Glycosylation defects in muscular dystrophies

Current Opinion in Neurology

Volumn 17, Issue 5, 2004, Pages 521-527

  Haliloǧlu, Göknur ^a   Topaloǧlu, Haluk ^a  

^a HACETTEPE UNIVERSITY   (Turkey)

Author keywords

dystroglycan; Glycosylation; Muscular dystrophies; Sialidation

Indexed keywords

DYSTROGLYCAN; GLYCAN; GLYCOCONJUGATE; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; LARGE PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

AUTOSOMAL RECESSIVE DISORDER; BIOCHEMISTRY; CARBOHYDRATE METABOLISM; CARBOHYDRATE SYNTHESIS; CELL INCLUSION; DISTAL MYOPATHY; FUKUYAMA CONGENITAL MUSCULAR DYSTROPHY; GENE MUTATION; GENE TRANSFER; HEREDITARY INCLUSION BODY MYOPATHY; HUMAN; LIMB GIRDLE MUSCULAR DYSTROPHY; MISSENSE MUTATION; MUSCLE EYE BRAIN DISEASE; MUSCULAR DYSTROPHY; NONAKA MYOPATHY; NONHUMAN; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING; REVIEW; WALKER WARBURG SYNDROME;

ANIMALS; DYSTROGLYCANS; GLYCOSYLATION; HUMANS; MUSCULAR DYSTROPHIES;

EID: 6944237265     PISSN: 13507540     EISSN: None     Source Type: Journal    
DOI: 10.1097/00019052-200410000-00002     Document Type: Review

References (57)

