Denervation-induced changes in lectin binding to sarcolemmal glycoproteins: exposure of cryptic recognition sites.
The increase in Concanavalin A (ConA) binding to sarcolemmal membranes of rat skeletal muscle following denervation has been attributed to conformational changes in membrane glycoproteins resulting in the unmasking of previously cryptic ConA binding sites (Leung et al., 1982). In this study, analysis of lectin binding patterns to alpha-fucosidase- or sialidase-treated sarcolemmal membranes reveals that the fucose moieties of carbohydrate structures may be principally involved in the unmasking process. By contrast, sialic acid has no apparent effect on the availability of the number of ConA binding sites, but plays a significant role in the masking of other lectin recognition sites.
Iannello
R C
RC
Murdoch Institute, Royal Children's Hospital, Melbourne, Victoria, Australia.
Jeffrey
P L
PL
D000818:Animals; D001665:Binding Sites; D005260:Female; D066298:In Vitro Techniques; D007700:Kinetics; D037102:Lectins / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D009121:Muscle Denervation; D009132:Muscles / Q000294:innervation / Q000378:metabolism; D009439:Neuraminidase; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012508:Sarcolemma / Q000378:metabolism*; D005644:alpha-L-Fucosidase
D037102:Lectins; D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D009439:Neuraminidase; D005644:alpha-L-Fucosidase