O. Ibraghimovbeskrovnaya et al., HUMAN DYSTROGLYCAN - SKELETAL-MUSCLE CDNA, GENOMIC STRUCTURE, ORIGIN OF TISSUE-SPECIFIC ISOFORMS AND CHROMOSOMAL LOCALIZATION, Human molecular genetics, 2(10), 1993, pp. 1651-1657
Dystroglycan is a novel laminin binding component of the dystrophin-gl
ycoprotein complex which provides a linkage between the subsarcolemmal
cytoskeleton and the extracellular matrix. Here we report the cDNA an
d genomic structure of human dystroglycan. The human dystroglycan is e
ncoded by a single gene (DAG1) mapped to chromosome 3 band p21. The co
ding sequence is organized into two exons, separated by a large intron
. The predicted amino acid sequence of human and rabbit dystroglycan a
re 93% identical with predicted glycosylation sites being conserved. H
uman 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 co
re might modulate laminin binding. The relationship of dystroglycan to
human diseases is discussed.