Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin

TY - JOUR

T1 - Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin

AU - Schachner, M

AU - Bartsch, U

N1 - Copyright 2000 Wiley-Liss, Inc.

PY - 2000/1/15

Y1 - 2000/1/15

N2 - The myelin-associated glycoprotein, a minor component of myelin in the central and peripheral nervous system, has been implicated in the formation and maintenance of myelin. Although the analysis of MAG null mutants confirms this view, the phenotype of this mutant is surprisingly subtle. In the CNS of MAG-deficient mice, initiation of myelination, formation of morphologically intact myelin sheaths and to a minor extent, integrity of myelin is affected. In the PNS, in comparison, only maintenance of myelin is impaired. Recently, the large isoform of MAG has been identified as the functionally important isoform in the CNS, whereas the small MAG isoform is sufficient to maintain the integrity of myelinated fibers in the PNS. Remarkably, none of the different defects in the MAG mutant is consistently associated with each myelinated fiber. These observations suggest that other molecules performing similar functions as MAG might compensate, at least partially, for the absence of MAG in the null mutant.

AB - The myelin-associated glycoprotein, a minor component of myelin in the central and peripheral nervous system, has been implicated in the formation and maintenance of myelin. Although the analysis of MAG null mutants confirms this view, the phenotype of this mutant is surprisingly subtle. In the CNS of MAG-deficient mice, initiation of myelination, formation of morphologically intact myelin sheaths and to a minor extent, integrity of myelin is affected. In the PNS, in comparison, only maintenance of myelin is impaired. Recently, the large isoform of MAG has been identified as the functionally important isoform in the CNS, whereas the small MAG isoform is sufficient to maintain the integrity of myelinated fibers in the PNS. Remarkably, none of the different defects in the MAG mutant is consistently associated with each myelinated fiber. These observations suggest that other molecules performing similar functions as MAG might compensate, at least partially, for the absence of MAG in the null mutant.

KW - Animals

KW - Central Nervous System

KW - Immunohistochemistry

KW - Mice

KW - Mice, Neurologic Mutants

KW - Myelin Sheath

KW - Myelin-Associated Glycoprotein

KW - Peripheral Nervous System

KW - Phenotype

KW - Protein Isoforms

KW - Signal Transduction

KW - Journal Article

KW - Review

M3 - SCORING: Journal article

C2 - 10625334

VL - 29

SP - 154

EP - 165

JO - GLIA

JF - GLIA

SN - 0894-1491

IS - 2

ER -