Alpha Galactosidase B Deficiency - Schindler disease
Discussion:
Schindler Disease is one of seven identified Glycoprotein storage diseases. These inherited diseases are part of a larger group of disorders called Lysosomal storage diseases. Lysosomes are membrane-bound compartments found in the cells of the body. These compartments contain enzymes, which are responsible for the breakdown of many different oligosaccharides (long sugar chains.) These sugar chains are continuously made and broken down in our bodies, and this process is necessary for the appropriate mental and physical development. Each enzyme in the lysosome is responsible for a certain step in the breakdown of the sugar chains.
When an enzyme is not working, it leads to the build up of the sugar chains in the lysosome. In Schindler Disease, the specific enzyme that is absent is called alpha-N-acetylgalactosaminidase (previously known as alpha-galactosidase B.) The build up of oligosaccharide sugars that is caused, is gradual and interferes with the correct function of the cell. ItThis build up is gradual and eventually leads to the clinical features of Schindler Disease. Features may progress in severity over time.
In Schindler Disease, the specific enzyme that is absent is called alpha-N- acetylgalactosaminidase (previously known as alpha-galactosidase B.) (1)
Synonums:
Genetic: Gene map locus 22q11 -
NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. Mutations in NAGA have been identified as the cause of Schindler disease types I and II (type II also known as Kanzaki disease).
Diagnosis:
Diagnosis of Schindler disease is based on the symptoms the individual has, as well as the age the symptoms began. A urine test, blood test, or skin sample (biopsy) may help confirm the diagnosis. In Schindler disease, the blood or skin sample will show decreased activity of alpha-NAGA.
Symptoms:
Teleangiectasia (widening of groups of blood vessels which causes skin redness), excess urinary sialylglycoaminoacids, warty discolorations on skin, mildly coarse facial features, mild intellectual impairment, edema/lymphedema, loss of previously acquired physical skills, loss of previously acquired mental abilities, progressive neurological symptoms (seizures)
Treatment:
Supportive - no treatment for underlying disorder, multidisciplinary approach (Peadiatrics, Neurology, Ophthalmology, Orthopedics), Genetic counselling (normal sib of an affected patient has a 67% risk of being a carrier).
The lymphedema treatment program would include: Manual lymphatic drainage; compression wraps or compression bandages (using short stretch bandages), compression garments, compression sleeves.
June 11, 2008
--------------------------------
| N-ACETYL-ALPHA-D-GALACTOSAMINIDASE; NAGA |
Alternative titles; symbols
ALPHA-GALACTOSIDASE B; GALBGene map locus 22q11Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) is a lysosomal glycohydrolase that cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates.
Wang et al. (1990) isolated a full-length 2.2-kb NAGA cDNA and a genomic cosmid clone containing the entire NAGA gene from a human fibroblast cDNA library. The cDNA encodes a 411-amino acid protein with a 17-residue signal peptide and 6 putative N-glycosylation sites. Northern blot analysis detected 2 mRNA transcripts of 3.6 and 2.2 kb. Sequence analysis revealed striking similarities between the NAGA gene and exons 1-6 of the alpha-galactosidase A gene (GLA; 300644), suggesting that the 2 genes evolved by duplication and divergence from a common ancestral locus. Wang and Desnick (1991) also pointed to remarkable amino acid identity between the NAGA and GLA genes.
Wang et al. (1998) isolated the mouse Naga cDNA from a fibroblast cDNA library and found that the deduced human and mouse proteins share 81.9% sequence identity.
Wang and Desnick (1991) determined that the NAGA gene contains 9 exons.
De Groot et al. (1978) assigned the human N-acetyl-alpha-D-galactosaminidase gene to chromosome 22 by human-rodent somatic cell hybridization. The authors suggested that 'alpha-NAGA' was a more appropriate designation for this enzyme than alpha-galactosidase B.
In human-rodent cell hybrids, Geurts van Kessel et al. (1979, 1980) studied chronic myeloid leukemia cells to determine the site of the break on 22q relative to markers assigned to chromosomes 22 and 9. Alpha-NAGA remained with the Ph-1 chromosome, whereas the aconitase gene (ACO2; 100850) went with chromosome 9. Alpha-NAGA was located to band 22q11 and ACO2 was located between it and 22qter.
