Recessive MYL2 mutations cause infantile type i muscle fibre disease and cardiomyopathy

Brain

Volumn 136, Issue 1, 2013, Pages 282-293

  Weterman, Marian A J ^a   Barth, Peter G ^b   Van Spaendonck Zwarts, Karin Y ^a,c   Aronica, Eleonora ^a   Poll The, Bwee Tien ^b   Brouwer, Oebele F ^c   Van Tintelen, J Peter ^c   Qahar, Zohal ^a   Bradley, Edward J ^a   De Wissel, Marit ^a   Salviati, Leonardo ^d   Angelini, Corrado ^d   Van Den Heuvel, Lambertus ^e   Thomasse, Yolande E M ^f,h   Backx, Ad P ^c   Nürnberg, Gudrun ^b,g   Nürnberg, Peter ^b,g   Baas, Frank ^a  

^a ACADEMIC MEDICAL CENTER   (Netherlands)

^b EMMA CHILDREN S HOSPITAL   (Netherlands)

^c UNIVERSITY MEDICAL CENTER GRONINGEN   (Netherlands)

^d UNIVERSITY OF PADOVA   (Italy)

^e IRCCS SAN CAMILLO HOSPITAL   (Italy)

^f RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^g UNIVERSITY OF COLOGNE   (Germany)

^h Department of Neurology University of Padua ^*  (Netherlands)

Author keywords

light chain myopathy; MYL2; myosin regulatory light chain; myosinopathy; type I hypotrophy

Indexed keywords

CALCIUM; MUTANT PROTEIN; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN 2;

ALTERNATIVE RNA SPLICING; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHROMOSOME 12; CLINICAL ARTICLE; CLINICAL FEATURE; CODON; COMPLEX FORMATION; CONGESTIVE CARDIOMYOPATHY; CONTROLLED STUDY; DIAGNOSTIC TEST ACCURACY STUDY; EXON; FEMALE; FRAMESHIFT MUTATION; GENE EXPRESSION; GENE LINKAGE DISEQUILIBRIUM; GENE TARGETING; HEREDITY; HETEROZYGOSITY; HOMOZYGOSITY; HUMAN; HUMAN TISSUE; HYPERTROPHIC CARDIOMYOPATHY; INFANT; INFANTILE TYPE 1 MUSCLE FIBER DISEASE; MALE; MISSENSE MUTATION; MULTICENTER STUDY; MUSCLE ATROPHY; MUSCLE CELL; MUSCLE CONTRACTION; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; RISK FACTOR; SCORING SYSTEM; SEQUENCE ANALYSIS; SKELETAL MUSCLE;

EID: 84873381040     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/aws293     Document Type: Article

References (56)

