The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Des  -  desmin

Mus musculus

Synonyms: Desmin
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Des

  • Extensive induction of important mediators of fibrosis and dystrophic calcification in desmin-deficient cardiomyopathy [1].
  • These data together with the observed up-regulation of transforming growth factor-beta1 and angiotensin-converting enzyme, could explain the extensive fibrosis and dystrophic calcification observed in the heart of desmin-null mice, potentially crucial events leading to heart failure [1].
  • MPA treatment was found to induce uterine secretory changes, glandular cystic hyperplasia, and eventually deciduomas that stained strongly for desmin and to a lesser degree for vimentin, suggesting a muscular differentiation [2].
  • Recently, mutations of the desmin gene have been reported to cause familial or sporadic forms of human skeletal, as well as cardiac, myopathy, termed desmin-related myopathy (DRM) [3].
  • Overexpression of bcl-2 in the desmin null heart results in correction of mitochondrial defects, reduced occurrence of fibrotic lesions in the myocardium, prevention of cardiac hypertrophy, restoration of cardiomyocyte ultrastructure, and significant improvement of cardiac function [4].

High impact information on Des

  • Skeletal and cardiac myopathy develops in mice that lack desmin, suggesting that mutations in the desmin gene may be pathogenic [5].
  • Expression of either MyoD or, more surprisingly, desmin in Lmna(-/-) myoblasts resulted in increased differentiation potential [6].
  • These findings suggest a model in which the primary pathophysiological mechanism in Lmna(-/-) mice is defective force transmission resulting from disruption of lamin interactions with the muscle-specific desmin network and loss of cytoskeletal tension [7].
  • In the following months, alveolar spaces enlarged in association with thickening of the alveolar walls due to an accumulation of desmin-containing fibroblasts, collagen fibers, and lymphocytes [8].
  • Remaining Kit-immunopositive cells in the pacemaker region of the small intestine developed ultrastructural features similar to smooth muscle cells, including prominent filament bundles and expression of the muscle-specific intermediate filament protein, desmin, and smooth muscle myosin [9].

Chemical compound and disease context of Des


Biological context of Des

  • However, myofibrillogenesis in regenerating fibers is often abortive, indicating that desmin may be implicated in this repair process [12].
  • Rescue of the normal phenotype was achieved either by spontaneous revertants, or by overexpression of the desmin sense RNA in the defective cell lines [13].
  • An E box in the desmin promoter cooperates with the E box and MEF-2 sites of a distal enhancer to direct muscle-specific transcription [14].
  • The lack of desmin was not compensated by an upregulation of vimentin in these mice either during development or regeneration [12].
  • Double mutations of E1 with E2 or MEF-2 sites suggested that, to achieve high levels of desmin gene expression, E1 serves most possibly as an intermediary for either E2 or MEF-2 enhancer elements to function [14].

Anatomical context of Des

  • The muscle-specific intermediate filament protein, desmin, is one of the earliest myogenic markers whose functional role during myogenic commitment and differentiation is unknown [13].
  • The results presented here show that desmin is essential to maintain the structural integrity of highly solicited skeletal muscle [12].
  • The predominantly longitudinal orientation of desmin filaments seen in myoblasts and in early myotubes is transformed at g.d. 17 and 18 to distinct Z line connected striations [15].
  • Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle [12].
  • Absence of desmin filaments within the sarcomere does not interfere with primary muscle formation or regeneration [12].

Associations of Des with chemical compounds


Physical interactions of Des

  • Mutation of this MyoD binding site abrogates desmin transcription, and transactivation of the promoter no longer occurs [19].
  • On the other hand, calponin bound strongly to nonfilamentous desmin tetramers and was incorporated into intermediate filaments when the two proteins were mixed in a buffer containing 6 M urea and dialyzed into a buffer containing 0.15 M NaCl [21].

Co-localisations of Des

  • Immunohistochemical staining of fibroblast cultures derived from the transgenic mice with antibodies specific for vimentin and desmin demonstrated that the pVVim2 protein is assembled into filaments that co-localize with the endogenous vimentin filaments [22].
  • We show that in wild-type mice, synemin, paranemin, and plectin were colocalized with desmin in Z-disc-associated striations and at the sarcolemma [23].

Regulatory relationships of Des


Other interactions of Des

  • Vimentin, still present together with desmin in the myoblasts, is lost from the myotubes [15].
  • Here, we used desmin and alpha-smooth muscle actin (ASMA) as markers to analyze vSMC/PC development in PDGF-B-/- and PDGFR-beta-/- embryos [28].
  • Extensive osteopontin localization is observed by immunohistochemistry in the desmin-null myocardium in areas with massive myocyte death, as well as in hypercellular regions with variable degrees of calcification and fibrosis [1].
  • In Ang-2 null mutants, alpha SMA, desmin, and PDGFR beta prominently immunolocalized in cortical peritubular locations [29].
  • Some alpha SMA-positive cells were closely associated with CD31- and Tie-2-positive peritubular capillary endothelia, and some of the alpha SMA-positive cells expressed PDGFR beta, desmin, and neural/glial cell 2 (NG2), consistent with a pericyte-like identity [29].