1. Jaeken J. Komrower lecture Congenital disorders of glycosylation (CDG): it's all in it. J Inherit Metab Dis 2003; 26:99-118. A general review of CDG.
2. Marquardt T, Denecke J. Congenital disorders of glycosylation. Review of their molecular bases, clinical presentations and specific therapies. Eur J Pediatr 2003; 162:359-379.
3. Martin PT, Freeze HH. Glycobiology of neuromuscular disorders. Glycobiology 2003; 13:67R-75R. A detailed overview of glycosylation defects in muscle.
4. Grewal PK, Hewitt JE. Glycosylation defects: a new mechanism for muscular dystrophy? Hum Mol Genet 2003; 12:R259-R264. A review of the topic.
5. Hewitt JE, Grewal PK. Glycosylation defects in inherited muscle disease. Cell Mol Life Sci 2003; 60:251-258.
6. Muntoni F, Brockington M, Blake DJ, et al. Defective glycosylation in muscular dystrophy. Lancet 2002; 360:1419-1421.
7. Muntoni F, Valero de Bernabe B, Bittner R, et al. 114th ENMC International Workshop on Congenital Muscular Dystrophy (CMD). Naarden, the Netherlands 17-19 January 2003 (8th Workshop of the International Consortium on CMD; 3rd Workshop of the MYO-CLUSTER project GENRE). Neuromusc Disord 2003; 13:579-588. The first cases were presented during this meeting.
8. Nishino I, Ozawa E. Muscular dystrophies. Curr Opin Neurol 2002; 15:539-544.
9. Muntoni F, Brockington M, Torelli S, Brown SC. Defective glycosylation in congenital muscular dystrophies. Curr Opin Neurol 2004; 17:205-209. The most recent update focusing on congenital forms.
10. Holzfeind PJ, Grewal PK, Reitsamer HA, et al. Skeletal, cardiac, and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large (myd) mouse defines a natural model for glycosylation-deficient muscle-eye-brain disorders. Hum Mol Genet 2002; 11:2673-2687.
11. Grewal PK, Hewitt JE. Mutation of Large, which encodes a putative glycosyltransferase, in an animal model for muscular dystrophy. Biochim Biophys Acta 2002; 1573:216-224.
12. Longman C, Brockington M, Torelli S, et al. Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of α-dystroglycan. Hum Mol Genet 2003; 12:2853-2861. The first report of a human LARGE mutation.
13. Karpati G, Holland P. Sweeteening the pot in muscle. Genetic defects of protein glycosylation causing muscle disease. Neurology 2002; 59:1674-1676.
14. Michele DE, Campbell KP. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J Biol Chem 2003; 278:15457-15460. A mini review of the dystrophin-glycoprotein complex emphasizing the role of alpha-dystroglycan on neuronal migration.
15. Williamson RA, Henry MD, Daniels KJ, et al. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag-1 null mice. Hum Mol Genet 1997; 6:831-841.
16. Henry MD, Campbell KP. A role for dystroglycan in basement membrane assembly. Cell 1998; 11:859-870.
17. Ervasti JM, Campbell KP. Dystrophin and membrane skeleton. Curr Opin Cell Biol 1993; 5:82-87.
18. Michele DE, Barresi R, Kanawaga M, et al. Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 2002; 418:417-422.
19. Toda T, Segawa M, Nomura Y, et al. Localization of a gene for Fukuyama type CMD to chromosome 9q31-33. Nat Genet 1993; 5:283-286.
20. Toda T, Ikegawa S, Okui K, et al. Refined mapping of a gene responsible for Fukuyama-type congenital muscular dystrophy: evidence for strong linkage disequilibrium. Am J Hum Genet 1994; 55:946-950.
21. Kobayashi K, Nakahori Y, Myake M, et al. An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy. Nature 1998; 394:388-392.
22. Toda T, Kobayashi K, Takeda S, et al. Fukuyama-type congenital muscular dystrophy (FCMD) and alpha-dystroglycanopathy. Congenit Anom Kyoto 2003; 43:97-104.
23. Takeda S, Kondo M, Sasaki J, et al. Fukutin is required for maintenance of muscle integrity, cortical histiogenesis and normal eye development. Hum Mol Genet 2003; 12:1149-1459.
24. Hayashi JK, Ogawa M, Tagawa K, et al. Selective deficiency of α-dystroglycan in Fukuyama-type congenital muscular dystrophy. Neurology 2001; 57:115-121.
25. Yamamoto T, Kato Y, Karita M, et al. Fukutin expression in glial cells and neurons: implication in the brain lesions of Fukuyama congenital muscular dystrophy. Acta Neuropathol (Berl) 2002; 104:217-224.
26. Saito Y, Kobayashi M, Itoh M, et al. Aberrant neuronal migration in the brainstem of fukuyama-type congenital muscular dystrophy. J Neuropathol Exp Neurol 2003; 62:497-508.
27. Takada K, Nakamura H, Suzumori K, et al. Cortical dysplasia in a 23-week fetus with Fukuyama congenital muscular dystrophy (FCMD). Acta Neuropathol 1987; 74:300-306.
28. Nakano I. Are breaches in the glia limitans the primary cause of the micropolygyria in Fukuyama-type congenital muscular dystrophy (FCMD)? Pathological study of the cerebral cortex of an FCMD fetus. Acta Neuropathol 1996; 91:313-321.
29. Saito Y, Mizuguchi M, Oka A, Takashima S. Fukutin protein is expressed in neurons of the normal developing human brain but is reduced in Fukuyama-type congenital muscular dystrophy brain. Ann Neurol 2000; 47:756-764.
