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Acta Neuropathologica
Published in: Acta Neuropathologica 1/2013

Open Access 01-01-2013 | Review

Desminopathies: pathology and mechanisms

Authors: Christoph S. Clemen, Harald Herrmann, Sergei V. Strelkov, Rolf Schröder

Published in: Acta Neuropathologica | Issue 1/2013

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Abstract

The intermediate filament protein desmin is an essential component of the extra-sarcomeric cytoskeleton in muscle cells. This three-dimensional filamentous framework exerts central roles in the structural and functional alignment and anchorage of myofibrils, the positioning of cell organelles and signaling events. Mutations of the human desmin gene on chromosome 2q35 cause autosomal dominant, autosomal recessive, and sporadic myopathies and/or cardiomyopathies with marked phenotypic variability. The disease onset ranges from childhood to late adulthood. The clinical course is progressive and no specific treatment is currently available for this severely disabling disease. The muscle pathology is characterized by desmin-positive protein aggregates and degenerative changes of the myofibrillar apparatus. The molecular pathophysiology of desminopathies is a complex, multilevel issue. In addition to direct effects on the formation and maintenance of the extra-sarcomeric intermediate filament network, mutant desmin affects essential protein interactions, cell signaling cascades, mitochondrial functions, and protein quality control mechanisms. This review summarizes the currently available data on the epidemiology, clinical phenotypes, myopathology, and genetics of desminopathies. In addition, this work provides an overview on the expression, filament formation processes, biomechanical properties, post-translational modifications, interaction partners, subcellular localization, and functions of wild-type and mutant desmin as well as desmin-related cell and animal models.
Literature
1.
Agbulut O, Li Z, Perie S, Ludosky MA, Paulin D, Cartaud J, Butler-Browne G (2001) Lack of desmin results in abortive muscle regeneration and modifications in synaptic structure. Cell Motil Cytoskelet 49:51–66CrossRef
2.
Anderson J, Li Z, Goubel F (2001) Passive stiffness is increased in soleus muscle of desmin knockout mouse. Muscle Nerve 24:1090–1092PubMedCrossRef
3.
Arbustini E, Morbini P, Grasso M, Fasani R, Verga L, Bellini O, Dal Bello B, Campana C, Piccolo G, Febo O, Opasich C, Gavazzi A, Ferrans VJ (1998) Restrictive cardiomyopathy, atrioventricular block and mild to subclinical myopathy in patients with desmin-immunoreactive material deposits. J Am Coll Cardiol 31:645–653PubMedCrossRef
4.
Arbustini E, Pasotti M, Pilotto A, Pellegrini C, Grasso M, Previtali S, Repetto A, Bellini O, Azan G, Scaffino M, Campana C, Piccolo G, Vigano M, Tavazzi L (2006) Desmin accumulation restrictive cardiomyopathy and atrioventricular block associated with desmin gene defects. Eur J Heart Fail 8:477–483PubMedCrossRef
5.
Arias M, Pardo J, Blanco-Arias P, Sobrido MJ, Arias S, Dapena D, Carracedo A, Goldfarb LG, Navarro C (2006) Distinct phenotypic features and gender-specific disease manifestations in a Spanish family with desmin L370P mutation. Neuromuscul Disord 16:498–503PubMedCrossRef
6.
Ariza A, Coll J, Fernandez-Figueras MT, Lopez MD, Mate JL, Garcia O, Fernandez-Vasalo A, Navas-Palacios JJ (1995) Desmin myopathy: a multisystem disorder involving skeletal, cardiac, and smooth muscle. Hum Pathol 26:1032–1037PubMedCrossRef
7.
Balogh J, Li Z, Paulin D, Arner A (2003) Lower active force generation and improved fatigue resistance in skeletal muscle from desmin deficient mice. J Muscle Res Cell Motil 24:453–459PubMedCrossRef
8.
Bang ML, Gregorio C, Labeit S (2002) Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J Struct Biol 137:119–127PubMedCrossRef
9.
Bär H, Fischer D, Goudeau B, Kley RA, Clemen CS, Vicart P, Herrmann H, Vorgerd M, Schröder R (2005) Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro. Hum Mol Genet 14:1251–1260PubMedCrossRef
10.
Bär H, Goudeau B, Walde S, Casteras-Simon M, Mücke N, Shatunov A, Goldberg YP, Clarke C, Holton JL, Eymard B, Katus HA, Fardeau M, Goldfarb L, Vicart P, Herrmann H (2007) Conspicuous involvement of desmin tail mutations in diverse cardiac and skeletal myopathies. Hum Mutat 28:374–386PubMedCrossRef
11.
Bär H, Kostareva A, Sjoberg G, Sejersen T, Katus HA, Herrmann H (2006) Forced expression of desmin and desmin mutants in cultured cells: impact of myopathic missense mutations in the central coiled-coil domain on network formation. Exp Cell Res 312:1554–1565PubMedCrossRef
12.
Bär H, Mücke N, Kostareva A, Sjoberg G, Aebi U, Herrmann H (2005) Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Proc Natl Acad Sci USA 102:15099–15104PubMedCrossRef
13.
Bär H, Mücke N, Ringler P, Müller SA, Kreplak L, Katus HA, Aebi U, Herrmann H (2006) Impact of disease mutations on the desmin filament assembly process. J Mol Biol 360:1031–1042PubMedCrossRef
14.
Bär H, Schopferer M, Sharma S, Hochstein B, Mücke N, Herrmann H, Willenbacher N (2010) Mutations in Desmin’s carboxy-terminal “Tail” domain severely modify filament and network mechanics. J Mol Biol 397:1188–1198PubMedCrossRef
15.
Bär H, Sharma S, Kleiner H, Mücke N, Zentgraf H, Katus HA, Aebi U, Herrmann H (2009) Interference of amino-terminal desmin fragments with desmin filament formation. Cell Motil Cytoskeleton 66:986–999PubMedCrossRef
16.
Bär H, Strelkov SV, Sjoberg G, Aebi U, Herrmann H (2004) The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation? J Struct Biol 148:137–152PubMedCrossRef
17.
Baron CP, Jacobsen S, Purslow PP (2004) Cleavage of desmin by cysteine proteases: calpains and cathepsin B. Meat Sci 68:447–456PubMedCrossRef
18.
Bellin RM, Sernett SW, Becker B, Ip W, Huiatt TW, Robson RM (1999) Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments. J Biol Chem 274:29493–29499PubMedCrossRef
19.
Bennardini F, Wrzosek A, Chiesi M (1992) Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res 71:288–294PubMedCrossRef
20.
Benvenuti LA, Aiello VD, Falcao BA, Lage SG (2012) Atrioventricular block pathology in cardiomyopathy by desmin deposition. Arq Bras Cardiol 98:e3–e6PubMedCrossRef
21.
