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Historical Background
Thirty years ago, the biochemical studies of plasma membranes of rodent NG108–15 neural hybrid cells, 14-day embryonic chicken brain, and mouse 3 T3 fibroblasts had led to the identification of cranin (LBP120), a glycosylated laminin-binding protein. Later, by sucrose-gradient centrifugation following purification of proteins from heavy microsomes of rabbit skeletal muscles using wheat germ agglutinin and DEAE-sepharose, four novel glycoproteins associated with dystrophin were purified and labelled as the “dystrophin-glycoprotein complex (DGC)” (Ervasti et al. 1990). At the center of this complex, the dystroglycan (DG) has been identified as a glycan component whose amino acid sequence is identical to cranin. Since then, other members of the DGC were identified. Thus, the DGC provides a link between proteins of the extracellular matrix (ECM) and...
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Bello, V., Darribère, T. (2018). Dystroglycan. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101578
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DOI: https://doi.org/10.1007/978-3-319-67199-4_101578
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