Journal article
Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization
Human molecular genetics, Vol.2(10), pp.1651-1657
1993
DOI: 10.1093/hmg/2.10.1651
PMID: 8268918
Abstract
Dystroglycan is a novel laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Here we report the cDNA and genomic structure of human dystroglycan. The human dystroglycan is encoded by a single gene (DAG1) mapped to chromosome 3 band p21. The coding sequence is organized into two exons, separated by a large intron. The predicted amino acid sequence of human and rabbit dystroglycan are 93% identical with predicted glycosylation sites being conserved. Human dystroglycan is expressed in a variety of fetal and adult tissues. Our data suggest that muscle and non-muscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence. Therefore, we hypothesize that variable glycosylation of the conserved protein core might modulate laminin binding. The relationship of dystroglycan to human diseases is discussed.
Details
- Title: Subtitle
- Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization
- Creators
- Oxana Ibraghimov-BeskrovnayaAthena MilatovichTayfun OzcelikBin YangKevin KoepnickUta FranckeKevin P Campbell
- Resource Type
- Journal article
- Publication Details
- Human molecular genetics, Vol.2(10), pp.1651-1657
- DOI
- 10.1093/hmg/2.10.1651
- PMID
- 8268918
- ISSN
- 0964-6906
- eISSN
- 1460-2083
- Language
- English
- Date published
- 1993
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Teaching and Learning
- Record Identifier
- 9984068383402771
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