Bergman JE, Veenstra-Knol HE, van Essen AJ, van Ravenswaaij CM, den Dunnen WF, van den Wijngaard A, van Tintelen JP (2007) Two related Dutch families with a clinically variable presentation of cardioskeletal myopathy caused by a novel S13F mutation in the desmin gene. Eur J Med Genet 50:355–366PubMedCrossRef
22.
Bonakdar N, Luczak J, Lautscham L, Czonstke M, Koch TM, Mainka A, Jungbauer T, Goldmann WH, Schröder R, Fabry B (2012) Biomechanical characterization of a desminopathy in primary human myoblasts. Biochem Biophys Res Commun 419:703–707PubMedCrossRef
23.
Boriek AM, Capetanaki Y, Hwang W, Officer T, Badshah M, Rodarte J, Tidball JG (2001) Desmin integrates the three-dimensional mechanical properties of muscles. Am J Physiol Cell Physiol 280:C46–C52PubMed
24.
Brachvogel B, Pausch F, Farlie P, Gaipl U, Etich J, Zhou Z, Cameron T, von der Mark K, Bateman JF, Poschl E (2007) Isolated Anxa5 +/Sca-1 + perivascular cells from mouse meningeal vasculature retain their perivascular phenotype in vitro and in vivo. Exp Cell Res 313:2730–2743PubMedCrossRef
25.
Breckler J, Lazarides E (1982) Isolation of a new high molecular weight protein associated with desmin and vimentin filaments from avian embryonic skeletal muscle. J Cell Biol 92:795–806PubMedCrossRef
26.
Burkhard P, Stetefeld J, Strelkov SV (2001) Coiled coils: a highly versatile protein folding motif. Trends Cell Biol 11:82–88PubMedCrossRef
27.
Capetanaki Y, Bloch RJ, Kouloumenta A, Mavroidis M, Psarras S (2007) Muscle intermediate filaments and their links to membranes and membranous organelles. Exp Cell Res 313:2063–2076PubMedCrossRef
28.
Carlsson L, Li Z, Paulin D, Thornell LE (1999) Nestin is expressed during development and in myotendinous and neuromuscular junctions in wild type and desmin knockout mice. Exp Cell Res 251:213–223PubMedCrossRef
29.
Carlsson L, Li ZL, Paulin D, Price MG, Breckler J, Robson RM, Wiche G, Thornell LE (2000) Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knockout mice. Histochem Cell Biol 114:39–47PubMed
30.
Carlsson L, Thornell LE (2001) Desmin-related myopathies in mice and man. Acta Physiol Scand 171:341–348PubMedCrossRef
31.
Carmignac V, Sharma S, Arbogast S, Fischer D, Serreri C, Serria M, Stoltenburg G, Maurage CA, Herrmann H, Cuisset JM, Bär H, Ferreiro A (2009) A homozygous desmin deletion causes an Emery-Dreifuss like recessive myopathy with desmin depletion. Neuromuscul Disord 19:600CrossRef
32.
Chen F, Chang R, Trivedi M, Capetanaki Y, Cryns VL (2003) Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis. J Biol Chem 278:6848–6853PubMedCrossRef
33.
Chernyatina AA, Nicolet S, Aebi U, Herrmann H, Strelkov SV (2012) Atomic structure of the vimentin central alpha-helical domain and its implications for intermediate filament assembly. Proc Natl Acad Sci USA 109:13620–13625PubMedCrossRef
34.
Claycomb WC, Lanson NA Jr, Stallworth BS, Egeland DB, Delcarpio JB, Bahinski A, Izzo NJ Jr (1998) HL-1 cells: a cardiac muscle cell line that contracts and retains phenotypic characteristics of the adult cardiomyocyte. Proc Natl Acad Sci USA 95:2979–2984PubMedCrossRef
35.
Clemen CS, Fischer D, Reimann J, Eichinger L, Muller CR, Muller HD, Goebel HH, Schröder R (2009) How much mutant protein is needed to cause a protein aggregate myopathy in vivo? Lessons from an exceptional desminopathy. Hum Mutat 30:E490–E499PubMedCrossRef
36.
Clemen CS, Fischer D, Roth U, Simon S, Vicart P, Kato K, Kaminska AM, Vorgerd M, Goldfarb LG, Eymard B, Romero NB, Goudeau B, Eggermann T, Zerres K, Noegel AA, Schröder R (2005) Hsp27-2D-gel electrophoresis is a diagnostic tool to differentiate primary desminopathies from myofibrillar myopathies. FEBS Lett 579:3777–3782PubMedCrossRef
37.
Colucci-Guyon E, Portier MM, Dunia I, Paulin D, Pournin S, Babinet C (1994) Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79:679–694PubMedCrossRef
38.
Costa ML, Escaleira R, Cataldo A, Oliveira F, Mermelstein CS (2004) Desmin: molecular interactions and putative functions of the muscle intermediate filament protein. Braz J Med Biol Res 37:1819–1830PubMedCrossRef
39.
Dagvadorj A, Goudeau B, Hilton-Jones D, Blancato JK, Shatunov A, Simon-Casteras M, Squier W, Nagle JW, Goldfarb LG, Vicart P (2003) Respiratory insufficiency in desminopathy patients caused by introduction of proline residues in desmin c-terminal alpha-helical segment. Muscle Nerve 27:669–675PubMedCrossRef
40.
Dagvadorj A, Olive M, Urtizberea JA, Halle M, Shatunov A, Bonnemann C, Park KY, Goebel HH, Ferrer I, Vicart P, Dalakas MC, Goldfarb LG (2004) A series of West European patients with severe cardiac and skeletal myopathy associated with a de novo R406 W mutation in desmin. J Neurol 251:143–149PubMedCrossRef
41.
Dalakas MC, Dagvadorj A, Goudeau B, Park KY, Takeda K, Simon-Casteras M, Vasconcelos O, Sambuughin N, Shatunov A, Nagle JW, Sivakumar K, Vicart P, Goldfarb LG (2003) Progressive skeletal myopathy, a phenotypic variant of desmin myopathy associated with desmin mutations. Neuromuscul Disord 13:252–258PubMedCrossRef
42.
Dalakas MC, Park KY, Semino-Mora C, Lee HS, Sivakumar K, Goldfarb LG (2000) Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene. N Engl J Med 342:770–780PubMedCrossRef
43.
Duprey P, Paulin D (1995) What can be learned from intermediate filament gene regulation in the mouse embryo. Int J Dev Biol 39:443–457PubMed
44.
Elamrani N, Brustis JJ, Dourdin N, Balcerzak D, Poussard S, Cottin P, Ducastaing A (1995) Desmin degradation and Ca(2 +)-dependent proteolysis during myoblast fusion. Biol Cell 85:177–183PubMedCrossRef
45.
