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Spectroscopy - Volume 24 2010, Issue 6, Pages 585-592



University Joseph Fourier, Grenoble, France

Institut Laue-Langevin, Grenoble, France

CNR-IOM, OGG, c-o Institut Laue-Langevin, Grenoble, France

Institut de Biologie Structurale, Grenoble, France

Department of Biochemistry, University of Oulu, Oulu, Finland

CNR-IOM, OGG, c-o Institut Laue-Langevin, BP 1566, rue Jules Horowitz-38042, Grenoble, France



Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Myelin is a multilamellar membrane which, wrapping the nerve axons, increases the efficiency of nervous signal transmission. Indeed, the molecular components of the myelin sheath interact tightly with each other and molecules on the axonal surface to drive myelination, to keep both myelin and the axon intact, and to transduce signals from myelin to the axon and vice versa. Myelin is strongly affected in human demyelinating diseases in both the central and peripheral nervous system CNS and PNS, respectively. Despite the presence of a well-defined set of myelin-specific proteins, little is known about the structure and the dynamics of these proteins, their interactions with the membrane and their influence on myelin stability. We present here the first neutron scattering results on the dynamics of the myelin sheath in PNS and of the interaction between its constituents. Specifically, the human P2 protein is shown to stabilize the lipid membrane upon binding to it.





Autor: W. Knoll, F. Natali, J. Peters, R. Nanekar, C. Wang, and P. Kursula

Fuente: https://www.hindawi.com/



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