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01-09-2014 | Original Communication

Arylsulphatase A activity in familial parkinsonism: a pathogenetic role?

Authors: Elena Antelmi, Giovanni Rizzo, Margherita Fabbri, Sabina Capellari, Cesa Scaglione, Paolo Martinelli

Published in: Journal of Neurology | Issue 9/2014

Abstract

Cellular mechanism leading to Parkinson Disease (PD) is still unknown, but impairment of lysosomal degradation of aberrant proteins seems to play a crucial role. The most known lysosomal disease associated with PD is Gaucher Disease. However, actually a number of different lysosomal disorders have been linked with PD. We report three families with Arylsulphatase A partial deficit in which we can find a high recurrence of parkinsonism among the siblings. The pedigree members show as well some atypical signs and symptoms among the PD spectrum features. Arylsulphatase A plays a crucial role in protein degradation. Even if a possibly casual association cannot be excluded, it can be speculated that Arylsulphatase A partial deficit can act as a cofactor for neurodegeneration in subjects with other genetic or environmental predispositions to PD or to other neurodegenerative disease.

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Goedert M, Spillantini MG, Del Tredici K, Braak H (2013) 100 years of lewy pathology. Nat Rev Neurol 9:13–24CrossRefPubMed

Trinh J, Farrer M (2013) Advances in the genetics of Parkinson disease. Nat Rev Neurol 9:445–454CrossRefPubMed

Aharon-Peretz J, Rosenbaum H, Gershoni-Baruch R (2004) Mutations in the glucocerebrosidase gene and Parkinson’s disease in Ashkenazi Jews. N Engl J Med 351:1972–1977CrossRefPubMed

Gan-Or Z, Giladi N, Rozovski U et al (2008) Genotype-phenotype correlations between GBA mutations and Parkinson disease risk and onset. Neurology 70:2277–2283CrossRefPubMed

Shachar T, Lo Bianco C, Recchia A (2011) Lysosomal storage disorder and Parkinson’s Disease: Gaucher Disease and beyond. Mov Disord 26:1593–1604CrossRefPubMed

Dehay B, Martinez-Vicente M, Caldwell GA et al (2013) Lysosomal impairment in Parkinson’s disease. Mov Disord 28:725–732CrossRefPubMed

Sharma N (2013) Lysosomal enzyme defects and Parkinson disease. Neurology 80:1544–1545CrossRefPubMed

Sangiorgi S, Ferini A, Zanetti A, Mochi M (1991) Reduced activity arylsulphatase A and predisposition to neurological disorders: analysis of 140 pediatric patients. Am J Med Genetic 40:365–369CrossRef

Martinelli P, Ippoliti M, Montanari M et al (1994) Arylsulphatase A (ASA) activity in parkinsonism and symptomatic essential tremor. Acta Neurol Scand 89:171–174CrossRefPubMed

10.

Gallassi R, Lenzi P, Stracciari A et al (1986) Neuropsychological assessment of mental deterioration: purpose of a brief battery and a probabilistic definition of “normality” and “non-normality”. Acta Psychiatr Scand 74:62–67CrossRefPubMed

11.

Lowry O, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with folin-phenol reagent. J Biol Chem 93:265–275

12.

Baum H, Dodgson KS, Spencer B (1959) The assay of arylsulphatase A and B in human urine. Clin Chim Acta 4:453–455CrossRefPubMed

13.

Sidransky E, Nalls MA, Aasly JO et al (2009) Multicenter analysis of glucocerebrosidase mutations in Parkinson’s disease. N Engl J Med 361:1651–1661PubMedCentralCrossRefPubMed

14.

Tayebi N, Callahan M, Madike V et al (2001) Gaucher disease and parkinsonism: a phenotypic and genotypic characterization. Mol Genet Metab 73:313–321CrossRefPubMed

15.

Tayebi N, Walker J, Stubblefield B et al (2003) Gaucher disease with parkinsonian manifestations: does glucocerebrosidase deficiency contribute to a vulnerability to parkinsonism? Mol Genet Metab 79:104–109CrossRefPubMed

16.

Goker-Alpan O, Lopez G, Vithayathil J et al (2008) The spectrum of parkinsonian manifestations associated with glucocerebrosidase mutations. Arch Neurol 65:1353–1357PubMedCentralCrossRefPubMed

17.

Neumann J, Bras J, Deas E et al (2009) Glucocerebrosidase mutations in clinical and pathologically proven Parkinson’s disease. Brain 132:1783–1794PubMedCentralCrossRefPubMed

18.

Setó-Salvia N, Pagonabarraga J, Houlden H et al (2011) Glucocerebrosidase mutations confer a greater risk of dementia during Parkinson’s disease course. Mov Disord 27:393–399CrossRefPubMed

19.

Ziegler SG, Eblan MJ, Gutti U et al (2007) Glucocerebrosidase mutations in Chinese subjects from Taiwan with sporadic Parkinson disease. Mol Genet Metab 91:195–200PubMedCentralCrossRefPubMed

20.