Favre B, Schneider Y, Lingasamy P, Bouameur JE, Begre N, Gontier Y, Steiner-Champliaud MF, Frias MA, Borradori L, Fontao L (2011) Plectin interacts with the rod domain of type III intermediate filament proteins desmin and vimentin. Eur J Cell Biol 90:390–400PubMedCrossRef
46.
Ferrer I, Martin B, Castano JG, Lucas JJ, Moreno D, Olive M (2004) Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol 63:484–498PubMed
47.
Fidzianska A, Kotowicz J, Sadowska M, Goudeau B, Walczak E, Vicart P, Hausmanowa-Petrusewicz I (2005) A novel desmin R355P mutation causes cardiac and skeletal myopathy. Neuromuscul Disord 15:525–531PubMedCrossRef
48.
Fischer D, Kley RA, Strach K, Meyer C, Sommer T, Eger K, Rolfs A, Meyer W, Pou A, Pradas J, Heyer CM, Grossmann A, Huebner A, Kress W, Reimann J, Schröder R, Eymard B, Fardeau M, Udd B, Goldfarb L, Vorgerd M, Olive M (2008) Distinct muscle imaging patterns in myofibrillar myopathies. Neurology 71:758–765PubMedCrossRef
49.
Fountoulakis M, Soumaka E, Rapti K, Mavroidis M, Tsangaris G, Maris A, Weisleder N, Capetanaki Y (2005) Alterations in the heart mitochondrial proteome in a desmin null heart failure model. J Mol Cell Cardiol 38:461–474PubMedCrossRef
50.
Fujii T, Takagi H, Arimoto M, Ootani H, Ueeda T (2000) Bundle formation of smooth muscle desmin intermediate filaments by calponin and its binding site on the desmin molecule. J Biochem 127:457–465PubMedCrossRef
51.
Garcia-Verdugo I, Synguelakis M, Degrouard J, Franco CA, Valot B, Zivy M, Chaby R, Tanfin Z (2008) Interaction of surfactant protein A with the intermediate filaments desmin and vimentin. Biochemistry 47:5127–5138PubMedCrossRef
52.
Gard DL, Lazarides E (1982) Analysis of desmin and vimentin phosphopeptides in cultured avian myogenic cells and their modulation by 8-bromo-adenosine 3′,5′-cyclic monophosphate. Proc Natl Acad Sci USA 79:6912–6916PubMedCrossRef
53.
Gard JJ, Yamada K, Green KG, Eloff BC, Rosenbaum DS, Wang X, Robbins J, Schuessler RB, Yamada KA, Saffitz JE (2005) Remodeling of gap junctions and slow conduction in a mouse model of desmin-related cardiomyopathy. Cardiovasc Res 67:539–547PubMedCrossRef
54.
Georgatos SD, Weber K, Geisler N, Blobel G (1987) Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc Natl Acad Sci USA 84:6780–6784PubMedCrossRef
55.
Goldfarb LG, Dalakas MC (2009) Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease. J Clin Invest 119:1806–1813PubMedCrossRef
56.
Goldfarb LG, Dalakas MC (2011) Erratum for: “Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease”. J Clin Invest 121:455CrossRef
57.
Goldfarb LG, Olive M, Vicart P, Goebel HH (2008) Intermediate filament diseases: desminopathy. Adv Exp Med Biol 642:131–164PubMedCrossRef
58.
Goldfarb LG, Park KY, Cervenakova L, Gorokhova S, Lee HS, Vasconcelos O, Nagle JW, Semino-Mora C, Sivakumar K, Dalakas MC (1998) Missense mutations in desmin associated with familial cardiac and skeletal myopathy. Nat Genet 19:402–403PubMedCrossRef
59.
60.
Goll DE, Thompson VF, Li H, Wei W, Cong J (2003) The calpain system. Physiol Rev 83:731–801PubMed
61.
Goodall MH, Ward CW, Pratt SJ, Bloch RJ, Lovering RM (2012) Structural and functional evaluation of branched myofibers lacking intermediate filaments. Am J Physiol Cell Physiol 303:C224–C232
62.
Goudeau B, Rodrigues-Lima F, Fischer D, Casteras-Simon M, Sambuughin N, de Visser M, Laforet P, Ferrer X, Chapon F, Sjoberg G, Kostareva A, Sejersen T, Dalakas MC, Goldfarb LG, Vicart P (2006) Variable pathogenic potentials of mutations located in the desmin alpha-helical domain. Hum Mutat 27:906–913PubMedCrossRef
63.
Granger BL, Lazarides E (1980) Synemin: a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell 22:727–738PubMedCrossRef
64.
Greenberg SA, Salajegheh M, Judge DP, Feldman MW, Kuncl RW, Waldon Z, Steen H, Wagner KR (2012) Etiology of limb girdle muscular dystrophy 1D/1E determined by laser capture microdissection proteomics. Ann Neurol 71:141–145PubMedCrossRef
65.
Gudkova A, Kostareva A, Sjoberg G, Smolina N, Turalchuk M, Kuznetsova I, Rybakova M, Edstrom L, Shlyakhto E, Sejersen T (2012) Diagnostic challenge in desmin cardiomyopathy with transformation of clinical phenotypes. Pediatr Cardiol. doi:10.​1007/​s00246-00012-00312-x PubMed
66.
Hager S, Mahrholdt H, Goldfarb LG, Goebel HH, Sechtem U (2006) Images in cardiovascular medicine. Giant right atrium in the setting of desmin-related restrictive cardiomyopathy. Circulation 113:e53–e55PubMedCrossRef
67.
Halperin R, Fleminger G, Kraicer PF, Hadas E (1991) Desmin as an immunochemical marker of human decidual cells and its expression in menstrual fluid. Hum Reprod 6:186–189PubMed
68.
Haubold KW, Allen DL, Capetanaki Y, Leinwand LA (2003) Loss of desmin leads to impaired voluntary wheel running and treadmill exercise performance. J Appl Physiol 95:1617–1622PubMed
69.
Hedberg C, Melberg A, Kuhl A, Jenne D, Oldfors A (2012) Autosomal dominant myofibrillar myopathy with arrhythmogenic right ventricular cardiomyopathy 7 is caused by a DES mutation. Eur J Hum Genet 20:984–985PubMedCrossRef
70.
Herrmann A, Tozzo E, Funk J (2012) Semi-automated quantitative image analysis of podocyte desmin immunoreactivity as a sensitive marker for acute glomerular damage in the rat puromycin aminonucleoside nephrosis (PAN) model. Exp Toxicol Pathol 64:45–49PubMedCrossRef
71.
Herrmann H, Aebi U (1998) Structure, assembly, and dynamics of intermediate filaments. Subcell Biochem 31:319–362PubMed
72.
Herrmann H, Aebi U (2000) Intermediate filaments and their associates: multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr Opin Cell Biol 12:79–90PubMedCrossRef
73.
Herrmann H, Aebi U (2004) Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu Rev Biochem 73:749–789PubMedCrossRef
74.
