Evidence for possible interactions between PLP and DM20 within the myelin sheath
✍ Scribed by M. McLaughlin; D.J.B. Hunter; C.E. Thomson; D. Yool; D. Kirkham; A.A. Freer; I.R. Griffiths
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 286 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0894-1491
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✦ Synopsis
PLP and its smaller DM20 isoform constitute the major proteins of CNS myelin. Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present study shows that each isoform is capable individually of inserting into compact myelin. Employing chromatographic extraction procedures designed to maintain the natural conformation of the proteins we found that most PLP and DM20 remained associated. Using an antibody specific to the PLP isoform, we were able to co-immunoprecipitate DM20 from the major fraction of the extracted equine myelin and from mouse native whole myelin. We suggest that PLP and DM20 may form a hetero-oligomeric complex within the myelin sheath, probably in association with specific lipids and that this arrangement is essential for the normal structure of myelin and axons.