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Brain Res. 2016 Jun 15;1641(Pt A):43-63. doi: 10.1016/j.brainres.2015.10.037. Epub 2015 Oct 28.

Evolution of myelin ultrastructure and the major structural myelin proteins.

Author information

1
Department of Electrical and Computer Engineering, Northeastern University, 360 Huntington Avenue, Boston, MA 02115, USA. Electronic address: h.inouye@neu.edu.
2
Biology Department, Boston College, 140 Commonwealth Avenue, Chestnut Hill, MA 02467-3811, USA. Electronic address: kirschnd@bc.edu.

Abstract

Myelin sheaths, as the specialized tissue wrapping the nerve fibers in the central and peripheral nervous systems (CNS and PNS), are responsible for rapid conduction of electrical signals in these fibers. We compare the nerve myelin sheaths of different phylogenetic origins-including mammal, rodent, bird, reptile, amphibian, lungfish, teleost, and elasmobranch-with respect to periodicities and inter-membrane separations at their cytoplasmic and extracellular appositions, and correlate these structural parameters with biochemical composition. P0 glycoprotein and P0-like proteins are present in PNS of terrestrial species or land vertebrates (Tetrapod) and in CNS and PNS of aquatic species. Proteolipid protein (PLP) is a major component only in the CNS myelin of terrestrial species and is involved in compaction of the extracellular apposition. The myelin structures of aquatic garfish and lungfish, which contain P0-like protein both in CNS and PNS, are similar to those of terrestrial species, indicating that they may be transitional organisms between water and land species. This article is part of a Special Issue entitled SI: Myelin Evolution.

KEYWORDS:

Biophysics; Evolution; Myelin structure; Neutron diffraction; Phylogeny; X-ray diffraction

PMID:
26519753
DOI:
10.1016/j.brainres.2015.10.037
[Indexed for MEDLINE]

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