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. 2022 Jan 10;13(1):41. doi: 10.1038/s41419-021-04485-y

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© The Author(s) 2021

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — A Activation of NK1R by hHK-1 transactivated phosphorylation of EGFR (pY1068). Cells were treated by 1 μM hHK-1 in indicated time after starving 2 h. B Aprepitant inhibited the phosphorylation of EGFR stimulated by 1 μM hHK-1 or by 0.1 μg EGF treatment. Total EGFR protein was used as loading control. C Aprepitant inhibited ERK1/2 and AKT phosphorylation induced by EGF. Total ERK and Akt protein were used as loading control. D Total or phosphorylated EGFR and NK1R expression in cells transfected with lenti-CRISPR sgRNA target to EGFR by western blot. E Cell proliferation in EGFR knockout cells with or without hHK-1/EGF treatment for 72 h (Celltiter-Glo assay). F Transwell assay for cell migration in EGFR konckout cells with or without hHK-1/EGF treatment. Data were shown as mean ± SD from three independent experiments. *P < 0.05, **P < 0.01, ***P < 0.001.