Mucolipidosis II and III alpha/beta in brazil: Analysis of the GNPTAB gene

Gene

Volumn 524, Issue 1, 2013, Pages 59-64

  Cury, G K ^a   Matte, U ^a,b   Artigalas O ^a   Alegra, T ^a   Velho, R V ^a   Sperb, F ^a,b   Burin, M G ^b   Ribeiro, E M ^c   Lourenco C M ^d   Kim, C A ^d   Valadares, E R ^e   Galera, M F ^f   Acosta, A X ^g   Schwartz, I V D ^a,b  

^a FEDERAL UNIVERSITY OF RIO GRANDE DO SUL   (Brazil)

^b HOSPITAL DE CLÍNICAS DE PORTO ALEGRE   (Brazil)

^c Association of Genetic Diseases of the State of Ceará   (Brazil)

^d UNIVERSITY OF SÃO PAULO   (Brazil)

^e FEDERAL UNIVERSITY OF MINAS GERAIS   (Brazil)

^f School of Medicine   (Brazil)

^g FEDERAL UNIVERSITY OF BAHIA   (Brazil)

Author keywords

GNPTAB; I cell disease; Lysosomal disease; M6P; Mucolipidosis; Pseudo Hurler polydystrophy

Indexed keywords

COMPLEMENTARY DNA; N ACETYLGLUCOSAMINE 1 PHOSPHATE TRANSFERASE ALPHA BETA SUBUNIT; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; BRAZIL; CLINICAL ARTICLE; DNA DETERMINATION; EXON; GENE MUTATION; GENE SEQUENCE; GENETIC VARIABILITY; HETEROZYGOTE; HUMAN; MUCOLIPIDOSIS TYPE 2; MUCOLIPIDOSIS TYPE 3; PRIORITY JOURNAL; RNA SPLICING;

ALLELES; BASE SEQUENCE; BIOLOGICAL MARKERS; BRAZIL; DNA, COMPLEMENTARY; EXONS; GENETIC HETEROGENEITY; GENOTYPE; HUMANS; LEUKOCYTES, MONONUCLEAR; MANNOSEPHOSPHATES; MOLECULAR SEQUENCE DATA; MUCOLIPIDOSES; MUTATION, MISSENSE; PHENOTYPE; RNA SPLICE SITES; RNA SPLICING; TRANSFERASES (OTHER SUBSTITUTED PHOSPHATE GROUPS);

EID: 84878106755     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2013.03.105     Document Type: Article

References (26)

1. Bao M., Elmendorf B.J., Booth J.L., Drake R.R., Canfield W.M. Bovine UDP-N-acetylglucosamine: lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II Enzymatic characterization and identification of the catalytic subunit. J. Biol. Chem. 1996, 271:31446-31451.
2. Bargal R., et al. When mucolipidosis III meets mucolipidosis II: GNPTA gene mutations in 24 patients. Mol. Genet. Metab. 2006, 88:359-363.
3. Braulke T., Pohl S., Storch S. Molecular analysis of the GlcNac-1-phosphotransferase. J. Inherit. Metab. Dis. 2008, 31:253-257.
4. Brooks D., Turner C., Muller V., Hopwood J., Meikle P. I-cell disease. Lysosomal Storage Disease 2007, 529-535. Springer. J.A. Barranger, M.A. Cabrera-Salazar (Eds.).
5. Cathey S.S., et al. Molecular order in mucolipidosis II and III nomenclature. Am. J. Med. Genet. 2008, 146(A):512-513.
6. Cathey S.S., Leroy J.G., Wood T. Phenotype and genotype in mucolipidosis II and III alpha/beta: a study of 61 probands. J. Med. Genet. 2010, 4:38-48.
7. Chamoles N.A., Blanco M.B., Gaggioli D., Casentini C. Hurler-like phenotype: enzymatic diagnosis in dried blood spots on filter paper. Clin. Chem. 2001, 47:2098-2102.
8. Encarnação M., et al. Molecular analysis of the GNPTAB and GNPTG gene in 13 patients with mucolipidosis type II or type III - identification of eight novel mutations. Clin. Genet. 2009, 76:76-84.
9. (Last access: 22/03/2012). http://genetics.bwh.harvard.edu/pph2/.
10. (Last access: 22/03/2012). http://http://genes.mit.edu/burgelab/maxent/Xmaxentscan_scoreseq.html.
11. (Last access: 22/02/2012). http://sift.jcvi.org/www.SIFT_seq_submit2.html.
12. (Last access: 01/10/2011). http://www.geneclinics.org.
13. (Last access: 01/06/2011). http://www.kasuza.or.jp/codon/cgi-bin/showcodon.cgi?species=9606.
14. Komar A.A. SNPs, silent but not invisible. Science 2007, 315:466-467.
15. Kornfeld S., Sly W.S. I-cell disease and pseudo-hurler polydystrophy: disorders of lysosomal enzyme phosphorylation and localization. The Metabolic and Molecular Bases of Inherited Disease 2001, 3469-3482. McGraw-Hill, New York. C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
16. Kudo M., et al. The alpha- and beta-subunits of the human UDP-N-acetylglucosamine: lysosomal enzyme N-acetylglucosamine-1-phosphotransferase [corrected] are encoded by a single cDNA. J. Biol. Chem. 2005, 280:36141-36149.
17. Kudo M., Brem M.S., Canfield W.M. Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations the GlcNac-phosphotransferase α/β-subunits precursor gene. Am. J. Hum. Genet. 2006, 78:451-463.
18. Paik K.H., et al. Identification of mutations in the GNPTA (MGC4170) gene coding for GlcNac-phosphotransferase alpha/beta subunits in Korean patients with mucolipidosis type II or type IIIA. Hum. Mutat. 2005, 26:308-314.
19. Persichetti E., et al. Identification and molecular characterization of six novel mutations in the UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTG) gene in patients with mucolipidosis III gamma. Hum. Mutat. 2009, 30:978-984.
20. Plante M., et al. Mucolipidosis II: a single causal mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTAB) in a French Canadian founder population. Clin. Genet. 2008, 73:236-244.
21. Sauna Z.E., Kimchi-Sarfaty C. Understanding the contribution of synonymous mutations to human disease. Nat. Rev. Genet. 2011, 12:683-691.
22. Tappino B., et al. Molecular characterization of 22 novel UDP-N-acetylglucosamine-1-phosphate transferase α- and β-subunits (GNPTAB) gene mutations causing mucolipidosis types IIα/β and IIIα/β in 46 patients. Hum. Mutat. 2009, 30:E956-E973.
23. Tiede S., et al. Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNac-1-phosphotransferase. Nat. Med. 2005, 11:1109-1112.
24. Tomatsu S., et al. Keratan sulphate levels in mucopolysaccharidoses and mucolipidoses. J. Inherit. Metab. Dis. 2005, 28:187-202.
25. Tomatsu S., et al. Mol. Genet. Metab. 2010, 99:124-131.
26. Zarghooni M., Dittakavi S.S.R. Molecular analysis of cell lines from patients with mucolipidosis II and mucolipidosis III. Am. J. Med. Genet. 2009, 149A:2753-2761.