1. Abecasis GR, Cherny SS, Cookson WO, Cardon LR. GRR: graphical representation of relationship errors. Bioinformatics 2001; 17: 742-3.
2. Andersen PS, Havndrup O, Bundgaard H, Moolman-Smook JC, Larsen LA, Mogensen J, et al. Myosin light chain mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations. J Med Genet 2001; 38: E43.
3. Barth PG, Wanders RJ, Ruitenbeek W, Roe C, Scholte HR, van der Harten H, et al. Infantile fibre type disproportion, myofibrillar lysis and cardiomyopathy: a disorder in three unrelated Dutch families. Neuromuscul Disord 1998; 8: 296-304.
4. Brandis A, Aronica E, Goebel HH. TPM2 mutation. Neuromuscul Disord 2008; 18: 1005.
5. Budde BS, Namavar Y, Barth PG, Poll-The BT, Nurnberg G, Becker C, et al. tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia. Nat Genet 2008; 40: 1113-18.
6. Chen J, Kubalak SW, Minamisawa S, Price RL, Becker KD, Hickey R, et al. Selective requirement of myosin light chain 2v in embryonic heart function. J Biol Chem 1998; 273: 1252-6.
7. Clarke NF, North KN. Congenital fiber type disproportion-30 years on. J Neuropathol Exp Neurol 2003; 62: 977-89.
8. Clarke NF, Kidson W, Quijano-Roy S, Estournet B, Ferreiro A, Guicheney P, et al. SEPN1: associated with congenital fiber-type disproportion and insulin resistance. Ann Neurol 2006; 59: 546-52.
9. Clarke NF, Kolski H, Dye DE, Lim E, Smith RL, Patel R, et al. Mutations in TPM3 are a common cause of congenital fiber type disproportion. Ann Neurol 2008; 63: 329-37.
10. Clarke NF, Waddell LB, Cooper ST, Perry M, Smith RL, Kornberg AJ, et al. Recessive mutations in RYR1 are a common cause of congenital fiber type disproportion. Hum Mutat 2010; 31: E1544-50.
11. Darin N, Tajsharghi H, Ostman-Smith I, Gilljam T, Oldfors A. New skeletal myopathy and cardiomyopathy associated with a missense mutation in MYH7. Neurology 2007; 68: 2041-2.
12. Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, et al. The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation. Cell 2001; 107: 631-41.
13. Dubowitz V. Definition of pathological changes seen in muscle biopsies. In: Dubowitz V, editor. Muscle biopsy. A practical approach. 2nd edn. London: Baillière Tindall; 1985. p. 82-128.
14. Flavigny J, Richard P, Isnard R, Carrier L, Charron P, Bonne G, et al. Identification of two novel mutations in the ventricular regulatory myosin light chain gene (MYL2) associated with familial and classical forms of hypertrophic cardiomyopathy. J Mol Med (Berl) 1998; 76: 208-14.
15. Grey C, Mery A, Puceat M. Fine-tuning in Ca2+ homeostasis underlies progression of cardiomyopathy in myocytes derived from genetically modified embryonic stem cells. Hum Mol Genet 2005; 14: 1367-77.
16. Gudbjartsson DF, Jonasson K, Frigge ML, Kong A. Allegro, a new computer program for multipoint linkage analysis. Nat Genet 2000; 25: 12-13.
17. Hailstones D, Barton P, Chan-Thomas P, Sasse S, Sutherland C, Hardeman E, et al. Differential regulation of the atrial isoforms of the myosin light chains during striated muscle development. J Biol Chem 1992; 267: 23295-300.
18. Hang CT, Yang J, Han P, Cheng HL, Shang C, Ashley E, et al. Chromatin regulation by Brg1 underlies heart muscle development and disease. Nature 2010; 466: 62-7.
19. Harrison BC, Allen DL, Leinwand LA. IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men. Skelet Muscle 2011; 1: 5.
20. Kabaeva ZT, Perrot A, Wolter B, Dietz R, Cardim N, Correia JM, et al. Systematic analysis of the regulatory and essential myosin light chain genes: genetic variants and mutations in hypertrophic cardiomyopathy. Eur J Hum Genet 2002; 10: 741-8.
21. Kazmierczak K, Muthu P, Huang W, Jones M, Wang Y, Szczesna-Cordary D. Myosin regulatory light chain mutation found in hyper-trophic cardiomyopathy patients increases isometric force production in transgenic mice. Biochem J 2012; 442: 95-103.
22. Kedar V, McDonough H, Arya R, Li HH, Rockman HA, Patterson C. Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci USA 2004; 101: 18135-40.
23. Kelly DP, Strauss AW. Inherited cardiomyopathies. N Engl J Med 1994; 330: 913-19.
24. Kerrick WG, Kazmierczak K, Xu Y, Wang Y, Szczesna-Cordary D. Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice. FASEB J 2009; 23: 855-65.
25. Koyama S, Hata S, Witt CC, Ono Y, Lerche S, Ojima K, et al. Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis. J Mol Biol 2008; 376: 1224-36.
26. Laing NG, Clarke NF, Dye DE, Liyanage K, Walker KR, Kobayashi Y, et al. Actin mutations are one cause of congenital fibre type disproportion. Ann Neurol 2004; 56: 689-94.
27. Laing NG, Laing BA, Meredith C, Wilton SD, Robbins P, Honeyman K, et al. Autosomal dominant distal myopathy: linkage to chromosome 14. Am J Hum Genet 1995; 56: 422-7.
28. Li Y, Wu G, Tang Q, Jiang H, Shi L, Tu X, et al. Slow cardiac myosin regulatory light chain 2 (MYL2) was down-expressed in chronic heart failure patients. Clin Cardiol 2011; 34: 30-4.
