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Chemical Compound Review

Altritan     1,2,4,5-tetrachloro-3-nitro- benzene

Synonyms: Hickstor, Tecnazen, Teknazen, Easytec, Fusarex, ...
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Disease relevance of Myfusan


High impact information on Myfusan

  • Additional isoforms, including products of tropomyosin, myosin light chain 1 fast, troponin T, titin, and nebulin genes, can be generated from the same gene through alternative splicing or use of alternative promoters [6].
  • A physiological role for titin and nebulin in skeletal muscle [7].
  • Titin and/or nebulin apparently provide axial continuity for the production of resting tension on stretch and also tend to keep the thick filaments centred within the sarcomere during force generation [7].
  • The amino acid sequence that is predicted from this portion of the DMD gene indicates that the protein product might serve a structural role in muscle, but the abundance and tissue distribution of the messenger RNA suggests that the DMD protein is not nebulin [8].
  • The mechanisms responsible for specifying the characteristic filament lengths in these systems are more elusive and may include strict control of the relative amounts of actin filament capping proteins and side-binding proteins, molecular templates (e.g. tropomyosin and nebulin) and/or verniers (e.g. tropomyosin) [9].

Chemical compound and disease context of Myfusan


Biological context of Myfusan


Anatomical context of Myfusan

  • None of the tagged nebulin fragments behaved as dominant negatives; they neither blocked the assembly nor induced the disassembly of mature striated myofibrils [15].
  • Considering that cardiac muscle lacks nebulin, it is very likely that these elastic filaments were composed predominantly of connectin molecules; indeed, anti-connectin monoclonal antibody specifically stained these elastic filaments [16].
  • Immunoblot analysis indicates that although polypeptides of similar size are present in cardiac and smooth muscles at low abundance, those proteins show no immunological cross-reactivity with skeletal muscle nebulin [17].
  • When the thin filaments were depolymerized with latrunculin B, myocytes with decreased nebulin levels reassembled them to unrestricted lengths, demonstrating its importance in length specification [11].
  • A monospecific antibody has been used to localize nebulin by immunoelectron microscopy in a mechanically split rabbit psoas muscle fiber preparation [17].

Associations of Myfusan with other chemical compounds

  • The C-terminal regions of nebulin and nebulette are identical in domain organization and share a family of highly related C-terminal repeats, a serine-rich domain with potential phosphorylation sites, and an SH3 domain [18].
  • Furthermore, the association of nebulin modules with the actin N-terminus in subdomain 1 supports the hypothesis that nebulin wraps around the outer edges of actin filaments where Sl, tropomyosin, and several actin binding proteins are known to interact [19].
  • After Triton X-100 permeabilization and high ionic strength extraction, the giant protein nebulin was found to be still present as a myofibrillar component [20].
  • We have employed the strategy of using ethyl methane sulfonate and taxol to perturb myofibril assembly to examine interactions critical for the addition of nebulin to the developing sarcomeres [21].
  • When chicken breast muscle myofibrils were treated with a solution containing 0.1 mM CaCl2 and 30 micrograms of leupeptin/ml, nebulin filaments were fragmented into 200-, 180-, 40-, 33-, and 23-kDa subfragments [22].

Gene context of Myfusan


Analytical, diagnostic and therapeutic context of Myfusan

  • SDS PAGE indicated that the residues consisted mainly of titin, nebulin, and variable amounts of residual myosin and actin [28].
  • mAbs specific for titin or nebulin were characterized by immunoblotting and fluorescence microscopy [29].
  • Immunofluorescence studies with antibodies specific to the C-terminal region of nebulin indicate that the mutations may cause protein truncation possibly associated with loss of fiber-type diversity, which may be relevant to disease pathogenesis [3].
  • We have used electron microscopy and a novel method of helical image analysis to characterize complexes of F-actin with a nebulin fragment [30].
  • A 28-mer overlapping motif-containing PEVK module binds to nebulin SH3 in and around the canonical cleft, especially to the acidic residues in the loops, as revealed by NMR titration [31].


