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Gene Review

DES  -  desmin

Gallus gallus

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High impact information on LOC395906


Biological context of LOC395906


Anatomical context of LOC395906

  • We conclude that desmin, perhaps in conjunction with actin, is responsible for interlinking Z discs of adjacent myofibrils, and may thus serve as a mechanical and structural integrator of muscle fibers [9].
  • Specificity of desmin to avian and mammalian muscle cells [10].
  • Desmin and vimentin may thus be involved in maintaining the lateral registration of sarcomeres by transversely linking adjacent myofibrils at their Z discs [3].
  • The data also suggest that in myoepithelial cells prekeratin filaments are arranged--and might function--in a manner similar to the desmin filaments in smooth muscle cells [11].
  • The distribution of the intermediate filament proteins vimentin and desmin in developing and mature myotubes in vivo was studied by single and double immunoelectron microscopic labeling of ultrathin frozen sections of iliotibialis muscle in 7-21-d-old chick embryos, and neonatal and 1-d-old postnatal chicks [12].

Associations of LOC395906 with chemical compounds

  • Gel filtration on Bio-Gel P300 in the presence of 1 M acetic acid reveals that the majority of desmin is monomeric under these conditions [13].
  • Embryonic chick heart cell cultures (permeabilized with Triton X-100) and enucleated adult chicken erythrocyte ghosts (Granger, B. L., E. A. Rapasky, and E. Lazarides, 1982, J. Cell Biol. 92:299-312) were then used for immunoelectronmicroscopic localization of desmin [7].
  • Gel filtration on Ultrogel AcA34 in the presence of 0.5% Sarkosyl NL-97 reveals nonmonomeric fractions of actin and desmin that comigrate through the column [13].
  • The inhibition in the accumulation of newly synthesized ankyrin, alpha-spectrin, and beta-spectrin in EGTA-treated myoblasts was not characteristic of all structural proteins, since the accumulation of the muscle-specific intermediate filament protein desmin was the same in control and fusion-blocked cells [14].
  • The definitive mononucleated myoblasts and multinucleated myotubes were identified by muscle-specific antibodies against light meromyosin or desmin, whereas the definitive chondroblasts were identified by a monoclonal antibody against the keratan sulfate chains of the cartilage-specific sulfated proteoglycan [15].

Regulatory relationships of LOC395906


Other interactions of LOC395906


Analytical, diagnostic and therapeutic context of LOC395906


  1. Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments. Geisler, N., Kaufmann, E., Weber, K. Cell (1982) [Pubmed]
  2. Phosphorylation of intermediate filament proteins by cAMP-dependent protein kinases. O'Connor, C.M., Gard, D.L., Lazarides, E. Cell (1981) [Pubmed]
  3. Desmin and vimentin coexist at the periphery of the myofibril Z disc. Granger, B.L., Lazarides, E. Cell (1979) [Pubmed]
  4. Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase A sites in the aminoterminal head domain. Geisler, N., Weber, K. EMBO J. (1988) [Pubmed]
  5. Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis. Schultheiss, T., Lin, Z.X., Ishikawa, H., Zamir, I., Stoeckert, C.J., Holtzer, H. J. Cell Biol. (1991) [Pubmed]
  6. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. Geisler, N., Weber, K. EMBO J. (1982) [Pubmed]
  7. Detection of desmin-containing intermediate filaments in cultured muscle and nonmuscle cells by immunoelectron microscopy. Ip, W., Danto, S.I., Fischman, D.A. J. Cell Biol. (1983) [Pubmed]
  8. Role of cell division in differentiation of myoblasts infected with a temperature-sensitive mutant of Rous sarcoma virus. Falcone, G., Boettiger, D., Alemà, S., Tatò, F. EMBO J. (1984) [Pubmed]
  9. The existence of an insoluble Z disc scaffold in chicken skeletal muscle. Granger, B.L., Lazarides, E. Cell (1978) [Pubmed]
  10. Specificity of desmin to avian and mammalian muscle cells. Lazarides, E., Balzer, D.R. Cell (1978) [Pubmed]
  11. Intermediate-sized filaments of the prekeratin type in myoepithelial cells. Franke, W.W., Schmid, E., Freudenstein, C., Appelhans, B., Osborn, M., Weber, K., Keenan, T.W. J. Cell Biol. (1980) [Pubmed]
  12. Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study. Tokuyasu, K.T., Maher, P.A., Singer, S.J. J. Cell Biol. (1985) [Pubmed]
  13. Copurification of actin and desmin from chicken smooth muscle and their copolymerization in vitro to intermediate filaments. Hubbard, B.D., Lazarides, E. J. Cell Biol. (1979) [Pubmed]
  14. Posttranslational control of membrane-skeleton (ankyrin and alpha beta-spectrin) assembly in early myogenesis. Nelson, W.J., Lazarides, E. J. Cell Biol. (1985) [Pubmed]
  15. Separation of precursor myogenic and chondrogenic cells in early limb bud mesenchyme by a monoclonal antibody. Sasse, J., Horwitz, A., Pacifici, M., Holtzer, H. J. Cell Biol. (1984) [Pubmed]
  16. Persistence of an embryonic intermediate filament-associated protein in the smooth muscle cells of elastic arteries and in Purkinje fibres. Vincent, M., Levasseur, S., Currie, R.W., Rogers, P.A. J. Mol. Cell. Cardiol. (1991) [Pubmed]
  17. The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison to the hamster gene. Zehner, Z.E., Li, Y., Roe, B.A., Paterson, B.M., Sax, C.M. J. Biol. Chem. (1987) [Pubmed]
  18. Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle. Tokuyasu, K.T., Dutton, A.H., Singer, S.J. J. Cell Biol. (1983) [Pubmed]
  19. Actin isoform compartments in chicken gizzard smooth muscle cells. North, A.J., Gimona, M., Lando, Z., Small, J.V. J. Cell. Sci. (1994) [Pubmed]
  20. Developmental change of protein constituents in chicken gizzards. Hirai, S., Hirabayashi, T. Dev. Biol. (1983) [Pubmed]
  21. Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle. Tokuyasu, K.T., Dutton, A.H., Singer, S.J. J. Cell Biol. (1983) [Pubmed]
  22. Visualization of longitudinally-oriented intermediate filaments in frozen sections of chicken cardiac muscle by a new staining method. Tokuyasu, K.T. J. Cell Biol. (1983) [Pubmed]
  23. Specific fluorescent labeling of chicken myofibril Z-line proteins catalyzed by guinea pig liver transglutaminase. Gard, D.L., Lazarides, E. J. Cell Biol. (1979) [Pubmed]
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