from 0.0125 to 12.5 pM, and on day 9 In-Cell Western (Li-Cor Biosciences) assays were assayed for a- and P-cardiac Myosin Heavy Chain (MYH6/MYH7)... 

Gallus gallus (two myosin heavy-chain kinases a Ca /calmodulin dependent and a Ca /calmodulin independent enzyme [10,11] the Ca /cal-modulin dependent heavy chain kinase has several properties in common with the family of type II calmodulin-dependent protein kinases [11]) [10,... 

---