Marras C, Schuele B, Munhoz RP et al (2011) Phenotype in parkinsonian and nonparkinsonian LRRK2 G2019S mutation carriers. Neurology 77:325–333PubMedCentralCrossRefPubMed

21.

Gegg ME, Burke D, Heales SJ et al (2012) Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains. Ann Neurol 72:455–463PubMedCentralCrossRefPubMed

22.

Hara T, Nakamura K, Matsui M et al (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441:885–889CrossRefPubMed

23.

Komatsu M, Waguri S, Chiba T et al (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441:880–884CrossRefPubMed

24.

Zhu JH, Guo F, Shelburne J, Watkins S, Chu CT (2003) Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathol 13:473–481PubMedCentralCrossRefPubMed

25.

Alvarez-Erviti L, Rodriguez-Oroz MC, Cooper JM et al (2010) Chaperone- mediated autophagy markers in Parkinson disease brains. Arch Neurol 67:1464–1472CrossRefPubMed

26.

Vila M, Bove J, Dehay B et al (2011) Lysosomal membrane permeabilization in Parkinson disease. Autophagy 7:98–100CrossRefPubMed

27.

Sanchez-Danes A, Richaud-Patin Y, Carballo-Carbajal I et al (2012) Disease-specific phenotypes in dopamine neurons from human iPS based models of genetic and sporadic Parkinson’s disease. EMBO Mol Med 4:380–395PubMedCentralCrossRefPubMed

28.

Xilouri M, Brekk OR, Stefanis L (2013) Alpha-synuclein and protein degradation systems: a reciprocal relationship. Mol Neurobiol 47:537–551CrossRefPubMed

29.

Neudorfer O, Giladi N, Elstein D et al (1996) Occurrence of Parkinson’s syndrome in type I Gaucher disease. QJM 89:691–694CrossRefPubMed

30.

Varkonyi J, Rosenbaum H, Baumann N et al (2003) Gaucher disease associated with parkinsonism: four further case reports. Am J Med Genet 116:348–351CrossRef

31.

Bembi B, Zambito Marsala S, Sidransky E et al (2003) Gaucher’s disease with Parkinson’s disease: clinical and pathological aspects. Neurology 61:99–101CrossRefPubMed

32.

Halperin A, Elstein D, Zimran A (2003) Increased incidence of Parkinson disease among relatives of patients with Gaucher disease. Blood Cells Mol Dis 36:426–428CrossRef

33.

Nichols WC, Pankratz N, Marek DK, For the Parkinson Study Group-PROGENI Investigators (2009) Mutations in GBA are associated with familial Parkinson disease susceptibility and age at onset. Neurology 72:310–316PubMedCentralCrossRefPubMed

34.

Mitsui J, Mizuta I, Toyoda et al (2009) Mutations for Gaucher disease confer high susceptibility to Parkinson disease. Arch Neurol 66:571–576CrossRefPubMed

35.

Duran R, Mencacci NE, Angeli AV et al (2013) The glucocerobrosidase E326K variant predisposes to Parkinson’s disease, but does not cause Gaucher’s disease. Mov Disord 28:232–236PubMedCentralCrossRefPubMed

36.

Winder-Rhodes SE, Evans JR, Ban M et al (2013) Glucocerebrosidase mutations influence the natural history of Parkinson’ s disease in a community-based incident cohort. Brain 136:392–399CrossRefPubMed

37.

Dermentzaki G, Dimitriou E, Xilouri M et al (2013) Loss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells. PLoS One 8(4):60674. doi:10.1371/journal.pone.0060674

38.

Kappler J, Watts RWE, Conzelmann E et al (1991) Low arysulphatase A activity and choreoathetotic syndrome in three siblings: differentiation of pseudodeficiency from metachromatic leukodystrophy. Eur J Pediatric 150:287–290CrossRef

39.

Suzuki K, Iseki E, Togo T et al (2007) Neuronal and glial accumulation of alpha and beta synucleins in human lipidoses. Acta Neuropathol 114:481–489CrossRefPubMed

40.

Parnetti L, Chiasserini D, Persichetti E et al (2014) Cerebrospinal fluid lysosomal enzymes and α-synuclein in Parkinson’s disease. Mov Disord. doi:10.1002/mds.25772

41.

Murphy KE, Gysbers AM, Abbott SK et al (2014) Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson’s disease. Brain 137:834–848PubMedCentralCrossRefPubMed

42.

Nuytemans L, Bademci G, Inchausti G (2013) Whole exome sequencing of rare variants in EIF4G1 and VPS35 in Parkinson disease. Neurology 80:982–989

Title: Arylsulphatase A activity in familial parkinsonism: a pathogenetic role?
Authors: Elena Antelmi
Giovanni Rizzo
Margherita Fabbri
Sabina Capellari
Cesa Scaglione
Paolo Martinelli
Publication date: 01-09-2014
Publisher: Springer Berlin Heidelberg
Published in: Journal of Neurology / Issue 9/2014
Print ISSN: 0340-5354
Electronic ISSN: 1432-1459
DOI: https://doi.org/10.1007/s00415-014-7425-5

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Arylsulphatase A activity in familial parkinsonism: a pathogenetic role?

Abstract

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Abstract

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