Altered binding of Ricinus communis I lectin by muscle membranes in Duchenne muscular dystrophy.
Recently, it has become clear that a structural or functional abnormality of the plasma membrane may be involved in the pathogenesis of Duchenne muscular dystrophy (DMD). We have used a D-galactose specific lectin, that binds strongly to the muscle cell surface, to search for differences in sarcolemmal staining in biopsies from 5 normal and 7 DMD individuals. Electron optical studies revealed a dramatic and consistent decrease in lectin binding by the muscle plasma membrane in DMD. Although unable at this stage to identify the specific molecular abnormality responsible for this decreased staining, the results provide good evidence that a basic structural change within the plasma membrane may be intimately associated with DMD.
D000293:Adolescent; D000328:Adult; D002648:Child; D002675:Child, Preschool; D005260:Female; D006017:Glycolipids / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D007223:Infant; D037102:Lectins / Q000378:metabolism*; D008297:Male; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D009136:Muscular Dystrophies / Q000378:metabolism*; D037121:Plant Lectins; D012508:Sarcolemma / Q000378:metabolism*
D006017:Glycolipids; D006023:Glycoproteins; D037102:Lectins; D008563:Membrane Lipids; D008565:Membrane Proteins; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1