Premium
Characterization of Axonally Transported Glycoproteins in Regenerating Garfish Olfactory Nerve
Author(s) -
Cole Gregory J.,
Elam John S.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb04796.x
Subject(s) - glycoprotein , concanavalin a , pronase , biochemistry , chemistry , membrane glycoproteins , glucosamine , glycopeptide , sodium dodecyl sulfate , wheat germ agglutinin , lectin , gel electrophoresis , trypsin , enzyme , in vitro , antibiotics
This study examined changes in composition and concanavalin A (Con A) binding of axonally transported glycoproteins and their pronase‐generated glycopeptides in regenerating garfish olfactory nerve. A previous study had demonstrated a regeneration‐related increase in the proportion of [ 3 H]glucosamine label in lower‐molecular‐weight Con A‐binding glycopeptides derived from transported glycoproteins. Further analysis of carbohydrate composition shows that these molecules resemble mannose‐rich oligosaccharides in composition and are increased in absolute amount in regenerating nerve. Subcellular analysis shows that the Con A‐binding glycopeptides are enriched in membrane subfractions, particularly in a high‐density fraction that morphologically resembles isolated cell surface coat. Regeneration‐related changes in intact axonally transported glycoproteins were also detected. Sodium dodecyl sulfate gel electrophoresis of transport‐labeled glycoproteins disclosed growth‐correlated increases in radioactivity associated with 180–200K, 105–115K, and 80–90K components, while a 150–160K molecular weight class of glycoproteins was diminished in relative labeling. Intact glycoproteins displaying an affinity for Con A were also augmented in regenerating nerve, the increases occurring primarily in molecules in the 50–140K range.