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The membrane palmitoylated protein, MPP6, is involved in myelin formation in the mouse peripheral nervous system

Authors
  • Saitoh, Yurika1, 2
  • Kamijo, Akio1
  • Yamauchi, Junji3
  • Sakamoto, Takeharu4
  • Terada, Nobuo1
  • 1 Shinshu University, Health Science Division, Department of Medical Sciences, Graduate School of Medicine, Science and Technology, 3-1-1 Asahi, Matsumoto City, Nagano, 390-8621, Japan , Matsumoto City (Japan)
  • 2 Teikyo University of Science, Center for Medical Education, Adachi-ku, Tokyo, Japan , Tokyo (Japan)
  • 3 Tokyo University of Pharmacy and Life Sciences, Laboratory of Molecular Neuroscience and Neurology, School of Life Sciences, Hachioji City, Tokyo, Japan , Hachioji City (Japan)
  • 4 The University of Tokyo, Division of Cellular and Molecular Biology, The Institute of Medical Science, Minato-ku, Tokyo, Japan , Tokyo (Japan)
Type
Published Article
Journal
Histochemistry and Cell Biology
Publisher
Springer Berlin Heidelberg
Publication Date
Oct 24, 2018
Volume
151
Issue
5
Pages
385–394
Identifiers
DOI: 10.1007/s00418-018-1745-y
Source
Springer Nature
Keywords
License
Yellow

Abstract

A membrane skeletal molecular complex, protein 4.1G–membrane palmitoylated protein 6 (MPP6)–Lin7–cell adhesion molecule 4 (CADM4), is incorporated in Schwann cells, especially in Schmidt–Lanterman incisures (SLIs), in the mouse peripheral nervous system (PNS). MPP6, Lin7, and CADM4 are transported to SLIs by 4.1G. In this study, we created MPP6-deficient mice and evaluated myelin structure and MPP6 protein complexes. In SLIs in MPP6-deficient nerves, Lin7 was rarely detected by immunohistochemistry and western blotting, but the localization and amount of CADM4 and 4.1G were not altered. Motor activity was not significantly impaired in a tail-suspension test, but the sciatic nerves of MPP6-deficient mice had thicker myelin in internodes by electron microscopy compared to that of wild-type mice. These results indicate that the MPP6–Lin7 complex regulates myelin formation.

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