Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 1999 May 3;145(3):619–631. doi: 10.1083/jcb.145.3.619

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Polymer-defective laminin from dy^2J/dy^2J mice does not form surface networks and does not induce sarcolemmal reorganization. (A) The top frame shows an SDS-PAGE of laminin from skeletal muscle of +/+ and dy^2J/dy^2J mice. Proteins extracted from mouse skeletal muscle were separated by SDS-PAGE under reducing conditions and visualized with Coomassie blue. The arrow depicts dy^2J laminin α2 subunit, roughly 25 kD smaller than native α2. Bottom frame: dy^2J–α2-laminin binds to the myotube surface but fails to form networks. On myotubes incubated for 4 h, α2-laminin from wild-type mice formed networks (+/+), whereas dy^2J–α2-laminin remained in a punctate, diffusely distributed pattern (dy^2J/dy^2J). Bar, 5 μm; insets, three times the magnification. (B) dy^2J–α2-laminin does not induce reorganization of sarcolemmal proteins into a cortical network. Myotubes were incubated for 4 h with laminin from either wild-type (wt-lm2) or dy^2J/dy^2J mice (dy2j-lm2) and costained to visualize laminin α2 subunit and b1 integrin subunit (β1), dystroglycan (DG), or vinculin (vin). α2-Laminin induces a reorganization of integrin, dystroglycan, and vinculin, whereas dy^2J–α2-laminin does not. Bar, 10 μm.

Polymer-defective laminin from dy^2J/dy^2J mice does not form surface networks and does not induce sarcolemmal reorganization. (A) The top frame shows an SDS-PAGE of laminin from skeletal muscle of +/+ and dy^2J/dy^2J mice. Proteins extracted from mouse skeletal muscle were separated by SDS-PAGE under reducing conditions and visualized with Coomassie blue. The arrow depicts dy^2J laminin α2 subunit, roughly 25 kD smaller than native α2. Bottom frame: dy^2J–α2-laminin binds to the myotube surface but fails to form networks. On myotubes incubated for 4 h, α2-laminin from wild-type mice formed networks (+/+), whereas dy^2J–α2-laminin remained in a punctate, diffusely distributed pattern (dy^2J/dy^2J). Bar, 5 μm; insets, three times the magnification. (B) dy^2J–α2-laminin does not induce reorganization of sarcolemmal proteins into a cortical network. Myotubes were incubated for 4 h with laminin from either wild-type (wt-lm2) or dy^2J/dy^2J mice (dy2j-lm2) and costained to visualize laminin α2 subunit and b1 integrin subunit (β1), dystroglycan (DG), or vinculin (vin). α2-Laminin induces a reorganization of integrin, dystroglycan, and vinculin, whereas dy^2J–α2-laminin does not. Bar, 10 μm.