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

. 2011 May 16;286(27):24374–24384. doi: 10.1074/jbc.M111.230797

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

© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

PMC Copyright notice

FIGURE 10. — Cross-linking of residues 81 and 412 traps rASIC1a in the desensitized state. A, reducing and oxidizing conditions had no effect on rASIC1a-wt currents. B, left panel, rASIC1a-A81C/V412C current amplitude gradually decreases with repeated stimulation by ligand (pH 6.4). Switching the pH to 7.8 has no effect on current amplitude, whereas reducing conditions dramatically increased current amplitude. Right panel, oxidizing conditions reduced current amplitude of rASIC1a-A81C/V412C. C, quantification of tachyphylaxis for rASIC1a-wt and -A81C/V412C (2C). The channels were repeatedly activated, and current amplitudes were normalized to the first amplitude. Repeated activation reduced rASIC1a-A81C/V412C currents significantly more strongly than wt currents. Absolute values of the initial amplitudes were 14.3 ± 2.5 μA (wt; n = 6) and 1.0 ± 0.2 μA (A81C/V412C; n = 6), respectively. The lines represent fits to a mono-exponential function. ***, p < 0.001.