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

. 2021 Sep 24;12:748574. doi: 10.3389/fphys.2021.748574

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

Copyright © 2021 Yamada, Yoshizaki, Ishikawa, Saito, Chiba, Fukumoto, Hino, Hoshikawa, Chiba, Nakamura, Iwamoto and Fukumoto.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

ERK1/2 phosphorylation is regulated by Cx43-mediated gap junction communication. (A) Phosphorylation of Smad2/3, ERK1/2, and p38 after stimulation by TGF-β1 with or without oleamide. n=5. (B) Phosphorylation of ERK1/2 after stimulation by TGF-β1 after transfection with expression vectors for Cx43 mutants (R76S or R202H). n=5. (C) Phosphorylation of ERK1/2 after stimulation by TGF-β1, BMP2, and BMP4 with or without oleamide. n=5. (D) Localization of Smad2/3 after stimulation by TGF-β1 with or without oleamide. n=5. Localization of ERK1/2 and phospho-ERK1/2 after stimulation by TGF-β1 with or without oleamide. n=5. (E) Immunoprecipitation of Runx2 in TGF-β1-stimulated dental epithelial cells. TGF-β1 induced Runx2 phosphorylation and caused the association of Runx2 with Smad2/3. Phosphorylation of serine residues of Runx2 and binding with Smad2/3 were inhibited by oleamide. n=5. (F) Phosphorylation of ERK1/2 in the presence of the IP3R agonist, adenophostin-A (Ad), or the IP3R antagonist, 2-APB, with or without TGF-β1 or oleamide.