Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin
β Scribed by Melitta Schachner; Udo Bartsch
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 776 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0894-1491
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β¦ Synopsis
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.
π SIMILAR VOLUMES
The myelin-associated glycoprotein (MAG) exhibits an abnormally high apparent molecular weight in sciatic nerve, but not in brain, of dysmyelinating trembler mutants (Inuzuka et al.: J Neurochem 44:79> 797,1985). Antibodies to the large and small isoforms of MAG (L-and S-MAG) and probes for oligosac