In the first described cases of type I Schindler disease (609241) (11,12:van Diggelen et al., 1987, 1988), Wang et al. (1990) identified a homozygous mutation in the NAGA gene (104170.0001).
In a Japanese woman with Kanzaki disease (609242) reported by Kanzaki et al. (1989), Wang et al. (1990, 1994) identified a homozygous mutation in the NAGA gene (104170.0002).
Wang et al. (1994) generated a mouse model of Schindler disease by targeted disruption of the Naga gene. Naga-null mice appeared clinically normal, survived into adulthood, and were fertile. Consistent with the human disease, the mice had no Naga activity and showed lysosomal pathology, including vacuolated peripheral lymphocytes.
Desnick and Schindler (2001) reported that Naga-null mice developed widespread lysosomal storage of abnormal material in the central nervous system and other organs, as well as focal axonal swellings or spheroids in the brain and spinal cord.
In the 2 German boys first described with Schindler disease (609241) (11,12:van Diggelen et al., 1987, 1988), Wang et al. (1990) identified a homozygous 973G-A transition in exon 8 of the NAGA gene, resulting in a glu325-to-lys (E325K) substitution. Keulemans et al. (1996) identified a distant affected relative of the 2 boys who had the E325K homozygous mutation. The boys had approximately 1% residual NAGA activity.
Bakker et al. (2001) reported homozygosity for the E325K mutation in a 3-year-old Moroccan boy with alpha-NAGA deficiency. He was born of consanguineous parents. The proband and his 7-year-old healthy brother had undetectable alpha-NAGA activity in leukocytes and a profound deficiency in fibroblasts. The parents had alpha-NAGA activity consistent with heterozygosity. Mutation analysis revealed homozygosity for the E325K mutation in the proband and his healthy brother, whereas a third sib and both parents were heterozygous. The family demonstrated the extreme clinical heterogeneity of alpha-NAGA deficiency, as the homozygous brother at the age of 7 years showed no clinical or neurologic symptoms.
In a Japanese woman with disseminated angiokeratoma (609242) reported by Kanzaki et al. (1989), Wang et al. (1990, 1994) identified a homozygous 985C-T transition in the NAGA gene, resulting in an arg329-to-trp (R329W) substitution. The base substitution was confirmed by hybridization of PCR-amplified genomic DNA from family members with allele-specific oligonucleotides. Wang et al. (1994) showed that in transiently expressed COS-1 cells, both the infantile-onset E325K (104170.0001) and the adult-onset R329W precursors were processed to the mature form; however, the E325K mutant polypeptide was more rapidly degraded than the R329W subunit, thereby providing a basis for the distinctly different infantile- and adult-onset phenotypes.
Keulemans et al. (1996) showed by PCR and sequence analysis that the Spanish brother and sister with manifestations of Kanzaki disease (609242) described by Chabas et al. (1994) were homozygous for a 5371G-T transversion in exon 5 of the NAGA gene (numbering according to Yamauchi et al., 1990), resulting in a glu193-to-ter (E193X) substitution, premature truncation, and complete loss of the NAGA protein.
In a Dutch girl with type III NAGA deficiency (609241) reported by de Jong et al. (1994), Keulemans et al. (1996) identified compound heterozygosity for 2 mutations in the NAGA gene: E325K (104170.0001) and a 4969C-G transversion in exon 4 (numbering according to Yamauchi et al., 1990), resulting in a ser160-to-cys (S160C) substitution. The same genotype was found in the clinically unaffected 3-year-old brother of the proband, and the authors suggested that the brother might be a preclinical case of NAGA deficiency; the brother's twin sister did not have the genotype. Residual enzyme activity in the proband was approximately 4% of controls. The S160C allele was not identified in 80 Dutch control alleles.
In a Japanese woman with Kanzaki disease (609242), Kodama et al. (2001) identified a homozygous 986G-A transition in the NAGA gene, resulting in an arg329-to-gln (R329Q) substitution. The patient had angiokeratoma corporis diffusum, Meniere syndrome, and no mental retardation. Her parents were consanguineous.