Herrmann H, Bär H, Kreplak L, Strelkov SV, Aebi U (2007) Intermediate filaments: from cell architecture to nanomechanics. Nat Rev Mol Cell Biol 8:562–573PubMedCrossRef
75.
Herrmann H, Fouquet B, Franke WW (1989) Expression of intermediate filament proteins during development of Xenopus laevis. II. Identification and molecular characterization of desmin. Development 105:299–307PubMed
76.
Herrmann H, Häner M, Brettel M, Ku NO, Aebi U (1999) Characterization of distinct early assembly units of different intermediate filament proteins. J Mol Biol 286:1403–1420PubMedCrossRef
77.
Herrmann H, Häner M, Brettel M, Müller SA, Goldie KN, Fedtke B, Lustig A, Franke WW, Aebi U (1996) Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J Mol Biol 264:933–953PubMedCrossRef
78.
Herrmann H, Hesse M, Reichenzeller M, Aebi U, Magin TM (2003) Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation. Int Rev Cytol 223:83–175PubMedCrossRef
79.
Herrmann H, Strelkov SV, Burkhard P, Aebi U (2009) Intermediate filaments: primary determinants of cell architecture and plasticity. J Clin Invest 119:1772–1783PubMedCrossRef
80.
Herrmann H, Wiche G (1987) Plectin and IFAP-300 K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J Biol Chem 262:1320–1325PubMed
81.
Hirako Y, Yamakawa H, Tsujimura Y, Nishizawa Y, Okumura M, Usukura J, Matsumoto H, Jackson KW, Owaribe K, Ohara O (2003) Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: co-localization and interaction with type III intermediate filament proteins and keratins. Cell Tissue Res 313:195–207PubMedCrossRef
82.
Hnia K, Tronchere H, Tomczak KK, Amoasii L, Schultz P, Beggs AH, Payrastre B, Mandel JL, Laporte J (2011) Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle. J Clin Invest 121:70–85PubMedCrossRef
83.
Hong D, Wang Z, Zhang W, Xi J, Lu J, Luan X, Yuan Y (2011) A series of Chinese patients with desminopathy associated with six novel and one reported mutations in the desmin gene. Neuropathol Appl Neurobiol 37:257–270PubMedCrossRef
84.
Hübbers CU, Clemen CS, Kesper K, Boddrich A, Hofmann A, Kamarainen O, Tolksdorf K, Stumpf M, Reichelt J, Roth U, Krause S, Watts G, Kimonis V, Wattjes MP, Reimann J, Thal DR, Biermann K, Evert BO, Lochmuller H, Wanker EE, Schoser BG, Noegel AA, Schröder R (2007) Pathological consequences of VCP mutations on human striated muscle. Brain 130:381–393PubMedCrossRef
85.
Hurlimann J (1994) Desmin and neural marker expression in mesothelial cells and mesotheliomas. Hum Pathol 25:753–757PubMedCrossRef
86.
Janmey PA, Euteneuer U, Traub P, Schliwa M (1991) Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol 113:155–160PubMedCrossRef
87.
Janue A, Odena MA, Oliveira E, Olive M, Ferrer I (2007) Desmin is oxidized and nitrated in affected muscles in myotilinopathies and desminopathies. J Neuropathol Exp Neurol 66:711–723PubMedCrossRef
88.
Janue A, Olive M, Ferrer I (2007) Oxidative stress in desminopathies and myotilinopathies: a link between oxidative damage and abnormal protein aggregation. Brain Pathol 17:377–388PubMedCrossRef
89.
Kaminska A, Strelkov SV, Goudeau B, Olive M, Dagvadorj A, Fidzianska A, Simon-Casteras M, Shatunov A, Dalakas MC, Ferrer I, Kwiecinski H, Vicart P, Goldfarb LG (2004) Small deletions disturb desmin architecture leading to breakdown of muscle cells and development of skeletal or cardioskeletal myopathy. Hum Genet 114:306–313PubMedCrossRef
90.
Kartenbeck J, Franke WW, Moser JG, Stoffels U (1983) Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes. EMBO J 2:735–742PubMed
91.
Kawano F, Fujita R, Nakai N, Terada M, Ohira T, Ohira Y (2012) HSP25 can modulate myofibrillar desmin cytoskeleton following the phosphorylation at Ser15 in rat soleus muscle. J Appl Physiol 112:176–186PubMedCrossRef
92.
Klauke B, Kossmann S, Gaertner A, Brand K, Stork I, Brodehl A, Dieding M, Walhorn V, Anselmetti D, Gerdes D, Bohms B, Schulz U, Zu Knyphausen E, Vorgerd M, Gummert J, Milting H (2010) De novo desmin-mutation N116S is associated with arrhythmogenic right ventricular cardiomyopathy. Hum Mol Genet 19:4595–4607PubMedCrossRef
93.
Konieczny P, Fuchs P, Reipert S, Kunz WS, Zeöld A, Fischer I, Paulin D, Schröder R, Wiche G (2008) Myofiber integrity depends on desmin network targeting to Z-disks and costameres via distinct plectin isoforms. J Cell Biol 181:667–681PubMedCrossRef
94.
Kostareva A, Sjoberg G, Bruton J, Zhang SJ, Balogh J, Gudkova A, Hedberg B, Edstrom L, Westerblad H, Sejersen T (2008) Mice expressing L345P mutant desmin exhibit morphological and functional changes of skeletal and cardiac mitochondria. J Muscle Res Cell Motil 29:25–36PubMedCrossRef
95.
Kostareva A, Sjoberg G, Gudkova A, Smolina N, Semernin E, Shlyakhto E, Sejersen T (2011) Desmin A213 V substitution represents a rare polymorphism but not a mutation and is more prevalent in patients with heart dilation of various origins. Acta Myol 30:42–45PubMed
96.
Kouloumenta A, Mavroidis M, Capetanaki Y (2007) Proper perinuclear localization of the TRIM-like protein myospryn requires its binding partner desmin. J Biol Chem 282:35211–35221PubMedCrossRef
97.
Kreplak L, Bär H (2009) Severe myopathy mutations modify the nanomechanics of desmin intermediate filaments. J Mol Biol 385:1043–1051PubMedCrossRef
98.
Kreplak L, Herrmann H, Aebi U (2008) Tensile properties of single desmin intermediate filaments. Biophys J 94:2790–2799PubMedCrossRef
99.
Kuisk IR, Li H, Tran D, Capetanaki Y (1996) A single MEF2 site governs desmin transcription in both heart and skeletal muscle during mouse embryogenesis. Dev Biol 174:1–13PubMedCrossRef
100.
Kumarapeli AR, Horak KM, Glasford JW, Li J, Chen Q, Liu J, Zheng H, Wang X (2005) A novel transgenic mouse model reveals deregulation of the ubiquitin-proteasome system in the heart by doxorubicin. FASEB J 19:2051–2053PubMed
101.
