α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath

Schwann cells integrate signals deriving from the axon and the basal lamina to myelinate peripheral nerves. Integrin α6β4 is a laminin receptor synthesized by Schwann cells and displayed apposed to the basal lamina. α6β4 integrin expression in Schwann cells is induced by axons at the onset of myelin...

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Prif Awduron: Nodari, Alessandro, Previtali, Stefano C., Dati, Gabriele, Occhi, Simona, Court, Felipe A., Colombelli, Cristina, Zambroni, Desirée, Dina, Giorgia, Del Carro, Ubaldo, Campbell, Kevin P., Quattrini, Angelo, Wrabetz, Lawrence, Feltri, M. Laura
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Iaith:English
Cyhoeddwyd: Society for Neuroscience 2008
Pynciau:
Brief Communications
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC2597422/
https://ncbi.nlm.nih.gov/pubmed/18579745
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1523/JNEUROSCI.0326-08.2008
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id pubmed-2597422
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spelling pubmed-25974222009-06-24 α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath Nodari, Alessandro Previtali, Stefano C. Dati, Gabriele Occhi, Simona Court, Felipe A. Colombelli, Cristina Zambroni, Desirée Dina, Giorgia Del Carro, Ubaldo Campbell, Kevin P. Quattrini, Angelo Wrabetz, Lawrence Feltri, M. Laura J Neurosci Brief Communications Schwann cells integrate signals deriving from the axon and the basal lamina to myelinate peripheral nerves. Integrin α6β4 is a laminin receptor synthesized by Schwann cells and displayed apposed to the basal lamina. α6β4 integrin expression in Schwann cells is induced by axons at the onset of myelination, and rises in adulthood. The β4 chain has a uniquely long cytoplasmic domain that interacts with intermediate filaments such as dystonin, important in peripheral myelination. Furthermore, α6β4 integrin binds peripheral myelin protein 22, whose alteration causes the most common demyelinating hereditary neuropathy. All these data suggest a role for α6β4 integrin in peripheral nerve myelination. Here we show that ablating α6β4 integrin specifically in Schwann cells of transgenic mice does not affect peripheral nerve development, myelin formation, maturation, or regeneration. However, consistent with maximal expression in adult nerves, α6β4 integrin-null myelin is more prone to abnormal folding with aging. When the laminin receptor dystroglycan is also ablated, major folding abnormalities occur, associated with acute demyelination in some peripheral nervous system districts. These data indicate that, similar to its role in skin, α6β4 integrin confers stability to myelin in peripheral nerves. Society for Neuroscience 2008-06-25 /pmc/articles/PMC2597422/ /pubmed/18579745 http://dx.doi.org/10.1523/JNEUROSCI.0326-08.2008 Text en Copyright © 2008 Society for Neuroscience 0270-6474/08/286714-06$15.00/0
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Brief Communications
spellingShingle Brief Communications
Nodari, Alessandro
Previtali, Stefano C.
Dati, Gabriele
Occhi, Simona
Court, Felipe A.
Colombelli, Cristina
Zambroni, Desirée
Dina, Giorgia
Del Carro, Ubaldo
Campbell, Kevin P.
Quattrini, Angelo
Wrabetz, Lawrence
Feltri, M. Laura
α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath
description Schwann cells integrate signals deriving from the axon and the basal lamina to myelinate peripheral nerves. Integrin α6β4 is a laminin receptor synthesized by Schwann cells and displayed apposed to the basal lamina. α6β4 integrin expression in Schwann cells is induced by axons at the onset of myelination, and rises in adulthood. The β4 chain has a uniquely long cytoplasmic domain that interacts with intermediate filaments such as dystonin, important in peripheral myelination. Furthermore, α6β4 integrin binds peripheral myelin protein 22, whose alteration causes the most common demyelinating hereditary neuropathy. All these data suggest a role for α6β4 integrin in peripheral nerve myelination. Here we show that ablating α6β4 integrin specifically in Schwann cells of transgenic mice does not affect peripheral nerve development, myelin formation, maturation, or regeneration. However, consistent with maximal expression in adult nerves, α6β4 integrin-null myelin is more prone to abnormal folding with aging. When the laminin receptor dystroglycan is also ablated, major folding abnormalities occur, associated with acute demyelination in some peripheral nervous system districts. These data indicate that, similar to its role in skin, α6β4 integrin confers stability to myelin in peripheral nerves.
author Nodari, Alessandro
Previtali, Stefano C.
Dati, Gabriele
Occhi, Simona
Court, Felipe A.
Colombelli, Cristina
Zambroni, Desirée
Dina, Giorgia
Del Carro, Ubaldo
Campbell, Kevin P.
Quattrini, Angelo
Wrabetz, Lawrence
Feltri, M. Laura
author_facet Nodari, Alessandro
Previtali, Stefano C.
Dati, Gabriele
Occhi, Simona
Court, Felipe A.
Colombelli, Cristina
Zambroni, Desirée
Dina, Giorgia
Del Carro, Ubaldo
Campbell, Kevin P.
Quattrini, Angelo
Wrabetz, Lawrence
Feltri, M. Laura
author_sort Nodari, Alessandro
title α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath
title_short α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath
title_full α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath
title_fullStr α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath
title_full_unstemmed α6β4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath
title_sort α6β4 integrin and dystroglycan cooperate to stabilize the myelin sheath
publisher Society for Neuroscience
publisher_facet Society for Neuroscience
publishDate 2008
url https://ncbi.nlm.nih.gov/pmc/articles/PMC2597422/
https://ncbi.nlm.nih.gov/pubmed/18579745
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1523/JNEUROSCI.0326-08.2008
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