PubMed ID : 2243144
Cassandra L.
Kniffin - updated : 5/11/2005
Cassandra L. Kniffin - updated : 4/6/2005
Cassandra L. Kniffin - reorganized : 4/1/2005
Cassandra L. Kniffin - updated : 3/8/2005
Michael B. Petersen - updated : 8/21/2001
Iosif W. Lurie - updated : 7/10/1996
Victor A. McKusick : 6/4/1986
carol : 3/28/2007
...............................
Blood group B glycosphingolipids in
alpha-galactosidase
deficiency (Fabry disease): influence of secretor status.
Ledvinova J, Poupetova H, Hanackova A, Pisacka M, Elleder M.
Institute of Inherited Metabolic Diseases, First Faculty of Medicine,
Charles
University, Prague, Czech Republic.
Defect in degradation of blood group B-immunoactive glycosphingolipids
in Fabry
disease (deficiency of lysosomal alpha-galactosidase EC 3.2.1.22) has
been
studied using highly sensitive and specific TLC-immunostaining analysis
of
urinary sediments and tonsillar tissues of blood group B patients and
healthy
controls, secretors and nonsecretors. The B glycolipid antigens with
hexasaccharide chains were consistently found increased (25- to
100-fold) in the
urinary sediments of three Fabry patients, blood group B or AB
secretors.
Conversely, they were absent in the urinary sediment of one blood group
B
nonsecretor patient. In normal secretors, B glycosphingolipids were
present only
in traces. Moreover, significant increase in B glycolipid antigens
(8-fold) was
found in the tonsillar tissue of a Fabry patient blood group B
secretor. We
conclude that the secretor status is responsible for increased
concentration of
blood group B glycosphingolipids in both urinary cells and tonsils in
alpha-galactosidase
deficiency. The quantity of stored B-immunoactive glycosphingolipids,
however,
is much lower than that of the mainly accumulated glycosphingolipid
Gb(3)Cer.
The results clearly indicate that active or silent Se gene, which
controls
synthesis of B-antigen precursors, is responsible for notable
difference in B-glycosphingolipids
expression in Fabry patients - secretors and nonsecretors. Whether this
novel
aspect may be of prognostic significance, remains to be established.
PMID: 9106497 [PubMed
- indexed for
MEDLINE]
...............................
Defects in degradation of blood group A
and B glycosphingolipids in Schindler and Fabry diseases.
Asfaw B, Ledvinova J, Dobrovolny R, Bakker HD, Desnick RJ, van
Diggelen OP,
de Jong JG, Kanzaki T, Chabas A, Maire I, Conzelmann E, Schindler D.
Institute of Inherited Metabolic Disorders, First Faculty of Medicine,
Charles
University, 128 08 Prague, Czech Republic. basfaw@beba.cesnet.cz
Skin fibroblast cultures from patients with inherited lysosomal
enzymopathies,
alpha-N-acetylgalactosaminidase (alpha-NAGA) and alpha-galactosidase A
deficiencies (Schindler and Fabry disease, respectively), and from
normal
controls were used to study in situ degradation of blood group A and B
glycosphingolipids. Glycosphingolipids A-6-2 (GalNAc (alpha
1-->3)[Fuc alpha
1-->2]Gal(beta1-->4)GlcNAc(beta 1-->3)Gal(beta
1--> 4)Glc (beta
1-->1')Cer,
IV(2)-alpha-fucosyl-IV(3)-alpha-N-acetylgalactosaminylneolactotetraosylceramide),
B-6-2 (Gal(alpha 1-->3)[Fuc alpha 1--> 2] Gal (beta
1-->4)GlcNAc(beta
1-->3)Gal(beta 1-->4)Glc(beta 1-->1')Cer, IV(2)-
alpha-fucosyl-IV(3)-alpha-galactosylneolactotetraosylceramide), and
globoside (GalNAc(beta
1-->3)Gal(alpha 1-->4)Gal(beta 1-->4)Glc(beta
1-->1') Cer,
globotetraosylceramide) were tritium labeled in their ceramide moiety
and used
as natural substrates. The degradation rate of glycolipid A-6-2 was
very low in
fibroblasts of all the alpha-NAGA-deficient patients (less than 7% of
controls),
despite very heterogeneous clinical pictures, ruling out different
residual
enzyme activities as an explanation for the clinical heterogeneity.
