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

. 1997 May 5;137(3):671–683. doi: 10.1083/jcb.137.3.671

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

The NH₂-terminal, laminin-binding domain of agrin causes AChR clusters to be small. (a) Fluorescence micrographs of cultured chick myotubes labeled with rhodamine–α-bungarotoxin. Myotubes were grown for 12 h in the presence of conditioned medium of transiently transfected COS cells containing either 100 pM cAgrin_7A4B8 or cΔN15Agrin_A4B8. AChR clusters induced by cAgrin_7A4B8 are considerably smaller than those induced by cΔN15Agrin_A4B8. In the presence of cN25₇Fc, the size of cAgrin_7A4B8-induced AChR clusters increases. (b) Quantification of the effect on the size of the AChR aggregates. The presence of 500 nM cN25₇Fc (+ cN25₇Fc) increases the size of the AChR clusters induced by cAgrin_7A4B8 twofold and makes them indistinguishable from AChR clusters induced by cΔN15Agrin_A4B8. In contrast, addition of 500 nM cN25₇Fc does not alter the size of cΔN15Agrin_A4B8-induced AChR aggregates. The result (mean ± SEM) of one representative experiment is shown where the size of AChR clusters in 20 myotube segments was determined. Bar, 50 μm.

The NH₂-terminal, laminin-binding domain of agrin causes AChR clusters to be small. (a) Fluorescence micrographs of cultured chick myotubes labeled with rhodamine–α-bungarotoxin. Myotubes were grown for 12 h in the presence of conditioned medium of transiently transfected COS cells containing either 100 pM cAgrin_7A4B8 or cΔN15Agrin_A4B8. AChR clusters induced by cAgrin_7A4B8 are considerably smaller than those induced by cΔN15Agrin_A4B8. In the presence of cN25₇Fc, the size of cAgrin_7A4B8-induced AChR clusters increases. (b) Quantification of the effect on the size of the AChR aggregates. The presence of 500 nM cN25₇Fc (+ cN25₇Fc) increases the size of the AChR clusters induced by cAgrin_7A4B8 twofold and makes them indistinguishable from AChR clusters induced by cΔN15Agrin_A4B8. In contrast, addition of 500 nM cN25₇Fc does not alter the size of cΔN15Agrin_A4B8-induced AChR aggregates. The result (mean ± SEM) of one representative experiment is shown where the size of AChR clusters in 20 myotube segments was determined. Bar, 50 μm.