29. Lowey S, Waller GS, Trybus KM. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature 1993; 365: 454-6.
30. Macera MJ, Szabo P, Wadgaonkar R, Siddiqui MA, Verma RS. Localization of the gene coding for ventricular myosin regulatory light chain (MYL2) to human chromosome 12q23-q24.3. Genomics 1992; 13: 829-31.
31. Minamisawa S, Gu Y, Ross J Jr, Chien KR, Chen J. A post-transcriptional compensatory pathway in heterozygous ventricular myosin light chain 2-deficient mice results in lack of gene dosage effect during normal cardiac growth or hypertrophy. J Biol Chem 1999; 274: 10066-70.
32. Muelas N, Hackman P, Luque H, Garces-Sanchez M, Azorin I, Suominen T, et al. MYH7 gene tail mutation causing myopathic profiles beyond Laing distal myopathy. Neurology 2010; 75: 732-41.
33. Muthu P, Mettikolla P, Calander N, Luchowski R, Gryczynski I, Gryczynski Z, et al. Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart. J Mol Cell Cardiol 2010; 48: 989-98.
34. Nakao K, Minobe W, Roden R, Bristow MR, Leinwand LA. Myosin heavy chain gene expression in human heart failure. J Clin Invest 1997; 100: 2362-70.
35. Ortolano S, Tarrio R, Blanco-Arias P, Teijeira S, Rodriguez-Trelles F, Garcia-Murias M, et al. A novel MYH7 mutation links congenital fiber type disproportion and myosin storage myopathy. Neuromuscul Disord 2011; 21: 254-62.
36. Perera S, Holt MR, Mankoo BS, Gautel M. Developmental regulation of MURF ubiquitin ligases and autophagy proteins nbr1, p62/SQSTM1 and LC3 during cardiac myofibril assembly and turnover. Dev Biol 2011; 351: 46-61.
37. Poetter K, Jiang H, Hassanzadeh S, Master SR, Chang A, Dalakas MC, et al. Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle. Nat Genet 1996; 13: 63-9.
38. Richard P, Charron P, Carrier L, Ledeuil C, Cheav T, Pichereau C, et al. Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy. Circulation 2003; 107: 2227-32.
39. Ruschendorf F, Nurnberg P. ALOHOMORA: a tool for linkage analysis using 10K SNP array data. Bioinformatics 2005; 21: 2123-5.
40. Rutsch F, Gailus S, Miousse IR, Suormala T, Sagné C, Toliat MR, et al. Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism. Nat Genet 2009; 41: 234-9.
41. Sanoudou D, Beggs AH. Clinical and genetic heterogeneity in nemaline myopathy-a disease of skeletal muscle thin filaments. Trends Mol Med 2001; 7: 362-8.
42. Schiaffino S, Reggiani C. Fiber types in mammalian skeletal muscles. Physiol Rev 2011; 91: 1447-531.
43. Szczesna D, Ghosh D, Li Q, Gomes AV, Guzman G, Arana C, et al. Familial hypertrophic cardiomyopathy mutations in the regulatory light chains of myosin affect their structure, Ca2 + binding, and phos-phorylation. J Biol Chem 2001; 276: 7086-92.
44. Szczesna-Cordary D, Guzman G, Ng SS, Zhao J. Familial hypertrophic cardiomyopathy-linked alterations in Ca2+ binding of human cardiac myosin regulatory light chain affect cardiac muscle contraction. J Biol Chem 2004; 279: 3535-42.
45. Szczesna-Cordary D, Guzman G, Zhao J, Hernandez O, Wei J, Diaz-Perez Z. The E22K mutation of myosin RLC that causes familial hyper-trophic cardiomyopathy increases calcium sensitivity of force and ATPase in transgenic mice. J Cell Sci 2005; 118: 3675-83.
46. Tajsharghi H, Thornell LE, Lindberg C, Lindvall B, Henriksson KG, Oldfors A. Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. Ann Neurol 2003; 54: 494-500.
47. Thiele H, Nurnberg P. HaploPainter: a tool for drawing pedigrees with complex haplotypes. Bioinformatics 2005; 21: 1730-2.
48. Uyeda TQ, Spudich JA. A functional recombinant myosin II lacking a regulatory light chain-binding site. Science 1993; 262: 1867-70.
49. van Rooij E, Sutherland LB, Qi X, Richardson JA, Hill J, Olson EN. Control of stress-dependent cardiac growth and gene expression by a microRNA. Science 2007; 316: 575-9.
50. VanBuren P, Waller GS, Harris DE, Trybus KM, Warshaw DM, Lowey S. The essential light chain is required for full force production by skeletal muscle myosin. Proc Natl Acad Sci USA 1994; 91: 12403-7.
51. Wadgaonkar R, Shafiq S, Rajmanickam C, Siddiqui MA. Interaction of a conserved peptide domain in recombinant human ventricular myosin light chain-2 with myosin heavy chain. Cell Mol Biol Res 1993; 39: 13-26.
52. Walsh R, Rutland C, Thomas R, Loughna S. Cardiomyopathy: a systematic review of disease-causing mutations in myosin heavy chain 7 and their phenotypic manifestations. Cardiology 2010; 115: 49-60.
53. Weiss A, Leinwand LA. The mammalian myosin heavy chain gene family. Annu Rev Cell Dev Biol 1996; 12: 417-39.
54. Weterman MA, Sorrentino V, Kasher PR, Jakobs ME, van Engelen BG, Fluiter K, et al. A frameshift mutation in LRSAM1 is responsible for a dominant hereditary polyneuropathy. Hum Mol Genet 2012; 21: 358-70.
55. Wimberly B, Thulin E, Chazin WJ. Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant. Protein Sci 1995; 4: 1045-55.
56. Witt SH, Granzier H, Witt CC, Labeit S. MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination. J Mol Biol 2005; 350: 713-22.