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Gene Review

SYNM  -  synemin, intermediate filament protein

Homo sapiens

Synonyms: DMN, Desmuslin, KIAA0353, SYN, Synemin
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Disease relevance of DMN


High impact information on DMN

  • These data suggest that this high molecular weight protein is closely associated with desmin and vimentin filaments in muscle cells; to indicate this, we have named the protein synemin, from the Greek oa uv (with) and v eta mu alpha (filament) [5].
  • The examples used were 1) exposure to DES and mammary carcinoma and 2) exposure to DMN and liver carcinoma [6].
  • Measurable CO2 was formed by bronchial explants from: 1) DMN, DEN, and NPy in all 4 patients; 2) DNP in 3 of 4 patients; and 3) NPd in only 1 of 4 patients [7].
  • Sequence analysis revealed that DMN has a short N-terminal domain, a conserved rod domain, and a long C-terminal domain, all common features of type 6 intermediate filament proteins [8].
  • Our findings suggest that DMN may serve as a direct linkage between the extracellular matrix and the Z-discs (through plectin) and may play an important role in maintaining muscle cell integrity [8].

Chemical compound and disease context of DMN


Biological context of DMN


Anatomical context of DMN

  • Immunofluorescent microscopy localizes DMN in a stripe-like pattern in longitudinal sections and in a mosaic pattern in cross sections of skeletal muscle [8].
  • These results indicate that synemin is an important IF protein in muscle cells that helps fortify the linkage between the peripheral layer of cellular myofibrils and the costameric regions located along the sarcolemma and the sarcolemma region located within the neuromuscular and myotendinous junctions (NMJs and MTJs) [13].
  • In normal rat and human livers, synemin immunoreactivity was found in HSCs, smooth muscle cells of hepatic arterioles, and nerve bundles in portal tracts, but not in portal fibroblasts [14].
  • CONCLUSIONS: Synemin forms heteropolymeric filaments with type-III IF proteins and acts as a bridging protein between IFs and a specific type of focal adhesions [14].
  • Low-resolution immunohistochemical analysis localizes beta-synemin within muscle along the sarcolemma, whereas confocal microscopic analysis further refines localization to the costamere and muscle Z-lines [15].

Associations of DMN with chemical compounds

  • In contrast, nine days of nicotine treatment reduced CART levels in the DMN as compared to saline controls [3].
  • Binding levels of DNP were as high as those with the two acyclic N-nitrosamines DMN and DEN, but binding levels of NPy and NPd were lower [7].
  • The actions of menadione on ROS production and cell fate were compared with those of a non-cycling analogue (2,4-dimethoxy-2-methylnaphthalene (DMN)) using real-time confocal microscopy of isolated perfused murine pancreatic acinar cells [16].
  • Furthermore, bile acid (taurolithocholic acid 3-sulfate)-induced caspase activation was also greatly increased by DMN, whereas DMN had no effect per se [16].
  • A small amount of a nitrosamine, N-nitrosodimethylamine (DMN), was detected in the stomach after a single dose of NaNO2 [17].

Physical interactions of DMN

  • By utilizing blot overlay assays, we show herein that synemin also interacts with the costameric protein vinculin [12].

Co-localisations of DMN


Regulatory relationships of DMN

  • Analysis of endogenous protein expression in SW13 clonal lines reveals that synemin is coexpressed and colocalized with vimentin IFs in SW13.C1 vim+ cells but is absent in SW13.C2 vim- cells [11].
  • DMN produced no change in reactive oxygen species per se but significantly potentiated menadione-induced effects, probably via enhancement of one-electron reduction, since DMN was found to inhibit NAD(P)H:quinone oxidoreductase detoxification [16].