Langley RC Jr, Cohen CM (1986) Association of spectrin with desmin intermediate filaments. J Cell Biochem 30:101–109PubMedCrossRef
102.
Li D, Tapscoft T, Gonzalez O, Burch PE, Quinones MA, Zoghbi WA, Hill R, Bachinski LL, Mann DL, Roberts R (1999) Desmin mutation responsible for idiopathic dilated cardiomyopathy. Circulation 100:461–464PubMedCrossRef
103.
Li H, Choudhary SK, Milner DJ, Munir MI, Kuisk IR, Capetanaki Y (1994) Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin. J Cell Biol 124:827–841PubMedCrossRef
104.
Li Z, Colucci-Guyon E, Pincon-Raymond M, Mericskay M, Pournin S, Paulin D, Babinet C (1996) Cardiovascular lesions and skeletal myopathy in mice lacking desmin. Dev Biol 175:362–366PubMedCrossRef
105.
Li Z, Mericskay M, Agbulut O, Butler-Browne G, Carlsson L, Thornell LE, Babinet C, Paulin D (1997) Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. J Cell Biol 139:129–144PubMedCrossRef
106.
Li ZL, Lilienbaum A, Butler-Browne G, Paulin D (1989) Human desmin-coding gene: complete nucleotide sequence, characterization and regulation of expression during myogenesis and development. Gene 78:243–254PubMedCrossRef
107.
Lichtenstern T, Mücke N, Aebi U, Mauermann M, Herrmann H (2012) Complex formation and kinetics of filament assembly exhibited by the simple epithelial keratins K8 and K18. J Struct Biol 177:54–62PubMedCrossRef
108.
Lindahl Allen M, Koch CM, Clelland GK, Dunham I, Antoniou M (2009) DNA methylation-histone modification relationships across the desmin locus in human primary cells. BMC Mol Biol 10:51PubMedCrossRef
109.
Linden M, Li Z, Paulin D, Gotow T, Leterrier JF (2001) Effects of desmin gene knockout on mice heart mitochondria. J Bioenerg Biomembr 33:333–341PubMedCrossRef
110.
Liu J, Chen Q, Huang W, Horak KM, Zheng H, Mestril R, Wang X (2006) Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J 20:362–364PubMed
111.
Lockard VG, Bloom S (1993) Trans-cellular desmin-lamin B intermediate filament network in cardiac myocytes. J Mol Cell Cardiol 25:303–309PubMedCrossRef
112.
Lyon GE, Buckingham ME (1993) Myogenic factor gene expression in mouse somites and limb buds. In: Bernfield M (ed) Molecular basis of morphogenesis. Symposia of the society for developmental biology series, vol 13, 1st edn. John, New York, pp 155–164
113.
Mavroidis M, Panagopoulou P, Kostavasili I, Weisleder N, Capetanaki Y (2008) A missense mutation in desmin tail domain linked to human dilated cardiomyopathy promotes cleavage of the head domain and abolishes its Z-disc localization. FASEB J 22:3318–3327PubMedCrossRef
114.
Milner DJ, Mavroidis M, Weisleder N, Capetanaki Y (2000) Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J Cell Biol 150:1283–1298PubMedCrossRef
115.
Milner DJ, Taffet GE, Wang X, Pham T, Tamura T, Hartley C, Gerdes AM, Capetanaki Y (1999) The absence of desmin leads to cardiomyocyte hypertrophy and cardiac dilation with compromised systolic function. J Mol Cell Cardiol 31:2063–2076PubMedCrossRef
116.
Milner DJ, Weitzer G, Tran D, Bradley A, Capetanaki Y (1996) Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J Cell Biol 134:1255–1270PubMedCrossRef
117.
Mitsui T, Kawajiri M, Kunishige M, Endo T, Akaike M, Aki K, Matsumoto T (2000) Functional association between nicotinic acetylcholine receptor and sarcomeric proteins via actin and desmin filaments. J Cell Biochem 77:584–595PubMedCrossRef
118.
Miyamoto Y, Akita H, Shiga N, Takai E, Iwai C, Mizutani K, Kawai H, Takarada A, Yokoyama M (2001) Frequency and clinical characteristics of dilated cardiomyopathy caused by desmin gene mutation in a Japanese population. Eur Heart J 22:2284–2289PubMedCrossRef
119.
Mizuno Y, Thompson TG, Guyon JR, Lidov HG, Brosius M, Imamura M, Ozawa E, Watkins SC, Kunkel LM (2001) Desmuslin, an intermediate filament protein that interacts with alpha -dystrobrevin and desmin. Proc Natl Acad Sci USA 98:6156–6161PubMedCrossRef
120.
Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y (2004) In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 15:1101–1111PubMedCrossRef
121.
Munoz-Marmol AM, Strasser G, Isamat M, Coulombe PA, Yang Y, Roca X, Vela E, Mate JL, Coll J, Fernandez-Figueras MT, Navas-Palacios JJ, Ariza A, Fuchs E (1998) A dysfunctional desmin mutation in a patient with severe generalized myopathy. Proc Natl Acad Sci USA 95:11312–11317PubMedCrossRef
122.
Nelson WJ, Traub P (1983) Proteolysis of vimentin and desmin by the Ca2 + -activated proteinase specific for these intermediate filament proteins. Mol Cell Biol 3:1146–1156PubMed
123.
Nicolet S, Herrmann H, Aebi U, Strelkov SV (2010) Atomic structure of vimentin coil 2. J Struct Biol 170:369–376PubMedCrossRef
124.
Nitou M, Ishikawa K, Shiojiri N (2000) Immunohistochemical analysis of development of desmin-positive hepatic stellate cells in mouse liver. J Anat 197(Pt 4):635–646PubMedCrossRef
125.
O’Connor CM, Asai DJ, Flytzanis CN, Lazarides E (1981) In vitro translation of the intermediate filament proteins desmin and vimentin. Mol Cell Biol 1:303–309PubMed
126.
Ohlsson M, Hedberg C, Bradvik B, Lindberg C, Tajsharghi H, Danielsson O, Melberg A, Udd B, Martinsson T, Oldfors A (2012) Hereditary myopathy with early respiratory failure associated with a mutation in A-band titin. Brain 135:1682–1694PubMedCrossRef
127.
Ohtakara K, Inada H, Goto H, Taki W, Manser E, Lim L, Izawa I, Inagaki M (2000) p21-activated kinase PAK phosphorylates desmin at sites different from those for Rho-associated kinase. Biochem Biophys Res Commun 272:712–716PubMedCrossRef
128.
Olive M, Armstrong J, Miralles F, Pou A, Fardeau M, Gonzalez L, Martinez F, Fischer D, Martinez Matos JA, Shatunov A, Goldfarb L, Ferrer I (2007) Phenotypic patterns of desminopathy associated with three novel mutations in the desmin gene. Neuromuscul Disord 17:443–450PubMedCrossRef
129.