Analytical, diagnostic and therapeutic context of Des

  • Immunohistochemistry with antibody reactive with desmin indicated a similar reduction in the number of differentiated myocytes in the myotome [30].
  • Alpha-smooth muscle actin, desmin and proliferating cell nuclear antigen were assessed by immunohistochemical testing of whole bladders and Western blot analysis of dissected detrusor layers [31].
  • Electron microscopy revealed that the perimeter of cellular fingerlike-projections was smaller in Des -/-, indicating that the cells have lost part of their connections to the extracellular matrix [32].
  • METHODS AND RESULTS: With the use of selective ligations of second-order mesenteric arteries, blood flow was either diminished (low flow [LF]) or elevated (high flow [HF]); respective LF to HF values were 136+/-18 to 206+/-29 microL/min for Des+/+ mice and 119+/-14 to 189+/-24 microL/min for Des-/-mice in daughter arteries [33].
  • Using SDS-PAGE gels and Western blots we found a gradient in desmin expression in the arterial tree; the desmin content increased from the elastic artery aorta, via the muscular mesenteric artery to the resistance-sized mesenteric microarteries approximately 150 microm in diameter in Des+/+ mice [34].


  1. Extensive induction of important mediators of fibrosis and dystrophic calcification in desmin-deficient cardiomyopathy. Mavroidis, M., Capetanaki, Y. Am. J. Pathol. (2002) [Pubmed]
  2. Mouse mammary tumors induced by medroxyprogesterone acetate: immunohistochemistry and hormonal receptors. Molinolo, A.A., Lanari, C., Charreau, E.H., Sanjuan, N., Pasqualini, C.D. J. Natl. Cancer Inst. (1987) [Pubmed]
  3. Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Bär, H., Mücke, N., Kostareva, A., Sjöberg, G., Aebi, U., Herrmann, H. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy. Weisleder, N., Taffet, G.E., Capetanaki, Y. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene. Dalakas, M.C., Park, K.Y., Semino-Mora, C., Lee, H.S., Sivakumar, K., Goldfarb, L.G. N. Engl. J. Med. (2000) [Pubmed]
  6. Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation. Frock, R.L., Kudlow, B.A., Evans, A.M., Jameson, S.A., Hauschka, S.D., Kennedy, B.K. Genes Dev. (2006) [Pubmed]
  7. Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice. Nikolova, V., Leimena, C., McMahon, A.C., Tan, J.C., Chandar, S., Jogia, D., Kesteven, S.H., Michalicek, J., Otway, R., Verheyen, F., Rainer, S., Stewart, C.L., Martin, D., Feneley, M.P., Fatkin, D. J. Clin. Invest. (2004) [Pubmed]
  8. Expression of a tumor necrosis factor-alpha transgene in murine lung causes lymphocytic and fibrosing alveolitis. A mouse model of progressive pulmonary fibrosis. Miyazaki, Y., Araki, K., Vesin, C., Garcia, I., Kapanci, Y., Whitsett, J.A., Piguet, P.F., Vassalli, P. J. Clin. Invest. (1995) [Pubmed]
  9. Blockade of kit signaling induces transdifferentiation of interstitial cells of cajal to a smooth muscle phenotype. Torihashi, S., Nishi, K., Tokutomi, Y., Nishi, T., Ward, S., Sanders, K.M. Gastroenterology (1999) [Pubmed]
  10. Monoclonal antibody P-31 recognizes a novel intermediate filament-associated protein (p250) in rat podocytes. Kurihara, H., Sunagawa, N., Kobayashi, T., Kimura, K., Takasu, N., Shike, T. Am. J. Physiol. (1998) [Pubmed]
  11. The stellate cells phenotypic transformation in the CCl4- injured liver fibrosis of ICR mice: their desmin immunoreactivity and vitamin A storage. Lukita-Atmadja, W., Subowo, n.u.l.l. The Kobe journal of medical sciences. (1993) [Pubmed]
  12. Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. Li, Z., Mericskay, M., Agbulut, O., Butler-Browne, G., Carlsson, L., Thornell, L.E., Babinet, C., Paulin, D. J. Cell Biol. (1997) [Pubmed]
  13. Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin. Li, H., Choudhary, S.K., Milner, D.J., Munir, M.I., Kuisk, I.R., Capetanaki, Y. J. Cell Biol. (1994) [Pubmed]
  14. An E box in the desmin promoter cooperates with the E box and MEF-2 sites of a distal enhancer to direct muscle-specific transcription. Li, H., Capetanaki, Y. EMBO J. (1994) [Pubmed]
  15. 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]
