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Title: Desmin  
Author: World Heritage Encyclopedia
Language: English
Subject: Dilated cardiomyopathy, Intermediate filament, Cytoskeleton, Arrhythmogenic right ventricular dysplasia, Myofibroblast
Collection: Tumor Markers
Publisher: World Heritage Encyclopedia


Symbols  ; CSM1; CSM2; LGMD2R
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Desmin is a protein that in humans is encoded by the DES gene.[1][2] Desmin is a muscle-specific, type III[3] intermediate filament that integrates the sarcolemma, Z disk and nuclear membrane in sarcomeres and regulates sarcomere architecture.[4]


  • Structure 1
  • Function 2
  • Clinical significance 3
  • References 4
  • External links 5


Desmin is a 53.5 kD protein composed of 470 amino acids.[5][6] There are three major domains to the desmin protein: a conserved

  • GeneReviews/NIH/NCBI/UW entry on Myofibrillar Myopathy
  • Desmin at the US National Library of Medicine Medical Subject Headings (MeSH)
  • LOVD mutation database: DES

External links

  1. ^ Muñoz-Mármol AM, Strasser G, Isamat M, Coulombe PA, Yang Y, Roca X, Vela E, Mate JL, Coll J, Fernández-Figueras MT, Navas-Palacios JJ, Ariza A, Fuchs E (September 1998). "A dysfunctional desmin mutation in a patient with severe generalized myopathy". Proc. Natl. Acad. Sci. U.S.A. 95 (19): 11312–7.  
  2. ^ a b Li ZL, Lilienbaum A, Butler-Browne G, Paulin D (May 1989). "Human desmin-coding gene: complete nucleotide sequence, characterization and regulation of expression during myogenesis and development". Gene 78 (2): 243–54.  
  3. ^ The Human Protein Atlas. Retrieved on 2013-07-29.
  4. ^ Sequeira V, Nijenkamp LL, Regan JA, van der Velden J (Feb 2014). "The physiological role of cardiac cytoskeleton and its alterations in heart failure". Biochimica Et Biophysica Acta 1838 (2): 700–22.  
  5. ^ "Mass spectrometry characterization of human DES at COPaKB". 
  6. ^ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research 113 (9): 1043–53.  
  7. ^ a b c d e f g h i Bär H, Strelkov SV, Sjöberg G, Aebi U, Herrmann H (November 2004). "The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation?". J. Struct. Biol. 148 (2): 137–52.  
  8. ^ a b Li Z, Mericskay M, Agbulut O, Butler-Browne G, Carlsson L, Thornell LE, Babinet C, Paulin D (October 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 (1): 129–44.  
  9. ^ Meng JJ, Bornslaeger EA, Green KJ, Steinert PM, Ip W (August 1997). "Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments". J. Biol. Chem. 272 (34): 21495–503.  
  10. ^ Bennardini F, Wrzosek A, Chiesi M (Aug 1992). "Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments". Circulation Research 71 (2): 288–94.  
  11. ^ Lazarides E, Hubbard BD (December 1976). "Immunological characterization of the subunit of the 100 A filaments from muscle cells". Proc. Natl. Acad. Sci. U.S.A. 73 (12): 4344–8.  
  12. ^ Izant JG, Lazarides E (April 1977). "Invariance and heterogeneity in the major structural and regulatory proteins of chick muscle cells revealed by two-dimensional gel electrophoresis". Proc. Natl. Acad. Sci. U.S.A. 74 (4): 1450–4.  
  13. ^ Costa ML, Escaleira R, Cataldo A, Oliveira F, Mermelstein CS (December 2004). "Desmin: molecular interactions and putative functions of the muscle intermediate filament protein". Braz. J. Med. Biol. Res. 37 (12): 1819–30.  
  14. ^ Stoeckert C (1997-03-16). "Dystrophin". Catalogue of Regulatory Elements. University of Pennsylvania. Retrieved 2010-06-28. 
  15. ^ Milner DJ, Weitzer G, Tran D, Bradley A, Capetanaki Y (Sep 1996). "Disruption of muscle architecture and myocardial degeneration in mice lacking desmin". The Journal of Cell Biology 134 (5): 1255–70.  
  16. ^ Milner DJ, Taffet GE, Wang X, Pham T, Tamura T, Hartley C, Gerdes AM, Capetanaki Y (Nov 1999). "The absence of desmin leads to cardiomyocyte hypertrophy and cardiac dilation with compromised systolic function". Journal of Molecular and Cellular Cardiology 31 (11): 2063–76.  
  17. ^ a b Paulin D, Li Z (November 2004). "Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle". Exp. Cell Res. 301 (1): 1–7.  
  18. ^ a b Shah SB, Davis J, Weisleder N, Kostavassili I, McCulloch AD, Ralston E, Capetanaki Y, Lieber RL (May 2004). "Structural and functional roles of desmin in mouse skeletal muscle during passive deformation". Biophys. J. 86 (5): 2993–3008.  
  19. ^ Heling A, Zimmermann R, Kostin S, Maeno Y, Hein S, Devaux B, Bauer E, Klövekorn WP, Schlepper M, Schaper W, Schaper J (Apr 2000). "Increased expression of cytoskeletal, linkage, and extracellular proteins in failing human myocardium". Circulation Research 86 (8): 846–53.  
  20. ^ Milner DJ, Mavroidis M, Weisleder N, Capetanaki Y (2000). "Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function.". Journal of Cell Biology 150: 1283–1298.  
  21. ^ Goldfarb LG, Vicart P, Goebel HH, Dalakas MC (April 2004). "Desmin myopathy". Brain 127 (Pt 4): 723–34.  
  22. ^ Li D, Tapscoft T, Gonzalez O, Burch PE, Quiñones MA, Zoghbi WA, Hill R, Bachinski LL, Mann DL, Roberts R (Aug 1999). "Desmin mutation responsible for idiopathic dilated cardiomyopathy". Circulation 100 (5): 461–4.  
  23. ^ Goldfarb LG, Park KY, Cervenáková L, Gorokhova S, Lee HS, Vasconcelos O, Nagle JW, Semino-Mora C, Sivakumar K, Dalakas MC (Aug 1998). "Missense mutations in desmin associated with familial cardiac and skeletal myopathy". Nature Genetics 19 (4): 402–3.  
  24. ^ 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 (23): 4595–607.  
  25. ^ Lorenzon A, Beffagna G, Bauce B, De Bortoli M, Li Mura IE, Calore M, Dazzo E, Basso C, Nava A, Thiene G, Rampazzo A (Feb 2013). "Desmin mutations and arrhythmogenic right ventricular cardiomyopathy". The American Journal of Cardiology 111 (3): 400–5.  
  26. ^ Brodehl A, Hedde PN, Dieding M, Fatima A, Walhorn V, Gayda S, Šarić T, Klauke B, Gummert J, Anselmetti D, Heilemann M, Nienhaus GU, Milting H (2012). "Dual color photoactivation localization microscopy of cardiomyopathy-associated desmin mutants". J. Biol. Chem. 287 (19): 16047–57.  
  27. ^ Brodehl A, Dieding M, Klauke B, Dec E, Madaan S, Huang T, Gargus J, Fatima A, Saric T, Cakar H, Walhorn V, Tönsing K, Skrzipczyk T, Cebulla R, Gerdes D, Schulz U, Gummert J, Svendsen JH, Olesen MS, Anselmetti D, Christensen AH, Kimonis V, Milting H (2013). "The novel desmin mutant p.A120D impairs filament formation, prevents intercalated disk localization, and causes sudden cardiac death". Circ Cardiovasc Genet 6 (6): 615–23.  
  28. ^ Saha K, Saha A, Datta C, Chatterjee U, Ray S, Bera M. Does desmin immunohistochemistry have a role in assessing stage of urothelial carcinoma in transurethral resection of bladder tumor specimens? Clin Cancer Investig J 2014;3(6):502-7.DOI: 10.4103/2278-0513.142634


