Identification of two novel arylsulfatase A mutations with a polymorphism as a cause of metachromatic leukodystrophy

REFERENCES

• von Figura K, Gieselmann V, Jaeken J. Metachromatic leukody-strophy. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic and Molecular Bases of Inherited Disease, New York: McGraw-Hill, 2001: pp. 3695–3724
   Google Scholar
• Sommerlade HJ, Selmer T, Ingendoh A, et al. Glycosylation and phosphorylation of arylsulfataseBiol Chem 1994; 33: 20977–20981
   Google Scholar
• Gieselmann V, Matzner U, Hess B, et al. Metachromatic leukodystrophy: Molecular genetics and animal model. I Inherit Metab Dis 1998; 21: 564–574
   PubMed Web of Science ®Google Scholar
• Polten A, Fluharty AL, Fluharty CB, et al. Molecular basis of different forms of metachromatic leukodystrophy. N Eng J Med 1991; 324: 18–22
   PubMed Web of Science ®Google Scholar
• Berna L, Gieselmann V, Poupetova H, et al. Novel mutations associated with metachromatic leukodystrophy: Phenotype and expression studies in nine Czech and Slovak patients. Am] Med Genet 2004; 129A: 277–281
   PubMed Web of Science ®Google Scholar
• Eng B, Heshka T, Tarnopolsky MA, et al. Infantile Metachromatic leukodystrophy (MLD) in a compound heterozygote for the c.459 + 1G > A mutation and a complete deletion of the arylsulfatase A gene. Am Med Genet A 2004; 128A: 95–97
   Google Scholar
• Gieselmann V, Polten A, Kreysing J, et al. Arylsulfatase A pseudodeficiency: Loss of a polyadenylation signal and N-glycosylation site. Proc Natl Acad Sci USA 1989; 86: 9436–9440
   PubMed Web of Science ®Google Scholar
• Harvey JS, Carey WE, Morris CP. Importance of the glycosylation and polyadenylation variants in metachromatic leukodystrophy pseudodeficiency pseudodeficiency phenotype. Hum Mol Genet 1998; 7: 1215–1219
   PubMed Web of Science ®Google Scholar
• Lowry OH, Rosebrough NJ, Farr AL, et al. Protein measurement with folin phenol reagent. Biol Chem 1951; 193: 265-275
   Web of Science ®Google Scholar
• Suzuki K, Enzymatic diagnosis of sphingolipidoses. Methods Enzymol 1987; 138: 727–763
   PubMed Web of Science ®Google Scholar
• Miller SA, Dykes DD, Polesky HE. A simple salting out method for extracting DNA from nucleated cells. Nucleic Acids Res 1988; 16: 1215
   PubMed Web of Science ®Google Scholar
• Gort L, Josep Coll M, Chabas A. Identification of 12 novel mutations and two new polymorph isms in the arylsulfatase A gene: Haplotype and genotype-phenotype correlation studies in Spanish metachromatic leukodystrophy patients. Hum Mutat 1999; 14: 240–248
   PubMed Web of Science ®Google Scholar
• Barth ML, Ward C, Harris A, et al. Frequency of arylsulfatase A pseudodeficiency associated mutations in a healthy population. J Med Genet 1994; 31: 667–671
   PubMed Web of Science ®Google Scholar
• Bognar SK, Furac I, Kubat M, et al. Croatian population data for arylsulfatase a pseudodeficiency-associated mutations in healthy subjects, and in patients with Alzheimer-type dementia and Down syndrome. Arch Med Res 2002; 33: 473–477
   PubMed Web of Science ®Google Scholar
• Orita M, Suzuki Y, Sekiya T, et al. Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics 1989; 5: 874–879
   PubMed Web of Science ®Google Scholar
• Ozkara HA, Navon R. At least six different mutations in HEXA gene cause Tay-Sachs disease among the Turkish population. Mol Genet Metab 1998; 65: 250–253
   PubMed Web of Science ®Google Scholar
• Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74: 5463–5467
   PubMed Web of Science ®Google Scholar
• Ozkara HA, Topcu M. Sphingolipidosis in Turkey. Brain Dev 2004; 26: 363–366
   PubMed Web of Science ®Google Scholar
• Lukatela G, Krauss N, Theis K, et al. Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry 1998; 37: 3654–3664
   PubMed Web of Science ®Google Scholar
• Tsuda T, Hasegawa Y, [to Y. Two novel mutations in a Japanese patient with the late infantile form of metachromatic leukodystro-phy. Brain Dev 1996; 18: 400–403
   PubMed Web of Science ®Google Scholar
• Kreysing J, Bohne W, Bösenberg C, et al. High residual arylsulfatase A (ARSA) activity in a patient with late-infantile metachromatic leukodystrophy. Am] Hum Genet 1993; 53: 339–346
   PubMed Web of Science ®Google Scholar
• Draghia R, Letourneur F, Drugan C, et al. Metachromatic Leukodystrophy: Identification of the first deletion in exon I and of nine novel point mutations in the arylsulfatase A gene. Hum Mutat 1997; 9: 234–242
   PubMed Web of Science ®Google Scholar
• Anlar B, Waye JS, Eng B, et al. Atypical clinical course in juvenile metachromatic leukodystrophy involving novel arylsulfatase A gene mutations. Dev Med Child Neurol 2006; 48: 383–387.
   PubMed Web of Science ®Google Scholar
• Regis S, Corsolini F, Stroppiano M, et al. Contribution of arylsulfatase A mutations located on the same allele to enzyme activity reduction and leukodystrophy severity. Hum Genet 2002; 110: 351–355
   PubMed Web of Science ®Google Scholar
• Bertelli M, Gallo S, Buda A, et al. Novel mutations in the arylsulfatase A gene in eight Italian families with metachromatic leukodystrophy. J Clin Neurosci 2006; 13: 443–448
   PubMed Web of Science ®Google Scholar
• Coulter-Mackie MB, Gagnier L. Spectrum of mutations in the arylsulfatase A gene in a Canadian DNA collection including two novel frameshift mutations, a new missense mutation (C488R) and an MLD mutation (R84Q) in cis with a pseudodeficiency allele. Mol Genet Metab 2003; 79: 91–98
   PubMed Web of Science ®Google Scholar
• Ozkara HA, Sandhoff K. A new point mutation (G412 to A) at the last nucleotide of exon 3 of hexosaminidase alpha-subunit gene affects splicing. Brain Dev 2003; 25: 203–206
   PubMed Web of Science ®Google Scholar