30. Sasaki J, Ishikawa K, Kobayashi K, et al. Neuronal expression of the fukutin gene. Hum Mol Genet 2000; 9:3083-3090.
31. Silan F, Yoshioka M, Kobayashi K, et al. A new mutation of the fukutin gene in a non-Japanese patient. Ann Neurol 2003; 53:392-396. The first fukutin mutation from outside Japan in a WWS phenotype.
32. Beltran-Valero de Bernabé D, van Bokhoven H, van Beusekom E, et al. A homozygous nonsense mutation in the Fukutin gene causes a Walker-Warburg syndrome phenotype. J Med Genet 2003; 40:845-848.
33. Santavuori P, Somer H, Sainio K, et al. Muscle-eye-brain disease (MEB). Brain Dev 1989; 11:147-153.
34. Taniguchi K, Kobayashi K, Saito K, et al. Worldwide distribution and broader clinical spectrum of muscle-eye-brain disease. Hum Mol Genet 2003; 12:527-534.
35. Yoshida A, Kobayashi K, Manya H, et al. Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev Cell 2001; 1:717-724.
36. Kano H, Kobayashi K, Herrmann R, et al. Deficiency of α-dystroglycan in muscle-eye-brain disease. Biochem Biophys Res Commun 2002; 291:1283-1286.
37. Zhang W, Vajsar J, Cao P, et al. Enzymatic diagnostic test for muscle-eye-brain type congenital muscular dystrophy using commercially available reagents. Clin Biochem 2003; 36:339-344.
38. Haliloglu G, Cross C, Talim B, et al. Severe autistic features in a child with muscle-eye-brain disease. 56th Annual Meeting of the American Academy of Neurology, PO1138, San Francisco, May 2004.
39. Brockington M, Blake DJ, Prandini P, et al. Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin α2 deficiency and abnormal glycosylation of α-dystroglycan. Am J Hum Genet 2001; 69:1198-1209. FKRP mutations were initially discovered in a group of cases with severe CMD without brain involvement.
40. Brockington M, Yuva Y, Prandini P, et al. Mutations in the fukutin-related protein gene (FKRP) identify limb-girdle muscular dystrophy 21 as a milder allelic variant of congenital muscular dystrophy MDC1C. Hum Mol Genet 2001; 10:2851-2859.
41. Topaloglu H, Brockington M, Yuva Y, et al. FKRP gene mutations cause congenital muscular dystrophy, mental retardation and cerebellar cysts. Neurology 2003; 60:988-992. FKRP mutations are also seen in CMD plus brain involvement.
42. Beltran Valero de Bernabé D, Voit T, Longman C, et al. Mutations in the FKRP gene can cause muscle-eye-brain disease and Walker-Warburg syndrome. J Med Genet 2003; 40:845-848.
43. Poppe M, Cree L, Bourke J, et al. The phenotype of limb-girdle muscular dystrophy type 21. Neurology 2003; 60:1246-1251.
44. Mercuri E, Brockington M, Straub V, et al. Phenotypic spectrum associated with mutations in the Fukutin-related protein gene. Ann Neurol 2003; 53:537-542.
45. Harel T, Goldberg Y, Shalev SA, et al. Limb-girdle muscular dystrophy type 21: phenotypic variability within a large consanguineous Bedouin family associated with a novel FKRP mutation. Eur J Hum Genet 2004; 12:38-43.
46. Cormand B, Pihko H, Bayes M, et al. Clinical and genetic distinction between Walker-Warburg syndrome and muscle-eye-brain disease. Neurology 2001; 56:1059-1069.
47. Beltran-Valero de Bernabe O, Currier S, Steinbrecher A, et al. Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome. Am J Hum Genet 2002; 71:1033-1043.
48. Willer T, Valero Carmen M, Tanner W, et al. O-mannosyl glycans: from yeast to novel associations with human disease. Curr Opin Struct Biol 2003; 13:621-630.
49. Willer T, Amselgruber W, Deutzmann R, Straahl S. Characterization of POMT2, a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. Glycobiology 2002; 12:771-783.
50. Kim DS, Hayashi YK, Matsumoto H, et al. POMT1 mutation results in defective glycosylation and loss of laminin-binding activity in the α-DG. Neurology 2004; 62:1009-1011.
51. Nishino I, Noguchi S, Munayama K, et al. Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy. Neurology 2002; 59:1689-1693.
52. Kanagawa M, Saito F, Kunz S, et al. Molecular recognition by LARGE is essential for expression of functional dystroglycan. Cell 2004; 117:953-964. Posttranslational modification of α-dystroglycan is essentially provided by LARGE.
53. Barresi R, Michele DE, Kanagawa M, et al. LARGE can functionally bypass α-dystroglycan glycosylation defects in distinct congenital muscular dystrophies. Nat Med 2004; 10:696-703. Modulation of LARGE expression or activity is a therapeutic strategy for glycosyltransferase-deficient CMD syndromes.
54. Eisenberg I, Avidan N, Potikha T, et al. The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. Nat Genet 2001; 29:83-87.
55. Vasconcelos OM, Raju R, Dalakas MC. GNE mutations in an American family with quadriceps-sparing IBM and absence of mutations in S-IBM. Neurology 2002; 59:1776-1779.
56. Broccolini A, Pescabri M, Amico A, et al. An Italian family with autosomal recessive inclusion body myopathy and mutations in the GNE gene. Neurology 2002; 59:1808-1809.
57. Tomimitsu H, Ishikaawa K, Shimisu J, et al. Distal myopathy with rimmed vacuoles: novel mutations in the GNE gene. Neurology 2002; 59:451-454.