Conditional disruption of {beta}1 integrin in Schwann cells impedes interactions with axons

doi:10.1083/jcb.200109021

Published online 3 January 2002. doi:10.1083/jcb.200109021

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© The Rockefeller University Press, 0021-9525/2002/1/199 $5.00
The Journal of Cell Biology, Volume 156, Number 1, January 7, 2002 199-210

Article

Conditional disruption of ß1 integrin in Schwann cells impedes interactions with axons

M. Laura Feltri¹, Diana Graus Porta², Stefano C. Previtali¹, Alessandro Nodari¹, Barbara Migliavacca¹, Arianna Cassetti¹, Amanda Littlewood-Evans², Louis F. Reichardt³, Albee Messing⁴, Angelo Quattrini¹, Ulrich Mueller² and Lawrence Wrabetz¹

¹ Departments of Biological and Technological Research and Neuroscience, San Raffaele Scientific Institute, 20132 Milan, Italy
² Friedrich Miescher Institute, CH 4058 Basel, Switzerland
³ Department of Physiology, Howard Hughes Medical Institute, University of California, San Francisco, CA 94143
⁴ Waisman Center and School of Veterinary Medicine, University of Wisconsin, Madison, WI 53705

Address correspondence to Maria Laura Feltri, Department of Biological and Technological Research, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italy. Tel.: (39) 02-26434782 Fax: (39) 02-26434767. E-mail: feltri.laura{at}hsr.it

In dystrophic mice, a model of merosin-deficient congenitalmuscular dystrophy, laminin-2 mutations produce peripheral nervedysmyelination and render Schwann cells unable to sort bundlesof axons. The laminin receptor and the mechanism through whichdysmyelination and impaired sorting occur are unknown. We describemice in which Schwann cell–specific disruption of ß1integrin, a component of laminin receptors, causes a severeneuropathy with impaired radial sorting of axons. ß1-nullSchwann 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 formnormal myelin, possibly due to the presence of other lamininreceptors such as dystroglycan and ${alpha}$ 6ß4 integrin. Thesedata suggest that ß1 integrin links laminin in thebasal lamina to the cytoskeleton in order for Schwann cellsto ensheath axons, and alteration of this linkage contributesto the peripheral neuropathy of congenital muscular dystrophy.

Key Words: axo–glial interactions; Cre/loxP; congenital muscular dystrophy; laminin; peripheral nerve

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