Mutation of Large, which encodes a putative glycosyltransferase, in an animal model of muscular dystrophy
| Autor: | Prabhjit K. Grewal, Jane E. Hewitt |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Glycosylation
Positional cloning Molecular Sequence Data Mutant Biophysics N-Acetylglucosaminyltransferases medicine.disease_cause Biochemistry Muscular Dystrophies Mice medicine Dystroglycan Animals Humans Amino Acid Sequence Muscular dystrophy Dystroglycans Molecular Biology Genetics Mutation Membrane Glycoproteins biology Glycosyltransferase Gene medicine.disease Molecular biology Phenotype Neoplasm Proteins Cytoskeletal Proteins Mice Inbred mdx biology.protein ITGA7 |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1573:216-224 |
| ISSN: | 0304-4165 |
| Popis: | The myodystrophy (myd) mutation arose spontaneously and has an autosomal recessive mode of inheritance. Homozygous mutant mice display a severe, progressive muscular dystrophy. Using a positional cloning approach, we identified the causative mutation in myd as a deletion within the Large gene, which encodes a putative glycosyltransferase with two predicted catalytic domains. By immunoblotting, the alpha-subunit of dystroglycan, a key muscle membrane protein, is abnormal in myd mice. This aberrant protein might represent altered glycosylation of the protein and contribute to the muscular dystrophy phenotype. Our results are discussed in the light of recent reports describing mutations in other glycosyltransferase genes in several forms of human muscular dystrophy. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect