Myelin associated glycoprotein modulates glia-axon contact in vivo

✍ Scribed by C. Li; B. Trapp; S. Ludwin; A. Peterson; J. Roder

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 494 KB
• Volume: 51
• Category: Article
• ISSN: 0360-4012
• DOI: 10.1002/(sici)1097-4547(19980115)51:2<210::aid-jnr9>3.0.co;2-g

✦ Synopsis

Myelin-associated glycoprotein (MAG) was postulated to play an important role in myelination. However, we showed previously that MAG null mutants exhibited no gross abnormality in myelination. Ultrastructural studies revealed subtle alterations in periaxonal organisation, indicating a restricted structural role for MAG in the formation and maintenance of periaxonal structures . Here we show that myelination in MAG deficient mice is not as finely controlled as it is in wild type mice. The abnormalities manifest themselves as a decrease in the proportion of myelinated axons and a reciprocal increase in the proportion of unmyelinated axons in mutants' optic nerves. In addition, dysregulated myelination is occasionally observed in the form of multiply myelinated fibres, grouping of myelinated axons and myelin debris by a large myelin sheath, redundant myelin loops and, very rarely, massive myelin surrounding relatively small axons. Thus, in the absence of MAG, some glial cells seem unable to determine when, where and how much myelin should be laid down. These data support the notion of MAG being a glial recognition/adhesion molecule. A model is proposed regarding the roles MAG could play in the formation and maintenance of myelin structure.