Besides its structural function in skeletal muscle, dystroglycan has also signalingįunctions and is found in many other tissues, especially the central and peripheral nervous systems, the retina, and epithelialĬells. In the DGC dystroglycan forms a membrane-spanning link between the intracellular dystrophinĪnd the extracellular laminin α2 chain. The DGC is thought to be essential for mediating mechanical forces between the actin cytoskeleton and the extracellular Therefore, this study defines a novel syntenic region among dog chromosome 20q15, human chromosome 3p21, and murineĭystroglycan is an important part of the skeletal muscle dystrophin-associated glycoprotein complex (DGC) ( Durbeej et al. The genes for aminomethyltransferase ( AMT), bassoon ( BSN), TCTA( T- cell leukemia translocation- associated) gene, and an as yet uncharacterized protein are located very close to the DAG1gene. The analysis of the entire reported sequence revealed that The dog DAG1 gene was assigned to chromosome 20q15.1–q15.2 by FISH analysis. The dog DAG1 gene we determined the transcription start site and several naturally occurring polymorphisms, which partially result inĪmino acid substitutions of the dystroglycan protein. ![]() Its 2679-nucleotide ORF encodesĪ polypeptide of 892 amino acids, which is highly similar to human, rabbit, and bovine orthologs. Here we report the cloning and sequencing of 162 kb of dog genomic DNA containing theĬomplete ∼71-kb canine DAG1 gene, which consists of three exons, with the translation start codon located in exon 2. So far the genomic organization of theĭystroglycan gene DAG1 has not been completely investigated. It is also involved in the organization of basement membranes. Dystroglycan is a laminin binding protein, which provides a structural link between the subsarcolemmal cytoskeleton and theĮxtracellular matrix.
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