  1. Is nebulin the defective gene product in Duchenne muscular dystrophy? Wood, D.S., Zeviani, M., Prelle, A., Bonilla, E., Salviati, G., Miranda, A.F., DiMauro, S., Rowland, L.P. N. Engl. J. Med. (1987) [Pubmed]
  2. Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. Bang, M.L., Li, X., Littlefield, R., Bremner, S., Thor, A., Knowlton, K.U., Lieber, R.L., Chen, J. J. Cell Biol. (2006) [Pubmed]
  3. Mutations in the nebulin gene associated with autosomal recessive nemaline myopathy. Pelin, K., Hilpelä, P., Donner, K., Sewry, C., Akkari, P.A., Wilton, S.D., Wattanasirichaigoon, D., Bang, M.L., Centner, T., Hanefeld, F., Odent, S., Fardeau, M., Urtizberea, J.A., Muntoni, F., Dubowitz, V., Beggs, A.H., Laing, N.G., Labeit, S., de la Chapelle, A., Wallgren-Pettersson, C. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  4. Characterization of control and immobilized skeletal muscle: an overview from genetic engineering. St-Amand, J., Okamura, K., Matsumoto, K., Shimizu, S., Sogawa, Y. FASEB J. (2001) [Pubmed]
  5. Nebulin as an actin zipper. A two-module nebulin fragment promotes actin nucleation and stabilizes actin filaments. Chen, M.J., Shih, C.L., Wang, K. J. Biol. Chem. (1993) [Pubmed]
  6. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Schiaffino, S., Reggiani, C. Physiol. Rev. (1996) [Pubmed]
  7. A physiological role for titin and nebulin in skeletal muscle. Horowits, R., Kempner, E.S., Bisher, M.E., Podolsky, R.J. Nature (1986) [Pubmed]
  8. Conservation of the Duchenne muscular dystrophy gene in mice and humans. Hoffman, E.P., Monaco, A.P., Feener, C.C., Kunkel, L.M. Science (1987) [Pubmed]
  9. Regulation of actin filament length in erythrocytes and striated muscle. Fowler, V.M. Curr. Opin. Cell Biol. (1996) [Pubmed]
  10. Expression and purification of large nebulin fragments and their interaction with actin. Zhang, J.Q., Weisberg, A., Horowits, R. Biophys. J. (1998) [Pubmed]
  11. Nebulin regulates the assembly and lengths of the thin filaments in striated muscle. McElhinny, A.S., Schwach, C., Valichnac, M., Mount-Patrick, S., Gregorio, C.C. J. Cell Biol. (2005) [Pubmed]
  12. Nebulin, a helical actin binding protein. Pfuhl, M., Winder, S.J., Pastore, A. EMBO J. (1994) [Pubmed]
  13. The utrophin actin-binding domain binds F-actin in two different modes: implications for the spectrin superfamily of proteins. Galkin, V.E., Orlova, A., VanLoock, M.S., Rybakova, I.N., Ervasti, J.M., Egelman, E.H. J. Cell Biol. (2002) [Pubmed]
  14. Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. Witt, C.C., Burkart, C., Labeit, D., McNabb, M., Wu, Y., Granzier, H., Labeit, S. EMBO J. (2006) [Pubmed]
  15. Distinct families of Z-line targeting modules in the COOH-terminal region of nebulin. Ojima, K., Lin, Z.X., Bang, M., Holtzer, S., Matsuda, R., Labeit, S., Sweeney, H.L., Holtzer, H. J. Cell Biol. (2000) [Pubmed]
  16. Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments. Funatsu, T., Kono, E., Higuchi, H., Kimura, S., Ishiwata, S., Yoshioka, T., Maruyama, K., Tsukita, S. J. Cell Biol. (1993) [Pubmed]
  17. Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. Wang, K., Wright, J. J. Cell Biol. (1988) [Pubmed]
  18. Characterization of nebulette and nebulin and emerging concepts of their roles for vertebrate Z-discs. Millevoi, S., Trombitas, K., Kolmerer, B., Kostin, S., Schaper, J., Pelin, K., Granzier, H., Labeit, S. J. Mol. Biol. (1998) [Pubmed]
  19. Molecular contacts between nebulin and actin: cross-linking of nebulin modules to the N-terminus of actin. Shih, C.L., Chen, M.J., Linse, K., Wang, K. Biochemistry (1997) [Pubmed]
  20. Exogenous gelsolin binds to sarcomeric thin filaments without severing. Gonsior, S., Hinssen, H. Cell Motil. Cytoskeleton (1995) [Pubmed]
  21. Assembly of nebulin into the sarcomeres of avian skeletal muscle. Moncman, C.L., Wang, K. Cell Motil. Cytoskeleton (1996) [Pubmed]
  22. Calcium-induced fragmentation of skeletal muscle nebulin filaments. Tatsumi, R., Takahashi, K. J. Biochem. (1992) [Pubmed]
  23. Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly. Fürst, D.O., Osborn, M., Weber, K. J. Cell Biol. (1989) [Pubmed]
  24. Gene expression profiling in dysferlinopathies using a dedicated muscle microarray. Campanaro, S., Romualdi, C., Fanin, M., Celegato, B., Pacchioni, B., Trevisan, S., Laveder, P., De Pittà, C., Pegoraro, E., Hayashi, Y.K., Valle, G., Angelini, C., Lanfranchi, G. Hum. Mol. Genet. (2002) [Pubmed]
  25. Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms. Ilkovski, B., Nowak, K.J., Domazetovska, A., Maxwell, A.L., Clement, S., Davies, K.E., Laing, N.G., North, K.N., Cooper, S.T. Hum. Mol. Genet. (2004) [Pubmed]
  26. The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments. McElhinny, A.S., Kolmerer, B., Fowler, V.M., Labeit, S., Gregorio, C.C. J. Biol. Chem. (2001) [Pubmed]
  27. Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. Bang, M.L., Mudry, R.E., McElhinny, A.S., Trombitás, K., Geach, A.J., Yamasaki, R., Sorimachi, H., Granzier, H., Gregorio, C.C., Labeit, S. J. Cell Biol. (2001) [Pubmed]
  28. A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle. Wang, K., Ramirez-Mitchell, R. J. Cell Biol. (1983) [Pubmed]
  29. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. Fürst, D.O., Osborn, M., Nave, R., Weber, K. J. Cell Biol. (1988) [Pubmed]
  30. Each actin subunit has three nebulin binding sites: implications for steric blocking. Lukoyanova, N., VanLoock, M.S., Orlova, A., Galkin, V.E., Wang, K., Egelman, E.H. Curr. Biol. (2002) [Pubmed]
  31. Titin as a Giant Scaffold for Integrating Stress and Src Homology Domain 3-mediated Signaling Pathways: THE CLUSTERING OF NOVEL OVERLAP LIGAND MOTIFS IN THE ELASTIC PEVK SEGMENT. Ma, K., Forbes, J.G., Gutierrez-Cruz, G., Wang, K. J. Biol. Chem. (2006) [Pubmed]
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