NA03560
DNA from Fibroblast
Description:
ASPARTYLGLUCOSAMINURIA
ASPARTYLGLUCOSAMINIDASE; AGA
|
Repository
|
NIGMS Human Genetic Cell Repository
|
| Subcollection |
Heritable Diseases
Lysosomal Storage Diseases |
| Class |
Disorders of Carbohydrate Metabolism |
| Quantity |
10 µg |
| Quantitation Method |
Please see our FAQ |
|
Cell Type
|
Fibroblast
|
|
Transformant
|
Untransformed
|
|
Sample Source
|
DNA from Fibroblast
|
|
Race
|
Black/African American
|
|
Relation to Proband
|
proband
|
|
Confirmation
|
Clinical summary/Case history
|
|
Species
|
Homo sapiens
|
|
Common Name
|
Human
|
|
Remarks
|
|
| Passage Frozen |
8 |
| |
| IDENTIFICATION OF SPECIES OF ORIGIN |
Species of Origin Confirmed by Nucleoside Phosphorylase Isoenzyme Electrophoresis |
| |
| N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase |
According to the submitter, biochemical test results for this subject showed decreased enzyme activity. EC Number: 3.5.1.26 |
| |
| Gene |
AGA |
| Chromosomal Location |
4q34.3 |
| Allelic Variant 1 |
613228.0009; ASPARTYLGLUCOSAMINURIA |
| Identified Mutation |
133-BP DEL, NT807-940DEL, FS, TER; In a 12-year old American black patient [(GM03560) Hreidarsson et al. Clin Genet 23: 427 (1983)], Ikonen et al [Genomics 11: 206 (1991)] found homozygosity for a deletion of nucleotides 807-940. In this patient further sequence analysis of both cDNA and genomic DNA confirmed that a 134-bp exon was missing from the cDNA and that a G-to-T substitution had occurred in the adjacent 3-prime intron at position +1 of the splice donor site. Thus this was a splicing mutation. The mutation resulted in a transcript that was 134-bp shorter than normal. The mutation also resulted in the shift of the reading frame and a premature termination codon at the beginning of the following exon. |
| |
| Gene |
AGA |
| Chromosomal Location |
4q34.3 |
| Allelic Variant 2 |
613228.0009; ASPARTYLGLUCOSAMINURIA |
| Identified Mutation |
133-BP DEL, NT807-940DEL, FS, TER; In a 12-year old American black patient [(GM03560) Hreidarsson et al. Clin Genet 23: 427 (1983)], Ikonen et al [Genomics 11: 206 (1991)] found homozygosity for a deletion of nucleotides 807-940. In this patient further sequence analysis of both cDNA and genomic DNA confirmed that a 134-bp exon was missing from the cDNA and that a G-to-T substitution had occurred in the adjacent 3-prime intron at position +1 of the splice donor site. Thus this was a splicing mutation. The mutation resulted in a transcript that was 134-bp shorter than normal. The mutation also resulted in the shift of the reading frame and a premature termination codon at the beginning of the following exon. |
| Remarks |
Deficient N-aspartyl-beta-glycosaminidase; mental retardation and dysmorphic features; donor subject is homozygous for a splice mutation in the AGA gene (glycoasparaginase), a G>T substitution resulting in a 133 base pair deletion at positions 807 through 940 in the mRNA; non-Finnish pt |
| Mononen I, Heisterkamp N, Kaartinen V, Mononen T, Williams JC, Groffen J, Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene. J Biol Chem267:3196-9 1992 |
| PubMed ID: 1737774 |
| |
| Mononen I, Heisterkamp N, Kaartinen V, Williams JC, Yates JR 3d, Griffin PR, Hood LE, Groffen J, Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase. Proc Natl Acad Sci U S A88:2941-5 1991 |
| PubMed ID: 2011603 |
|