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. 2020 Nov 9;10:19303. doi: 10.1038/s41598-020-75774-3

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Diffuse high-molecular weight signals in PDGFRα and PDGFRβ immunoblots correlate with receptor phosphorylation and downstream pathway activation. M28-D5 fibroblasts were stimulated by 20 ng/ml of PDGF-AA, AB, or BB ligands for 6 m after serum depletion in 0.2% FBS media for 12 h. Immunoblots show (a) robust PDGFRα phosphorylation in the total PDGFRα immunoblot (red arrowheads) in the high-molecular weight (> 250 kDa) regions which is well correlated with (b) the robust increase in Tyr754 phosphorylation of PDGFRα. Likewise, the high-molecular weight signals in (c) total PDGFRβ immunoblot (blue arrowheads) are well correlated with (d) the Tyr1009 phosphorylation of PDGFRβ. (e–j) Phosphorylation of several key signaling molecules downstream of PDGFR was confirmed by phospho-specific antibodies to detect canonical phosphorylation/activation sites. In response to all AA, AB, and BB PDGF ligands, Src, Akt, and ERK were robustly phosphorylated while total levels of these proteins remained constant. (k) Alpha tubulin was used as a loading control.