Proteolipid protein cannot replace P0 protein as the major structural protein of peripheral nervous system myelin. Issue 1 (28th July 2014)

• Record Type: Journal Article
• Authors: Yin, Xinghua; Kiryu‐Seo, Sumiko; Kidd, Grahame J.; Feltri, M. Laura; Wrabetz, Lawrence; Trapp, Bruce D.
• Is Part Of: Glia. Volume 63:Issue 1(2015:Jan.)
• Page Start: 66
• Page End: 77
• Publication Date: 2014-07-28
• Subjects: Neuroglia -- Periodicals; Neurology -- Periodicals; 611.0188
• DOI: 10.1002/glia.22733
• Languages: English
• ISSNs: 0894-1491

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The central nervous system (CNS) of terrestrial vertebrates underwent a prominent molecular change when proteolipid protein (PLP) replaced P₀ protein as the most abundant protein of CNS myelin. However, PLP did not replace P₀ in peripheral nervous system (PNS) myelin. To investigate the possible consequences of a PLP to P₀ shift in PNS myelin, we engineered mice to express PLP instead of P₀ in PNS myelin (PLP‐PNS mice). PLP‐PNS mice had severe neurological disabilities and died between 3 and 6 months of age. Schwann cells in sciatic nerves from PLP‐PNS mice sorted axons into one‐to‐one relationships but failed to form myelin internodes. Mice with equal amounts of P₀ and PLP had normal PNS myelination and lifespans similar to wild‐type (WT) mice. When PLP was overexpressed with one copy of the P₀ gene, sciatic nerves were hypomyelinated; mice displayed motor deficits, but had normal lifespans. These data support the hypothesis that while PLP can co‐exist with P₀ in PNS myelin, PLP cannot replace P₀ as the major structural protein of PNS myelin. GLIA 2015;63:66–77</p> </abstract>