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Age‐Dependent Changes in the Oligosaccharide Structure of the Major Myelin Glycoprotein, P 0
Author(s) -
Brunden Kurt R.
Publication year - 1992
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.1471-4159.1992.tb10038.x
Subject(s) - oligosaccharide , glycoprotein , concanavalin a , myelin associated glycoprotein , biochemistry , chemistry , mannose , myelin , lectin , biology , endocrinology , central nervous system , in vitro
The single oligosaccharide moiety of the major myelin glycoprotein, P 0 , resides in an immunoglobulin‐like domain that appears to participate in homophilic binding. The studies presented here indicate that the structure of the P 0 oligosaccharide from rat nerve changes as a function of Schwann cell age. Examination of 5‐day‐old nerve revealed that P 0 contained predominantly endo‐β‐β‐acetylglucosa‐minidase H (endo H)‐resistant, complex‐type oligosaccharide. In contrast, P 0 from adult rats had mostly endo H‐sensitive carbohydrate, indicating the presence of appreciable high‐mannose and/or hybrid‐type oligosaccharide on the glycoprotein. The endo H‐sensitive and resistant P 0 of adult nerve could be readily phosphorylated by protein kinase C, as could the complex‐type P 0 from 5‐day‐old nerve. This suggests that the glycoprotein progresses to the plasma membrane and myelin regardless of the type of oligosaccharide chain. Analysis of 35 SO 4 2‐labeled P 0 showed that the sulfate group was found on both endo H‐sensitive and ‐resistant oligosaccharide. The endo H‐sensitive P 0 carbohydrate from adult nerve appears to be primarily of the hybrid type, as evidenced by (a) the elution profile of [ 3 H]mannose‐labeled P 0 glycopeptides from adult nerve during concanavalin A chromatography and (b) the inability of P 0 from adult nerve to interact with Galanthus nivalis agglutinin. The observed age‐dependent changes of P 0 oligosaccharide may modify the binding properties of this myelin glycoprotein.