PMID: 9545593May 16, 1998Paper

Oligomerization of beta-dystroglycan in rabbit diaphragm and brain as revealed by chemical crosslinking

Biochimica Et Biophysica Acta
D M Finn, K Ohlendieck

Abstract

The surface component beta-dystroglycan is a member of the dystrophin-glycoprotein complex providing a trans-sarcolemmal linkage between the actin membrane cytoskeleton and the extracellular matrix component laminin-alpha2. Although abnormalities in this complex are involved in the pathophysiology of various neuromuscular disorders, little is known about the organization of dystrophin-associated glycoproteins in diaphragm and brain. We therefore investigated the oligomerization of beta-dystroglycan and its connection with the most abundant dystrophin homologues in these two tissues. Employing detergent solubilization and alkaline extraction procedures of native membranes, it was confirmed that beta-dystroglycan behaves like an integral surface molecule as predicted by its cDNA sequence. Immunoblot analysis following chemical crosslinking of native membranes showed that beta-dystroglycan has a tendency to form high-molecular-mass complexes. Within these crosslinkable complexes, immuno-reactive overlaps were observed between beta-dystroglycan, alpha-dystroglycan, laminin and 427 kDa dystrophin in diaphragm and skeletal muscle. In synaptosomes, the major brain dystrophin isoform Dp116 also exhibited an immuno-reactive overlap with...Continue Reading

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Citations

Oct 6, 1999·Current Opinion in Cell Biology·M D Henry, K P Campbell
Jan 18, 2006·Journal of Cell Science·Rita Barresi, Kevin P Campbell
Aug 26, 1998·Biochemical and Biophysical Research Communications·D M FinnK Ohlendieck
Sep 24, 2021·Pflügers Archiv : European journal of physiology·Kay Ohlendieck, Dieter Swandulla

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