NA02057
DNA from Fibroblast
Description:
ASPARTYLGLUCOSAMINURIA
ASPARTYLGLUCOSAMINIDASE; AGA
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Repository
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NIGMS Human Genetic Cell Repository
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| Subcollection |
Heritable Diseases
Lysosomal Storage Diseases |
| Class |
Disorders of Carbohydrate Metabolism |
| Quantity |
10 µg |
| Quantitation Method |
Please see our FAQ |
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Cell Type
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Fibroblast
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Transformant
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Untransformed
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Sample Source
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DNA from Fibroblast
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Race
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White
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Ethnicity
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FINNISH
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Relation to Proband
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proband
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Confirmation
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Clinical summary/Case history
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Species
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Homo sapiens
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Common Name
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Human
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Remarks
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| Passage Frozen |
6 |
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| IDENTIFICATION OF SPECIES OF ORIGIN |
Species of Origin Confirmed by Nucleoside Phosphorylase Isoenzyme Electrophoresis |
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| MUTATION VERIFICATION |
Fisher and Aronson (J. Biol. Chem. 266:12105-12113) reported two mutations in the aspartylglucosaminidase gene of this aspartylglucosaminuria patient. The two base changes consisted of a G482>A transition that resulted in an Arg 161>Gln substitution and a G488>C transversion that caused Cys 163>Ser. Expression studies in COS-1 cells revealed only the Cys 163>Ser mutation caused a deficiency of enzyme activity. |
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| 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; <10% activity. |
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| Gene |
AGA |
| Chromosomal Location |
4q34.3 |
| Allelic Variant 1 |
R161Q; ASPARTYLGLUCOSAMINURIA, FINNISH TYPE |
| Identified Mutation |
ARG161GLN |
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| Gene |
AGA |
| Chromosomal Location |
4q34.3 |
| Allelic Variant 1 |
613228.0001; ASPARTYLGLUCOSAMINURIA, FINNISH TYPE |
| Identified Mutation |
CYS163SER; By direct sequencing of PCR-amplified AGA cDNA from an AGU patient, Ikonen et al. [Genomics 11: 206 (1991)] found a G-to-C mutation resulting in the substitution of serine for cysteine at codon 163. |
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| Gene |
AGA |
| Chromosomal Location |
4q34.3 |
| Allelic Variant 2 |
613228.0001; ASPARTYLGLUCOSAMINURIA, FINNISH TYPE |
| Identified Mutation |
CYS163SER; By direct sequencing of PCR-amplified AGA cDNA from an AGU patient, Ikonen et al. [Genomics 11: 206 (1991)] found a G-to-C mutation resulting in the substitution of serine for cysteine at codon 163. |
| Remarks |
Finnish; less than 10% of normal Naspartyl-beta-glycosaminidase activity; the donor subject is heterozygous for a G-to-A transition (CGG>CAG) at nucleotide 482 of the AGA gene which results in a substitution of glutamine for arginine at codon 161 [Arg161Gln (R161Q)] and is homozygous for a G-to-C transversion (TGC>TCC) at nucleotide 488 of the AGA gene which results in a substitution of serine for cysteine at codon 163 [Cys163Ser (C163S)]. |
| Fisher KJ, Aronson NN Jr, Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits. J Biol Chem266:12105-13 1991 |
| PubMed ID: 1904874 |
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| 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 |
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| Aula P, Autio S, Raivio K, Nanto V, Detection of heterozygotes for aspartylglucosaminuria (AGU) in cultured fibroblasts. Humangenetik25:307-14 1974 |
| PubMed ID: 4464238 |
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