Biochemical Demonstration of the Myelin‐Associated Glycoprotein in the Peripheral Nervous System

Biochemical Demonstration of the Myelin‐Associated Glycoprotein in the Peripheral Nervous System Abstract: Recent immunocytochemical studies indicated that the myelin‐associated glycoprotein (MAG) is localized in the periaxonal region of central nervous system (CNS) and peripheral nervous system (PNS) myelin sheaths but previous biochemical studies had not demonstrated the presence of MAG in peripheral nerve. The glycoproteins in rat sciatic nerves were heavily labeled by injection of (3H)fucose in order to re‐examine whether MAG could be detected chemically in peripheral nerve. Myelin and a myelin‐related fraction, WI, were isolated from the nerves. Labeled glycoproteins in the PNS fractions were extracted by the lithium diiodosalicylate (LIS)‐phenol procedure, and the extracts were treated with antiserum prepared to CNS MAG in a double antibody precipitation. This resulted in the immune precipitation of a single (3H)fucose‐labeled glycoprotein with electrophoretic mobility very similar to that of (14C)fucose‐labeled MAG from rat brain. A sensitive peptide mapping procedure involving iodination with Bolton‐Hunter reagent and autoradiography was used to compare the peptide maps generated by limited proteolysis from this PNS component and CNS MAG. The peptide maps produced by three distinct proteases were virtually identical for the two glycoproteins, showing that the PNS glycoprotein is MAG. The MAG in the PNS myelin and Wl fractions was also demonstrated by Coomassie blue and periodic acid‐Schiff staining of gels on which the whole US‐phenol extracts were electrophoresed, and densitometric scanning of the gels indicated that both fractions contained substantially less MAG than purified rat brain myelin. The presence of MAG in the periaxonal region of both peripheral and central myelin sheaths is consistent with a similar involvement of this glycoprotein in axon‐sheath cell interactions in the PNS and CNS. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

Biochemical Demonstration of the Myelin‐Associated Glycoprotein in the Peripheral Nervous System

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Publisher
Wiley
Copyright
Copyright © 1982 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
D.O.I.
10.1111/j.1471-4159.1982.tb12551.x
Publisher site
See Article on Publisher Site

Abstract

Abstract: Recent immunocytochemical studies indicated that the myelin‐associated glycoprotein (MAG) is localized in the periaxonal region of central nervous system (CNS) and peripheral nervous system (PNS) myelin sheaths but previous biochemical studies had not demonstrated the presence of MAG in peripheral nerve. The glycoproteins in rat sciatic nerves were heavily labeled by injection of (3H)fucose in order to re‐examine whether MAG could be detected chemically in peripheral nerve. Myelin and a myelin‐related fraction, WI, were isolated from the nerves. Labeled glycoproteins in the PNS fractions were extracted by the lithium diiodosalicylate (LIS)‐phenol procedure, and the extracts were treated with antiserum prepared to CNS MAG in a double antibody precipitation. This resulted in the immune precipitation of a single (3H)fucose‐labeled glycoprotein with electrophoretic mobility very similar to that of (14C)fucose‐labeled MAG from rat brain. A sensitive peptide mapping procedure involving iodination with Bolton‐Hunter reagent and autoradiography was used to compare the peptide maps generated by limited proteolysis from this PNS component and CNS MAG. The peptide maps produced by three distinct proteases were virtually identical for the two glycoproteins, showing that the PNS glycoprotein is MAG. The MAG in the PNS myelin and Wl fractions was also demonstrated by Coomassie blue and periodic acid‐Schiff staining of gels on which the whole US‐phenol extracts were electrophoresed, and densitometric scanning of the gels indicated that both fractions contained substantially less MAG than purified rat brain myelin. The presence of MAG in the periaxonal region of both peripheral and central myelin sheaths is consistent with a similar involvement of this glycoprotein in axon‐sheath cell interactions in the PNS and CNS.

Journal

Journal of NeurochemistryWiley

Published: Sep 1, 1982

References

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