Living reference work entry
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...
KeywordsMuscular Dystrophy Glycan Structure Notochord Cell Congenital Muscular Dystrophy Mycobacterium Leprae
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- Martínez-Vieyra IA, Vásquez-Limeta A, González-Ramírez R, Morales-Lázaro SL, Mondragón M, Mondragón R, et al. A role for β-dystroglycan in the organization and structure of the nucleus in myoblasts. Biochim Biophys Acta. 2013;1833(3):698–711. doi:10.1016j.bbamcr.2012.11.019.CrossRefPubMedGoogle Scholar
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