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Conditional disruption of beta 1 integrin in schwann cells impedes interactions with axons

Academic Article
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Overview

authors

  • Feltri, M. L.
  • Porta, D. G.
  • Previtali, S. C.
  • Nodari, A.
  • Migliavacca, B.
  • Cassetti, A.
  • Littlewood-Evans, A.
  • Reichardt, L. F.
  • Messing, A.
  • Quattrini, A.
  • Mueller, Ulrich
  • Wrabetz, L.

publication date

  • 2002

journal

  • Journal of Cell Biology  Journal

abstract

  • In dystrophic mice, a model of merosin-deficient congenital muscular dystrophy, laminin-2 mutations produce peripheral nerve dysmyelination and render Schwann cells unable to sort bundles of axons. The laminin receptor and the mechanism through which dysmyelination and impaired sorting occur are unknown. We describe mice in which Schwann cell-specific disruption of beta1 integrin, a component of laminin receptors, causes a severe neuropathy with impaired radial sorting of axons. beta 1-null Schwann cells populate nerves, proliferate, and survive normally, but do not extend or maintain normal processes around axons. Interestingly, some Schwann cells surpass this problem to form normal myelin, possibly due to the presence of other laminin receptors such as dystroglycan and alpha 6 beta 4 integrin. These data suggest that beta 1 integrin links laminin in the basal lamina to the cytoskeleton in order for Schwann cells to ensheath axons, and alteration of this linkage contributes to the peripheral neuropathy of congenital muscular dystrophy.

subject areas

  • Animals
  • Antigens, CD29
  • Axons
  • Bromodeoxyuridine
  • Cell Adhesion
  • Cell Division
  • Cell Size
  • Cell Survival
  • DNA
  • Gene Deletion
  • Gene Expression Regulation
  • In Situ Nick-End Labeling
  • Mice
  • Mice, Knockout
  • Mice, Neurologic Mutants
  • Muscular Dystrophy, Animal
  • Myelin Sheath
  • Organ Specificity
  • Receptors, Laminin
  • Schwann Cells
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Research

keywords

  • Cre/loxP
  • axo-glial interactions
  • congenital muscular dystrophy
  • laminin
  • peripheral nerve
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Identity

PubMed Central ID

  • PMC2173589

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200109021

PubMed ID

  • 11777940
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Additional Document Info

start page

  • 199

end page

  • 209

volume

  • 156

issue

  • 1

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