Olive M, Goldfarb L, Moreno D, Laforet E, Dagvadorj A, Sambuughin N, Martinez-Matos JA, Martinez F, Alio J, Farrero E, Vicart P, Ferrer I (2004) Desmin-related myopathy: clinical, electrophysiological, radiological, neuropathological and genetic studies. J Neurol Sci 219:125–137PubMedCrossRef
130.
Olive M, Odgerel Z, Martinez A, Poza JJ, Bragado FG, Zabalza RJ, Jerico I, Gonzalez-Mera L, Shatunov A, Lee HS, Armstrong J, Maravi E, Arroyo MR, Pascual-Calvet J, Navarro C, Paradas C, Huerta M, Marquez F, Rivas EG, Pou A, Ferrer I, Goldfarb LG (2011) Clinical and myopathological evaluation of early- and late-onset subtypes of myofibrillar myopathy. Neuromuscul Disord 21:533–542PubMedCrossRef
131.
Olive M, van Leeuwen FW, Janue A, Moreno D, Torrejon-Escribano B, Ferrer I (2008) Expression of mutant ubiquitin (UBB + 1) and p62 in myotilinopathies and desminopathies. Neuropathol Appl Neurobiol 34:76–87PubMed
132.
Omary MB (2009) “IF-pathies”: a broad spectrum of intermediate filament-associated diseases. J Clin Invest 119:1756–1762PubMedCrossRef
133.
Otten E, Asimaki A, Maass A, van Langen IM, van der Wal A, de Jonge N, van den Berg MP, Saffitz JE, Wilde AA, Jongbloed JD, van Tintelen JP (2010) Desmin mutations as a cause of right ventricular heart failure affect the intercalated disks. Heart Rhythm 7:1058–1064PubMedCrossRef
134.
Panagopoulou P, Davos CH, Milner DJ, Varela E, Cameron J, Mann DL, Capetanaki Y (2008) Desmin mediates TNF-alpha-induced aggregate formation and intercalated disk reorganization in heart failure. J Cell Biol 181:761–775PubMedCrossRef
135.
Park KY, Dalakas MC, Goebel HH, Ferrans VJ, Semino-Mora C, Litvak S, Takeda K, Goldfarb LG (2000) Desmin splice variants causing cardiac and skeletal myopathy. J Med Genet 37:851–857PubMedCrossRef
136.
Park KY, Dalakas MC, Semino-Mora C, Lee HS, Litvak S, Takeda K, Ferrans VJ, Goldfarb LG (2000) Sporadic cardiac and skeletal myopathy caused by a de novo desmin mutation. Clin Genet 57:423–429PubMedCrossRef
137.
Paulin D, Huet A, Khanamyrian L, Xue Z (2004) Desminopathies in muscle disease. J Pathol 204:418–427PubMedCrossRef
138.
Pfeffer G, Elliott HR, Griffin H, Barresi R, Miller J, Marsh J, Evila A, Vihola A, Hackman P, Straub V, Dick DJ, Horvath R, Santibanez-Koref M, Udd B, Chinnery PF (2012) Titin mutation segregates with hereditary myopathy with early respiratory failure. Brain 135:1695–1713PubMedCrossRef
139.
Pica EC, Kathirvel P, Pramono ZA, Lai PS, Yee WC (2008) Characterization of a novel S13F desmin mutation associated with desmin myopathy and heart block in a Chinese family. Neuromuscul Disord 18:178–182PubMedCrossRef
140.
Pinol-Ripoll G, Shatunov A, Cabello A, Larrode P, de la Puerta I, Pelegrin J, Ramos FJ, Olive M, Goldfarb LG (2009) Severe infantile-onset cardiomyopathy associated with a homozygous deletion in desmin. Neuromuscul Disord 19:418–422PubMedCrossRef
141.
Pinset C, Montarras D, Chenevert J, Minty A, Barton P, Laurent C, Gros F (1988) Control of myogenesis in the mouse myogenic C2 cell line by medium composition and by insulin: characterization of permissive and inducible C2 myoblasts. Differentiation 38:28–34PubMedCrossRef
142.
Poon E, Howman EV, Newey SE, Davies KE (2002) Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex. J Biol Chem 277:3433–3439PubMedCrossRef
143.
Price MG (1987) Skelemins: cytoskeletal proteins located at the periphery of M-discs in mammalian striated muscle. J Cell Biol 104:1325–1336PubMedCrossRef
144.
Pruszczyk P, Kostera-Pruszczyk A, Shatunov A, Goudeau B, Draminska A, Takeda K, Sambuughin N, Vicart P, Strelkov SV, Goldfarb LG, Kaminska A (2007) Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation. Int J Cardiol 117:244–253PubMedCrossRef
145.
Raats JM, Schaart G, Henderik JB, van der Kemp A, Dunia I, Benedetti EL, Pieper FR, Ramaekers FC, Bloemendal H (1996) Muscle-specific expression of a dominant negative desmin mutant in transgenic mice. Eur J Cell Biol 71:221–236PubMed
146.
Reipert S, Steinbock F, Fischer I, Bittner RE, Zeold A, Wiche G (1999) Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp Cell Res 252:479–491PubMedCrossRef
147.
Robson RM, Huiatt TW, Bellin RM (2004) Muscle intermediate filament proteins. Methods Cell Biol 78:519–553PubMedCrossRef
148.
Rogatsch H, Jezek D, Hittmair A, Mikuz G, Feichtinger H (1996) Expression of vimentin, cytokeratin, and desmin in Sertoli cells of human fetal, cryptorchid, and tumour-adjacent testicular tissue. Virchows Arch 427:497–502PubMedCrossRef
149.
Sam M, Shah S, Friden J, Milner DJ, Capetanaki Y, Lieber RL (2000) Desmin knockout muscles generate lower stress and are less vulnerable to injury compared with wild-type muscles. Am J Physiol Cell Physiol 279:C1116–C1122PubMed
150.
Sandoval IV, Colaco CA, Lazarides E (1983) Purification of the intermediate filament-associated protein, synemin, from chicken smooth muscle. Studies on its physicochemical properties, interaction with desmin, and phosphorylation. J Biol Chem 258:2568–2576PubMed
151.
Sarparanta J, Jonson PH, Golzio C, Sandell S, Luque H, Screen M, McDonald K, Stajich JM, Mahjneh I, Vihola A, Raheem O, Penttila S, Lehtinen S, Huovinen S, Palmio J, Tasca G, Ricci E, Hackman P, Hauser M, Katsanis N, Udd B (2012) Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy. Nat Genet 44(450–455):S451–S452
152.
Sax CM, Farrell FX, Zehner ZE (1989) Down-regulation of vimentin gene expression during myogenesis is controlled by a 5′-flanking sequence. Gene 78:235–242PubMedCrossRef
153.
Schaffeld M, Herrmann H, Schultess J, Markl J (2001) Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: sequence, expression patterns and in vitro assembly. Eur J Cell Biol 80:692–702PubMedCrossRef
154.