Strongly
elevated urinary excretion of blood group A glycolipids was detected in
one
patient with blood group A, secretor status (five times higher than
upper limit
of controls), in support of the notion that blood group A-active
glycolipids may
contribute as storage compounds in blood group A patients. When
glycolipid B-6-2
was fed to alpha-galactosidase A-deficient cells, the degradation rate
was
surprisingly high (50% of controls), while that of
globotriaosylceramide was
reduced to less than 15% of control average, presumably reflecting
differences
in the lysosomal enzymology of polar glycolipids versus less-polar
ones.
Relatively high-degree degradation of substrates with
alpha-D-Galactosyl
moieties hints at a possible contribution of other enzymes.
PMID: 12091494 [PubMed
- indexed for
MEDLINE]
...............................
Schindler disease: the molecular lesion in
the alpha-N-acetylgalactosaminidase gene that causes an infantile
neuroaxonal
dystrophy.
Wang AM, Schindler D, Desnick R.
Division of Medical and Molecular Genetics, Mount Sinai School of
Medicine, New
York 10029.
Schindler disease is a recently recognized infantile neuroaxonal
dystrophy
resulting from the deficient activity of the lysosomal hydrolase,
alpha-N-acetylgalctosaminidase
(alpha-GalNAc). The recent isolation and expression of the full-length
cDNA
encoding alpha-GalNAc facilitated the identification of the molecular
lesions in
the affected brothers from family D, the first cases described with
this
autosomal recessive disease. Southern and Northern hybridization
analyses of DNA
and RNA from the affected homozygotes revealed a grossly normal
alpha-GalNAc
gene structure and normal transcript sizes and amounts. Therefore, the
alpha-GalNAc
transcript from an affected homozygote was reverse-transcribed,
amplified by the
polymerase chain reaction (PCR), and sequenced. A single G to A
transition at
nucleotide 973 was detected in multiple subclones containing the PCR
products.
This point mutation resulted in a glutamic acid to lysine substitution
in
residue 325 (E325K) of the alpha-GalNAc polypeptide. The base
substitution was
confirmed by dot blot hybridization analyses of PCR-amplified genomic
DNA from
family members with allele-specific oligonucleotides. Furthermore,
transient
expression of an alpha-GalNAc construct containing the E325K mutation
resulted
in the expression of an immunoreactive polypeptide which had no
detectable
alpha-GalNAc activity.
PMID: 2243144 [PubMed
- indexed for
MEDLINE]
...............................
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, 01003, USA.
alpha-N-acetylgalactosaminidase (alpha-NAGAL; E.C. 3.2.1.49) is a lysosomal exoglycosidase that cleaves terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. In humans, a deficiency of alpha-NAGAL activity results in the lysosomal storage disorders Schindler disease and Kanzaki disease. To better understand the molecular defects in the diseases, we determined the crystal structure of human alpha-NAGAL after expressing wild-type and glycosylation-deficient glycoproteins in recombinant insect cell expression systems. We measured the enzymatic parameters of our purified wild-type and mutant enzymes, establishing their enzymatic equivalence. To investigate the binding specificity and catalytic mechanism of the human alpha-NAGAL enzyme, we determined three crystallographic complexes with different catalytic products bound in the active site of the enzyme. To better understand how individual defects in the alpha-NAGAL glycoprotein lead to Schindler disease, we analyzed the effect of disease-causing mutations on the three-dimensional structure.
PubMed
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2771859/?tool=pubmed
...............................
...............................
Schindler Disease |
Disorder Subdivisions
General Discussion
Schindler Disease is a rare inherited metabolic disorder characterized
by a
deficiency of the lysosomal enzyme alpha-N-acetylgalactosaminidase
(alpha-NAGA).
The disorder belongs to a group of diseases known as lysosomal storage
disorders. Lysosomes function as the primary digestive units within
cells.
