NA01675
DNA from Fibroblast
Description:
TAY-SACHS DISEASE, AB VARIANT
GM2 ACTIVATOR; GM2A
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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 Lipid 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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Black/African American
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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 |
5 |
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| IDENTIFICATION OF SPECIES OF ORIGIN |
Species of Origin Confirmed by Nucleoside Phosphorylase Isoenzyme Electrophoresis |
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| Gene |
GM2A |
| Chromosomal Location |
5q31.3-q33.1 |
| Allelic Variant 1 |
272750.0001; GM2-GANGLIOSIDOSIS, VARIANT AB |
| Identified Mutation |
CYS107ARG; In a patient with immunologically proven GM2 activator protein deficiency, Schroder et al. [FEBS Lett 290: 1 (1991)] found a T-to-C transition at nucleotide 412 (counted from A of the initiation codon), which resulted in the substitution of arginine for the normal cysteine-107 in the mature GM2 activator protein. Xie et al. [Am J Hum Genet 50: 1046 (1992)] found a T-to-C transition in nucleotide 412 of the GM2A gene, in homozygous form, in a patient with the AB variant. The change was predicted to result in the substitution of arginine for cysteine-138. Expression studies of the mutant supported the view that the point mutation described was responsible for the disease phenotype. The mutations identified by Schroder et al. [FEBS Lett 290: 1 (1991)] (CYS107ARG) and Xie et al. [Am J Hum Genet 50: 1046 (1992)] (CYS138ARG) are the same but derived from different amino acid numbering systems. |
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| Gene |
GM2A |
| Chromosomal Location |
5q31.3-q33.1 |
| Allelic Variant 2 |
272750.0001; GM2-GANGLIOSIDOSIS, VARIANT AB |
| Identified Mutation |
CYS107ARG; In a patient with immunologically proven GM2 activator protein deficiency, Schroder et al. [FEBS Lett 290: 1 (1991)] found a T-to-C transition at nucleotide 412 (counted from A of the initiation codon), which resulted in the substitution of arginine for the normal cysteine-107 in the mature GM2 activator protein. Xie et al. [Am J Hum Genet 50: 1046 (1992)] found a T-to-C transition in nucleotide 412 of the GM2A gene, in homozygous form, in a patient with the AB variant. The change was predicted to result in the substitution of arginine for cysteine-138. Expression studies of the mutant supported the view that the point mutation described was responsible for the disease phenotype. The mutations identified by Schroder et al. [FEBS Lett 290: 1 (1991)] (CYS107ARG) and Xie et al. [Am J Hum Genet 50: 1046 (1992)] (CYS138ARG) are the same but derived from different amino acid numbering systems. |
| Remarks |
Normal B-hexosaminidase A alpha and beta chains; cDNA and genomic DNA of the GM2 activator protein gene are homozygous for a T>C412 transition that results in a substitution of Cys-138 by Arg; normal levels of activator protein mRNA |
| Xie B, Wang W, Mahuran DJ, A Cys138-to-Arg substitution in the GM2 activator protein is associated with the AB variant form of GM2 gangliosidosis. Am J Hum Genet50:1046-52 1992 |
| PubMed ID: 1570834 |
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| Hasilik A, Neufeld EF, Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues. J Biol Chem255:4946-50 1980 |
| PubMed ID: 6989822 |
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| Hasilik A, Neufeld EF, Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight. J Biol Chem255:4937-45 1980 |
| PubMed ID: 6989821 |
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