Developmental Neuroscience
Original Paper
Carbohydrate Moieties of Myelin-Associated Glycoprotein, Major Glycoprotein of the Peripheral Nervous System Myelin and Other Myelin Glycoproteins Potentially Involved in Cell AdhesionBadache A.a · Burger D.b · Villarroya H.c · Robert Y.d · Kuchler S.a · Steck A.J.b · Zanetta J.aa Laboratoire de Neurobiologie moléculaire des Interactions cellulaires, Centre de Neurochimie du CNRS, Strasbourg, France; b Laboratoire de Neurobiologie, Centre Hospitalier Universitaire Vaudois, Lausanne, Suisse; c Laboratoire de Neurobiologie cellulaire moléculaire et clinique, INSERM U 134, Hôpital de la Salpêtrière, Paris; d Laboratoire d'Etudes radio-immunologiques, Département de Biologie, CEN Saclay, Gif-sur-Yvette, France
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Article / Publication Details
Received: April 28, 1992
Accepted: October 23, 1992
Published online: May 28, 2010
Issue release date: 1992
Number of Print Pages: 9
Number of Figures: 0
Number of Tables: 0
ISSN: 0378-5866 (Print)
eISSN: 1421-9859 (Online)
For additional information: https://www.karger.com/DNE
Abstract
The myelin-associated glycoprotein (MAG) and the major glycoprotein of the peripheral nervous system myelin (P0) are two members of the family of cell adhesion molecules (CAMs). A role in cell adhesion of the carbohydrate moiety of these molecules has been attributed to the presence of N-glycans bearing the HNK-1 carbohydrate epitope. On the other hand, it has been suggested that these glycoproteins could be ligands of an endogenous mannose-binding lectin present in myelin, the cerebellar soluble lectin (CSL). In order to further document the heterogeneity of the glycans of these two CAMs, we have used several probes: an anti-carbohydrate antibody of the HNK-1 type, called Elec-39, the plant lectin concanavalin A (ConA), and the endogenous lectin CSL involved in myelin compaction. This study shows that CSL binds to a small proportion of the polypeptide chains of MAG found in adult CNS of rats and man and the polypeptide chains of P0 molecules from adult human and rat sciatic nerve. For MAG from adult rat brain, the binding of CSL is restricted to glycans of polypeptide chains which could be separated from the others according to their solubility properties. These MAG molecular entities react also with the Elec-39 antibody and with ConA. These results confirm that P0 and MAG are heterogeneous in their carbohydrate moieties. They show that, in the CNS of adult rats, the MAG molecules potentially involved in cell adhesion as ligands of the endogenous lectin CSL possess polypeptide chains physicochemically different from the others, but endowed with similar porperties to those of other CSL ligands, unrelated to MAG, present in myelin preparations.
© 1992 S. Karger AG, Basel
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Article / Publication Details
Received: April 28, 1992
Accepted: October 23, 1992
Published online: May 28, 2010
Issue release date: 1992
Number of Print Pages: 9
Number of Figures: 0
Number of Tables: 0
ISSN: 0378-5866 (Print)
eISSN: 1421-9859 (Online)
For additional information: https://www.karger.com/DNE
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Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher.Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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