Desmin has been evaluated for role in assessing the depth of invasion of urothelial carcinoma in TURBT specimens.[28]

Desmin-related myofibrillar myopathy (DRM or Desminopathy) is a subgroup of the myofibrillar myopathy diseases and is the result of a mutation in the gene that codes for desmin which prevents it from forming protein filaments, and rather, forms aggregates of desmin and other proteins throughout the cell.[7] Desmin mutations have been associated with restrictive and idopathic cardiomyopathy.;[22][23] and recently, mutations were identified in patients with arrhythmogenic right ventricular cardiomyopathy (ARVC).[24][25] Some of these DES mutations like p.N116S or p.E114del cause an aggregation of desmin within the cytoplasm.[26] A mutation p.A120D was discovered in a family where several members had sudden cardiac death.[27]

Clinical significance

In adult desmin-null mice, hearts from 10 wk-old animals showed drastic alterations in muscle architecture, including a misalignment of myofibrils and disorganization and swelling of mitochondria; findings that were more severe in cardiac relative to skeletal muscle. Cardiac tissue also exhibited progressive necrosis and calcification of the myocardium.[15] A separate study examined this in more detail in cardiac tissue and found that murine hearts lacking desmin developed hypertrophic cardiomyopathy and chamber dilation combined with systolic dysfunction.[16] In adult muscle, desmin forms a scaffold around the Z-disk of the sarcomere and connects the Z-disk to the subsarcolemmal cytoskeleton.[17] It links the myofibrils laterally by connecting the Z-disks.[7] Through its connection to the sarcomere, desmin connects the contractile apparatus to the cell nucleus, mitochondria, and post-synaptic areas of motor endplates.[7] These connections maintain the structural and mechanical integrity of the cell during contraction while also helping in force transmission and longitudinal load bearing.[17][18] In human heart failure, desmin expression is upregulated, which has been hyopthesized to be a defense mechanism in an attempt to maintain normal sarcomere alignment amidst disease pathogenesis.[19] There is some evidence that desmin may also connect the sarcomere to the extracellular matrix (ECM) through desmosomes which could be important in signalling between the ECM and the sarcomere which could regulate muscle contraction and movement.[18] Finally, desmin may be important in mitochondria function. When desmin is not functioning properly there is improper mitochondrial distribution, number, morphology and function.[20][21] Since desmin links the mitochondria to the sarcomere it may transmit information about contractions and energy need and through this regulate the aerobic respiration rate of the muscle cell.

Desmin was first described in 1976,[11] first purified in 1977,[12] the gene was cloned in 1989,[2] and the first knockout mouse was created in 1996.[13] The function of desmin has been deduced through studies in knockout mice. Desmin is one of the earliest protein markers for muscle tissue in embryogenesis as it is detected in the somites.[7] Although it is present early in the development of muscle cells, it is only expressed at low levels, and increases as the cell nears terminal differentiation. A similar protein, vimentin, is present in higher amounts during embryogenesis while desmin is present in higher amounts after differentiation. This suggests that there may be some interaction between the two in determining muscle cell differentiation. However desmin knockout mice develop normally and only experience defects later in life.[8] Since desmin is expressed at a low level during differentiation another protein may be able to compensate for desmin's function early in development but not later on.[14]


[10].αB-crystallin and [9]desmoplakin with interact. Desmin has been shown to intercalated discs and Z-discs In cardiac muscle, desmin is present in [8] tissue.smooth muscle and skeletal muscle, cardiac muscle Desmin is a subunit of intermediate filaments in [7]

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