Schmid E, Schiller DL, Grund C, Stadler J, Franke WW (1983) Tissue type-specific expression of intermediate filament proteins in a cultured epithelial cell line from bovine mammary gland. J Cell Biol 96:37–50PubMedCrossRef
155.
Schopferer M, Bär H, Hochstein B, Sharma S, Mücke N, Herrmann H, Willenbacher N (2009) Desmin and vimentin intermediate filament networks: their viscoelastic properties investigated by mechanical rheometry. J Mol Biol 388:133–143PubMedCrossRef
156.
Schramm N, Born C, Weckbach S, Reilich P, Walter MC, Reiser MF (2008) Involvement patterns in myotilinopathy and desminopathy detected by a novel neuromuscular whole-body MRI protocol. Eur Radiol 18:2922–2936PubMedCrossRef
157.
Schrickel JW, Stockigt F, Krzyzak W, Paulin D, Li Z, Lubkemeier I, Fleischmann B, Sasse P, Linhart M, Lewalter T, Nickenig G, Lickfett L, Schroder R, Clemen CS (2010) Cardiac conduction disturbances and differential effects on atrial and ventricular electrophysiological properties in desmin deficient mice. J Interv Card Electrophysiol 28:71–80PubMedCrossRef
158.
Schröder R, Goudeau B, Simon MC, Fischer D, Eggermann T, Clemen CS, Li Z, Reimann J, Xue Z, Rudnik-Schoneborn S, Zerres K, van der Ven PF, Fürst DO, Kunz WS, Vicart P (2003) On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria. Hum Mol Genet 12:657–669PubMedCrossRef
159.
Schröder R, Goudeau B, Simon MC, Fischer D, Eggermann T, Clemen CS, Li Z, Reimann J, Xue Z, Rudnik-Schoneborn S, Zerres K, van der Ven PF, Fürst DO, Kunz WS, Vicart P (2007) Erratum for: “On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria”. Hum Mol Genet 16:2989–2990CrossRef
160.
Schröder R, Schoser B (2009) Myofibrillar myopathies: a clinical and myopathological guide. Brain Pathol 19:483–492PubMedCrossRef
161.
162.
Schröder R, Warlo I, Herrmann H, van der Ven PF, Klasen C, Blumcke I, Mundegar RR, Furst DO, Goebel HH, Magin TM (1999) Immunogold EM reveals a close association of plectin and the desmin cytoskeleton in human skeletal muscle. Eur J Cell Biol 78:288–295PubMedCrossRef
163.
Schweitzer SC, Klymkowsky MW, Bellin RM, Robson RM, Capetanaki Y, Evans RM (2001) Paranemin and the organization of desmin filament networks. J Cell Sci 114:1079–1089PubMed
164.
165.
Selcen D, Engel AG (2004) Mutations in myotilin cause myofibrillar myopathy. Neurology 62:1363–1371PubMedCrossRef
166.
Selcen D, Ohno K, Engel AG (2004) Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients. Brain 127:439–451PubMedCrossRef
167.
Sharma S, Mücke N, Katus HA, Herrmann H, Bär H (2009) Disease mutations in the “head” domain of the extra-sarcomeric protein desmin distinctly alter its assembly and network-forming properties. J Mol Med 87:1207–1219PubMedCrossRef
168.
Sjoberg G, Jiang WQ, Ringertz NR, Lendahl U, Sejersen T (1994) Colocalization of nestin and vimentin/desmin in skeletal muscle cells demonstrated by three-dimensional fluorescence digital imaging microscopy. Exp Cell Res 214:447–458PubMedCrossRef
169.
Sjoberg G, Saavedra-Matiz CA, Rosen DR, Wijsman EM, Borg K, Horowitz SH, Sejersen T (1999) A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation. Hum Mol Genet 8:2191–2198PubMedCrossRef
170.
Sparn HG, Lieder-Ochs BA, Franke WW (1994) Immunohistochemical identification and characterization of a special type of desmin-producing stromal cells in human placenta and other fetal tissues. Differentiation 56:191–199PubMedCrossRef
171.
Sprinkart AM, Block W, Traber F, Meyer R, Paulin D, Clemen CS, Schröder R, Gieseke J, Schild H, Thomas D (2011) Characterization of the failing murine heart in a desmin knockout model using a clinical 3 T MRI scanner. Int J Cardiovasc Imaging 28:1699–1705
172.
Steinert PM, Chou YH, Prahlad V, Parry DA, Marekov LN, Wu KC, Jang SI, Goldman RD (1999) A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin. J Biol Chem 274:9881–9890PubMedCrossRef
173.
Strach K, Sommer T, Grohe C, Meyer C, Fischer D, Walter MC, Vorgerd M, Reilich P, Bär H, Reimann J, Reuner U, Germing A, Goebel HH, Lochmuller H, Wintersperger B, Schröder R (2008) Clinical, genetic, and cardiac magnetic resonance imaging findings in primary desminopathies. Neuromuscul Disord 18:475–482PubMedCrossRef
174.
Sugawara M, Kato K, Komatsu M, Wada C, Kawamura K, Shindo PS, Yoshioka PN, Tanaka K, Watanabe S, Toyoshima I (2000) A novel de novo mutation in the desmin gene causes desmin myopathy with toxic aggregates. Neurology 55:986–990PubMedCrossRef
175.
Sung RK, Ursell PC, Rame JE, Bailey H, Caleshu C, Nussbaum RL, Scheinman MM (2011) QTc prolongation and family history of sudden death in a patient with desmin cardiomyopathy. Pacing Clin Electrophysiol 34:e105–e108PubMedCrossRef
176.
Szeverenyi I, Cassidy AJ, Chung CW, Lee BT, Common JE, Ogg SC, Chen H, Sim SY, Goh WL, Ng KW, Simpson JA, Chee LL, Eng GH, Li B, Lunny DP, Chuon D, Venkatesh A, Khoo KH, McLean WH, Lim YP, Lane EB (2008) The Human Intermediate Filament Database: comprehensive information on a gene family involved in many human diseases. Hum Mutat 29:351–360PubMedCrossRef
177.
Tam JL, Triantaphyllopoulos K, Todd H, Raguz S, de Wit T, Morgan JE, Partridge TA, Makrinou E, Grosveld F, Antoniou M (2006) The human desmin locus: gene organization and LCR-mediated transcriptional control. Genomics 87:733–746PubMedCrossRef
178.
Taylor MR, Slavov D, Ku L, Di Lenarda A, Sinagra G, Carniel E, Haubold K, Boucek MM, Ferguson D, Graw SL, Zhu X, Cavanaugh J, Sucharov CC, Long CS, Bristow MR, Lavori P, Mestroni L (2007) Prevalence of desmin mutations in dilated cardiomyopathy. Circulation 115:1244–1251PubMedCrossRef
179.
