Sanfilippo Disease, Type A with some Features of Ceroid Lipofuscinosis

Wisniewski, K. E.; Rudelli, R. D.; Laure‐Kamionowska, Milena; Sklower, Susan L.; Houck, GeorgeE.; Kieras, Fred J.; Ramos, Pilar; Wı́sniewski, Henryk M.; Braak, Heiko

doi:10.1055/s-2008-1052551

Cited by 32 publications

(21 citation statements)

References 5 publications

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“…Wisniewski et al [1985] had described three brothers affected by the disease, all aged more than 30, showing histological alterations like patients affected by ceroid lipofuscinosis. Unfortunately, clinical information on the functional abilities of these patients have not been reported.…”

Section: Discussionmentioning

confidence: 98%

“…However, among the hundreds of patients affected by mucopolysaccharidosis III, only few cases of adults have been reported with clinical signs of Sanfilippo type A syndrome moderately involved from the neurological and physical point of view: three brothers reported by Wisniewski et al [1985], two sibs described by Lindor et al [1994], two more by Date et al [1998], and another one recently reported by Miyazaki et al [2002]. Di Natale et al [2003] described two second cousins, one affected by the classical severe form of the disease and the other affected by a mild form of the illness; in the same year, Van Hove et al [2003] reported an additional adult patient whose main clinical feature was the presence of severe cardiomyopathy in the absence of any neurological involvement.…”

Section: Introductionmentioning

confidence: 98%

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An adult Sanfilippo type A patient with homozygous mutation R206P in the sulfamidase gene

et al. 2005

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The Sanfilippo type A syndrome, one of the most frequent forms of mucopolysaccharidosis III, is characterized by severe mental retardation, progressive neurological degeneration, and mild somatic changes. It is due to a deficiency of heparan-N-sulfatase (sulfamidase) activity and consequent excretion of heparan sulfate in the urine. The disease is transmitted through an autosomal recessive mechanism, and more than 60 gene mutations have been identified. Up to now, only 10 cases of attenuated form of Sanfilippo type A syndrome have been described, and the specific mutation has been identified only in two of them. We report here on a female patient, 20 years old, with Sanfilippo type A syndrome presenting with a mild clinical phenotype characterized essentially by a moderate nonevolving mental retardation. The genetic analysis demonstrated that the patient is homozygous for mutation R206P; presence of polymorphism R456H was also found. This study places R206P as a mild mutation underlying Sanfilippo type A disease.

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Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 98%

An adult Sanfilippo type A patient with homozygous mutation R206P in the sulfamidase gene

et al. 2005

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“…The accumulation of autofluorescent material, which was observed in Arsg-deficient dogs (10) as well as Arsg-deficient mice ( Fig. 1 E′ and F′), likely results from secondary storage, which is observed in several LSDs (14) and in MPSs in particular (15,16). Glucosamine residues bearing 3-O-sulfate groups are relatively rare in heparan sulfate and are generated by members of the 3-O-sulfotransferase family of enzymes (17).…”

Section: Discussionmentioning

confidence: 99%

Arylsulfatase G inactivation causes loss of heparan sulfate 3- O -sulfatase activity and mucopolysaccharidosis in mice

Kowalewski

Lamanna

Lawrence

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Deficiency of glycosaminoglycan (GAG) degradation causes a subclass of lysosomal storage disorders called mucopolysaccharidoses (MPSs), many of which present with severe neuropathology. Critical steps in the degradation of the GAG heparan sulfate remain enigmatic. Here we show that the lysosomal arylsulfatase G (ARSG) is the long-sought glucosamine-3- O -sulfatase required to complete the degradation of heparan sulfate. Arsg -deficient mice accumulate heparan sulfate in visceral organs and the central nervous system and develop neuronal cell death and behavioral deficits. This accumulated heparan sulfate exhibits unique nonreducing end structures with terminal N -sulfoglucosamine-3- O -sulfate residues, allowing diagnosis of the disorder. Recombinant human ARSG is able to cleave 3- O -sulfate groups from these residues as well as from an authentic 3- O -sulfated N -sulfoglucosamine standard. Our results demonstrate the key role of ARSG in heparan sulfate degradation and strongly suggest that ARSG deficiency represents a unique, as yet unknown form of MPS, which we term MPS IIIE.

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“…The mutations identified (E355K and S298P) are both previously described pathogenic alleles (19,20), one of which is associated with attenuated disease (20,32), which is consistent with our find- ings. It is interesting to note that although autofluorescent inclusions are not generally regarded as a defining feature of MPSIIIA they have been observed in some patients (34), which may explain possible confusion with NCLs.…”

Section: Discussionmentioning

confidence: 99%

Mass Spectrometry-based Protein Profiling to Determine the Cause of Lysosomal Storage Diseases of Unknown Etiology

Sleat¹,

Ding

Wang

et al. 2009

Molecular & Cellular Proteomics

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Diagnosis of lysosomal storage diseases (LSDs) can be problematic in atypical cases where clinical phenotype may overlap with other genetically distinct disorders. In addition, LSDs may result from mutations in genes not yet implicated in disease. Thus, there are individuals that are diagnosed with apparent LSD based upon clinical criteria where the gene defect remains elusive. The objective of this study was to determine whether comparative proteomics approaches could provide useful insights into such cases. Most LSDs arise from mutations in genes encoding lysosomal proteins that contain mannose 6-phosphate, a carbohydrate modification that acts as a signal for intracellular targeting to the lysosome. We purified mannose 6-phosphorylated proteins by affinity chromatography and estimated relative abundance of individual proteins in the mixture by spectral counting of peptides detected by tandem mass spectrometry. Our rationale was that proteins that are decreased or absent in patients compared with controls could represent candidates for the primary defect, directing biochemical or genetics studies. On a survey of brain autopsy specimens from 23 patients with either confirmed or possible lysosomal disease, this approach identified or validated the genetic basis for disease in eight cases. These results indicate that this protein expression approach is useful for identifying defects in cases of undiagnosed lysosomal disease, and we demonstrated that it can be used with more accessible patient samples, e.g. cultured cells. Furthermore this approach was instrumental in the identification or validation of mutations in two lysosomal proteins, CLN5 and sulfamidase, in the adult form of neuronal ceroid lipofuscinosis.

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Sanfilippo Disease, Type A with some Features of Ceroid Lipofuscinosis

Cited by 32 publications

References 5 publications

An adult Sanfilippo type A patient with homozygous mutation R206P in the sulfamidase gene

An adult Sanfilippo type A patient with homozygous mutation R206P in the sulfamidase gene

Arylsulfatase G inactivation causes loss of heparan sulfate 3- O -sulfatase activity and mucopolysaccharidosis in mice

Mass Spectrometry-based Protein Profiling to Determine the Cause of Lysosomal Storage Diseases of Unknown Etiology

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