Other interactions of DMN


Analytical, diagnostic and therapeutic context of DMN


  1. Expression of the intermediate filament protein synemin in myofibrillar myopathies and other muscle diseases. Olivé, M., Goldfarb, L., Dagvadorj, A., Sambuughin, N., Paulin, D., Li, Z., Goudeau, B., Vicart, P., Ferrer, I. Acta Neuropathol. (2003) [Pubmed]
  2. Genomic organization and single-nucleotide polymorphism map of desmuslin, a novel intermediate filament protein on chromosome 15q26.3. Mizuno, Y., Puca, A.A., O'Brien, K.F., Beggs, A.H., Kunkel, L.M. BMC Genet. (2001) [Pubmed]
  3. Nicotine administration effects on feeding and cocaine-amphetamine-regulated transcript (CART) expression in the hypothalamus. Kramer, P.R., Kramer, S.F., Marr, K., Guan, G., Wellman, P.J., Bellinger, L.L. Regul. Pept. (2007) [Pubmed]
  4. Intermediate filament protein synemin is present in human reactive and malignant astrocytes and associates with ruffled membranes in astrocytoma cells. Jing, R., Pizzolato, G., Robson, R.M., Gabbiani, G., Skalli, O. Glia (2005) [Pubmed]
  5. Synemin: a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Granger, B.L., Lazarides, E. Cell (1980) [Pubmed]
  6. Statistical aspects of extrapolation of dichotomous dose-response data. Brown, C.C. J. Natl. Cancer Inst. (1978) [Pubmed]
  7. Metabolism of acyclic and cyclic N-nitrosamines in cultured human bronchi. Harris, C.C., Autrup, H., Stoner, G.D., McDowell, E.M., Trump, B.F., Schafer, P. J. Natl. Cancer Inst. (1977) [Pubmed]
  8. Desmuslin, an intermediate filament protein that interacts with alpha -dystrobrevin and desmin. Mizuno, Y., Thompson, T.G., Guyon, J.R., Lidov, H.G., Brosius, M., Imamura, M., Ozawa, E., Watkins, S.C., Kunkel, L.M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  9. Effects of phenethyl isothiocyanate on metabolism and on genotoxicity of dimethylnitrosamine and 2-amino-1-methyl-6-phenylimidazo[4, 5-beta]pyridine (PhIP). Knasmüller, S., Friesen, M.D., Holme, J.A., Alexander, J., Sanyal, R., Kassie, F., Bartsch, H. Mutat. Res. (1996) [Pubmed]
  10. Measurement of the aquatic toxicity of volatile nitrosamines. Draper, A.C., Brewer, W.S. Journal of toxicology and environmental health. (1979) [Pubmed]
  11. Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments. Bellin, R.M., Sernett, S.W., Becker, B., Ip, W., Huiatt, T.W., Robson, R.M. J. Biol. Chem. (1999) [Pubmed]
  12. Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. Bellin, R.M., Huiatt, T.W., Critchley, D.R., Robson, R.M. J. Biol. Chem. (2001) [Pubmed]
  13. Interactions of intermediate filament protein synemin with dystrophin and utrophin. Bhosle, R.C., Michele, D.E., Campbell, K.P., Li, Z., Robson, R.M. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  14. Hepatic stellate cells express synemin, a protein bridging intermediate filaments to focal adhesions. Uyama, N., Zhao, L., Van Rossen, E., Hirako, Y., Reynaert, H., Adams, D.H., Xue, Z., Li, Z., Robson, R., Pekny, M., Geerts, A. Gut (2006) [Pubmed]
  15. Beta-synemin localizes to regions of high stress in human skeletal myofibers. Mizuno, Y., Guyon, J.R., Watkins, S.C., Mizushima, K., Sasaoka, T., Imamura, M., Kunkel, L.M., Okamoto, K. Muscle Nerve (2004) [Pubmed]
  16. Menadione-induced Reactive Oxygen Species Generation via Redox Cycling Promotes Apoptosis of Murine Pancreatic Acinar Cells. Criddle, D.N., Gillies, S., Baumgartner-Wilson, H.K., Jaffar, M., Chinje, E.C., Passmore, S., Chvanov, M., Barrow, S., Gerasimenko, O.V., Tepikin, A.V., Sutton, R., Petersen, O.H. J. Biol. Chem. (2006) [Pubmed]
  17. Transplacental mutagenesis of products formed in the stomach of golden hamsters given sodium nitrite and morpholine. Inui, N., Nishi, Y., Taketomi, M., Mori, M., Yamamoto, M., Yamada, T., Tanimura, A. Int. J. Cancer (1979) [Pubmed]
  18. Human synemin gene generates splice variants encoding two distinct intermediate filament proteins. Titeux, M., Brocheriou, V., Xue, Z., Gao, J., Pellissier, J.F., Guicheney, P., Paulin, D., Li, Z. Eur. J. Biochem. (2001) [Pubmed]
  19. Smooth-muscle-associated contractile protein in renal mesenchymal tumour cells and in transformed cells from DMN-injected rats. Toh, B.H., Hard, G.C., Cauchi, M.N., Muller, H.K. Br. J. Cancer (1976) [Pubmed]
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