  16. Expression of myogenic regulatory factors during the development of mouse tongue striated muscle. Yamane, A., Mayo, M., Shuler, C., Crowe, D., Ohnuki, Y., Dalrymple, K., Saeki, Y. Arch. Oral Biol. (2000) [Pubmed]
  17. Assignment of the mouse desmin gene to chromosome 1 band C3. Li, Z.L., Mattei, M.G., Mattei, J.F., Paulin, D. Genet. Res. (1990) [Pubmed]
  18. Non-beating HL-1 cells for confocal microscopy: application to mitochondrial functions during cardiac preconditioning. Pelloux, S., Robillard, J., Ferrera, R., Bilbaut, A., Ojeda, C., Saks, V., Ovize, M., Tourneur, Y. Prog. Biophys. Mol. Biol. (2006) [Pubmed]
  19. A proximal promoter element in the hamster desmin upstream regulatory region is responsible for activation by myogenic determination factors. van de Klundert, F.A., Jansen, H.J., Bloemendal, H. J. Biol. Chem. (1994) [Pubmed]
  20. Bone marrow-derived progenitor cells contribute to experimental choroidal neovascularization. Espinosa-Heidmann, D.G., Caicedo, A., Hernandez, E.P., Csaky, K.G., Cousins, S.W. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  21. Association of calponin with desmin intermediate filaments. Mabuchi, K., Li, B., Ip, W., Tao, T. J. Biol. Chem. (1997) [Pubmed]
  22. Tissue-specific expression of a vimentin--desmin hybrid gene in transgenic mice. Krimpenfort, P.J., Schaart, G., Pieper, F.R., Ramaekers, F.C., Cuypers, H.T., van den Heuvel, R.M., Vree Egberts, W.T., van Eys, G.J., Berns, A., Bloemendal, H. EMBO J. (1988) [Pubmed]
  23. Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knock-out mice. Carlsson, L., Li, Z.L., Paulin, D., Price, M.G., Breckler, J., Robson, R.M., Wiche, G., Thornell, L.E. Histochem. Cell Biol. (2000) [Pubmed]
  24. Nestin is expressed during development and in myotendinous and neuromuscular junctions in wild type and desmin knock-out mice. Carlsson, L., Li, Z., Paulin, D., Thornell, L.E. Exp. Cell Res. (1999) [Pubmed]
  25. Transforming growth factor alpha up-regulates desmin expression during embryonic mouse tongue myogenesis. Yamane, A., Bringas, P., Mayo, M.L., Amano, O., Takahashi, K., Vo, H., Shum, L., Slavkin, H.C. Dev. Dyn. (1998) [Pubmed]
  26. Intrinsic differences in MyoD and myogenin expression between primary cultures of SJL/J and BALB/C skeletal muscle. Maley, M.A., Fan, Y., Beilharz, M.W., Grounds, M.D. Exp. Cell Res. (1994) [Pubmed]
  27. Lhx2 is expressed in the septum transversum mesenchyme that becomes an integral part of the liver and the formation of these cells is independent of functional Lhx2. Kolterud, A., Wandzioch, E., Carlsson, L. Gene Expr. Patterns (2004) [Pubmed]
  28. Role of PDGF-B and PDGFR-beta in recruitment of vascular smooth muscle cells and pericytes during embryonic blood vessel formation in the mouse. Hellström, M., Kalén, M., Lindahl, P., Abramsson, A., Betsholtz, C. Development (1999) [Pubmed]
  29. Dysmorphogenesis of kidney cortical peritubular capillaries in angiopoietin-2-deficient mice. Pitera, J.E., Woolf, A.S., Gale, N.W., Yancopoulos, G.D., Yuan, H.T. Am. J. Pathol. (2004) [Pubmed]
  30. Strain-dependent embryonic lethality in mice lacking the retinoblastoma-related p130 gene. LeCouter, J.E., Kablar, B., Whyte, P.F., Ying, C., Rudnicki, M.A. Development (1998) [Pubmed]
  31. Smooth muscle differentiation and cell turnover in mouse detrusor development. Smeulders, N., Woolf, A.S., Wilcox, D.T. J. Urol. (2002) [Pubmed]
  32. Mechanical properties and structure of carotid arteries in mice lacking desmin. Lacolley, P., Challande, P., Boumaza, S., Cohuet, G., Laurent, S., Boutouyrie, P., Grimaud, J.A., Paulin, D., Lamazière, J.M., Li, Z. Cardiovasc. Res. (2001) [Pubmed]
  33. Excessive microvascular adaptation to changes in blood flow in mice lacking gene encoding for desmin. Loufrani, L., Li, Z., Lévy, B.I., Paulin, D., Henrion, D. Arterioscler. Thromb. Vasc. Biol. (2002) [Pubmed]
  34. Mechanical function of intermediate filaments in arteries of different size examined using desmin deficient mice. Wede, O.K., Löfgren, M., Li, Z., Paulin, D., Arner, A. J. Physiol. (Lond.) (2002) [Pubmed]
WikiGenes - Universities