Thornell L, Carlsson L, Li Z, Mericskay M, Paulin D (1997) Null mutation in the desmin gene gives rise to a cardiomyopathy. J Mol Cell Cardiol 29:2107–2124PubMedCrossRef
180.
181.
Tolstonog GV, Wang X, Shoeman R, Traub P (2000) Intermediate filaments reconstituted from vimentin, desmin, and glial fibrillary acidic protein selectively bind repetitive and mobile DNA sequences from a mixture of mouse genomic DNA fragments. DNA Cell Biol 19:647–677PubMedCrossRef
182.
Traub P (1995) Intermediate filaments and gene regulation. Physiol Chem Phys Med NMR 27:377–400PubMed
183.
van Spaendonck-Zwarts K, van Hessem L, Jongbloed JD, de Walle HE, Capetanaki Y, van der Kooi AJ, van Langen IM, van den Berg MP, van Tintelen JP (2010) Desmin-related myopathy: a review and meta-analysis. Clin Genet 80:354–366CrossRef
184.
van Spaendonck-Zwarts KY, van der Kooi AJ, van den Berg MP, Ippel EF, Boven LG, Yee WC, van den Wijngaard A, Brusse E, Hoogendijk JE, Doevendans PA, de Visser M, Jongbloed JD, van Tintelen JP (2012) Recurrent and founder mutations in the Netherlands: the cardiac phenotype of DES founder mutations p.S13F and p.N342D. Neth Heart J 20:219–228PubMedCrossRef
185.
van Tintelen JP, Van Gelder IC, Asimaki A, Suurmeijer AJ, Wiesfeld AC, Jongbloed JD, van den Wijngaard A, Kuks JB, van Spaendonck-Zwarts KY, Notermans N, Boven L, van den Heuvel F, Veenstra-Knol HE, Saffitz JE, Hofstra RM, van den Berg MP (2009) Severe cardiac phenotype with right ventricular predominance in a large cohort of patients with a single missense mutation in the DES gene. Heart Rhythm 6:1574–1583PubMedCrossRef
186.
Vernengo L, Chourbagi O, Panuncio A, Lilienbaum A, Batonnet-Pichon S, Bruston F, Rodrigues-Lima F, Mesa R, Pizzarossa C, Demay L, Richard P, Vicart P, Rodriguez MM (2010) Desmin myopathy with severe cardiomyopathy in a Uruguayan family due to a codon deletion in a new location within the desmin 1A rod domain. Neuromuscul Disord 20:178–187PubMedCrossRef
187.
Vicart P, Caron A, Guicheney P, Li Z, Prevost MC, Faure A, Chateau D, Chapon F, Tome F, Dupret JM, Paulin D, Fardeau M (1998) A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 20:92–95PubMedCrossRef
188.
Vorgias CE, Traub P (1986) Nucleic acid-binding activities of the intermediate filament subunit proteins desmin and glial fibrillary acidic protein. Z Naturforsch C 41:897–909PubMed
189.
Vrabie A, Goldfarb LG, Shatunov A, Nagele A, Fritz P, Kaczmarek I, Goebel HH (2005) The enlarging spectrum of desminopathies: new morphological findings, eastward geographic spread, novel exon 3 desmin mutation. Acta Neuropathol 109:411–417PubMedCrossRef
190.
Wahbi K, Behin A, Charron P, Dunand M, Richard P, Meune C, Vicart P, Laforet P, Stojkovic T, Becane HM, Kuntzer T, Duboc D (2012) High cardiovascular morbidity and mortality in myofibrillar myopathies due to DES gene mutations: a 10-year longitudinal study. Neuromuscul Disord 22:211–218PubMedCrossRef
191.
Walter MC, Reilich P, Huebner A, Fischer D, Schröder R, Vorgerd M, Kress W, Born C, Schoser BG, Krause KH, Klutzny U, Bulst S, Frey JR, Lochmüller H (2007) Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum of adult-onset, dominant myopathies are associated with the desmin mutation R350P. Brain 130:1485–1496PubMedCrossRef
192.
Wang Q, Tolstonog GV, Shoeman R, Traub P (2001) Sites of nucleic acid binding in type I-IV intermediate filament subunit proteins. Biochemistry 40:10342–10349PubMedCrossRef
193.
Wang X, Klevitsky R, Huang W, Glasford J, Li F, Robbins J (2003) αB-Crystallin Modulates Protein Aggregation of Abnormal Desmin. Circ Res 93:998–1005PubMedCrossRef
194.
Wang X, Osinska H, Dorn GW 2nd, Nieman M, Lorenz JN, Gerdes AM, Witt S, Kimball T, Gulick J, Robbins J (2001) Mouse model of desmin-related cardiomyopathy. Circulation 103:2402–2407PubMedCrossRef
195.
Wang X, Osinska H, Klevitsky R, Gerdes AM, Nieman M, Lorenz J, Hewett T, Robbins J (2001) Expression of R120G-alphaB-crystallin causes aberrant desmin and alphaB-crystallin aggregation and cardiomyopathy in mice. Circ Res 89:84–91PubMedCrossRef
196.
Weisleder N, Taffet GE, Capetanaki Y (2004) Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy. Proc Natl Acad Sci USA 101:769–774PubMedCrossRef
197.
Wieneke S, Stehle R, Li Z, Jockusch H (2000) Generation of tension by skinned fibers and intact skeletal muscles from desmin-deficient mice. Biochem Biophys Res Commun 278:419–425PubMedCrossRef
198.
Yuan J, Huiatt TW, Liao CX, Robson RM, Graves DJ (1999) The effects of mono-ADP-ribosylation on desmin assembly-disassembly. Arch Biochem Biophys 363:314–322PubMedCrossRef
199.
Yuri T, Miki K, Tsukamoto R, Shinde A, Kusaka H, Tsubura A (2007) Autopsy case of desminopathy involving skeletal and cardiac muscle. Pathol Int 57:32–36PubMedCrossRef
200.
Zheng Q, Su H, Ranek MJ, Wang X (2011) Autophagy and p62 in cardiac proteinopathy. Circ Res 109:296–308PubMedCrossRef
201.
Zhou H, Huiatt TW, Robson RM, Sernett SW, Graves DJ (1996) Characterization of ADP-ribosylation sites on desmin and restoration of desmin intermediate filament assembly by de-ADP-ribosylation. Arch Biochem Biophys 334:214–222PubMedCrossRef
Metadata
Title
Desminopathies: pathology and mechanisms
Authors
Christoph S. Clemen
Harald Herrmann
Sergei V. Strelkov
Rolf Schröder
Publication date
01-01-2013
Publisher
Springer-Verlag
Published in
Acta Neuropathologica / Issue 1/2013
Print ISSN: 0001-6322
Electronic ISSN: 1432-0533
DOI
https://doi.org/10.1007/s00401-012-1057-6

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