Enzymes within lysosomes break down or digest particular nutrients,
such as
certain fats and carbohydrates. In individuals with Schindler Disease,
deficiency of the alpha-NAGA enzyme leads to an abnormal accumulation
of certain
complex compounds (glycosphingolipids) in many tissues of the body.
There are two forms of Schindler Disease. The classical form of the
disorder,
known as Schindler Disease, Type I, has an infantile onset. Affected
individuals
appear to develop normally until approximately 1 year of age, when they
begin to
lose previously acquired skills that require the coordination of
physical and
mental activities (developmental regression). Additional neurological
and
neuromuscular symptoms may become apparent, including diminished muscle
tone (hypotonia)
and weakness; involuntary, rapid eye movements (nystagmus); visual
impairment;
and episodes of uncontrolled electrical activity in the brain
(seizures). With
continuing disease progression, affected children typically develop
restricted
movements of certain muscles due to progressively increased muscle
rigidity,
severe mental retardation, hearing and visual impairment, and a lack of
response
to stimuli in the environment.
Schindler Disease, Type II, which is also known as Kanzaki Disease, is
the
adult-onset form of the disorder. Associated symptoms may not become
apparent
until the second or third decade of life. In this milder form of the
disease,
symptoms may include the development of clusters of wart-like
discolorations on
the skin (angiokeratomas); permanent widening of groups of blood
vessels (telangiectasia),
causing redness of the skin in affected areas; relative coarsening of
facial
features; and mild intellectual impairment. The progressive
neurological
degeneration characteristically seen in the infantile form of the
disease has
not occurred in association with Schindler Disease, Type II.
Both forms of Schindler Disease are inherited as autosomal recessive
traits.
According to investigators, different changes (mutations) of the same
gene are
responsible for the infantile- and adult-onset forms of the disease.
The gene
has been mapped to the long arm (q) of chromosome 22 (22q11).
Organizations related to
Schindler Disease
5223 Brookfield LaneCLIMB (Children Living with Inherited Metabolic Diseases)
Sylvania OH 43560-1809
Phone #: 419-885-1497
800 #: --
e-mail: VOLK4OLKS@aol.comHome page: N/A
Climb Building
Crewe Intl CW2 6BG
Phone #: 44 -870- 7700 325
800 #: --
e-mail: info@climb.org.uk
International Society for Mannosidosis & Related Diseases, Inc. - ISMRD (1)
3210 Batavia Ave, Baltimore, MD, 21214
Baltimore MD 21214
Phone #: 410-254-4903
800 #: N/A
e-mail: pres@mannosidosis.org
NIH/NINDS Brain Resources and Information Network
PO Box 5801
Bethesda MD 20824
Phone #: 301-496-5751
800 #: 800-352-9424
e-mail: N/A
National Lipid Diseases Foundation
1201 Corbin StreetNational Tay-Sachs and Allied Diseases Association, Inc.
Elizabeth NJ 07201
Phone #: 908-527-8000
800 #: 800-527-8005
e-mail: N/A
Home page: N/A
2001 Beacon StreetVaincre Les Maladies Lysosomales
Boston MA 02135
Phone #: 617-277-4463
800 #: 800-906-8723
e-mail: info@ntsad.org
9 Place du 19 Mars 1962,
Evry Cedex None 91035
Phone #: 016-091-7500
800 #: --
e-mail: accueil@vml-asso.org
===========================
External Links:
...........................
Schindler disease - Webmd
Schindler disease - Pedbase.org
Schindler Disease
http://ghr.nlm.nih.gov/condition/schindler-disease
Schindler Disease - Developmental Disorders of the Lymphatics
http://lymphsystemdisorders.blogspot.com/2005/12/alpha-galactosidase-b-deficiency.html
===========================
Classification and Codes:
...........................
ICD 10 code - E74.2
OMIM
N-ACETYL-ALPHA-D-GALACTOSAMINIDASE; NAGA 104170
SCHINDLER DISEASE, TYPE I 609241
KANZAKI DISEASE 609242
MGI- NAGA
HomoloGene - NAGA N-acetylgalactosaminidase, alpha
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