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. 2021 May 31;11:11376. doi: 10.1038/s41598-021-89765-5

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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 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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High glucose exposure activated c-Met and downstream signaling via promoting ligand-independent homodimerization. (a) Immunoblotting of time-dependent c-Met protein expression and activation phosphorylations (Y1234/Y1235) in response to high glucose treatment in HuH-7, HepG2, SNU-449, and SK-HEP-1 cells. Immunofluorescence imaging of Alexa-594-labeled c-Met protein and Alexa-488 labeled c-Met activation phosphorylations (Y1234/Y1235) in response to no- and high-glucose (25 mM) conditions in (b) HuH-7 and (c) SNU-499 cells. Cell nuclei were counterstained with DAPI staining. Immunoblotting of time-dependent expressions of Erk1/2 activation phosphorylations (T202/Y204), Erk1/2 total protein and Egr-1 protein in response to high glucose stimulation in (d) HuH-7 and (e) SNU-449 cells. Calnexin (Canx) immunoblotting performed as an internal control. (f) Graphical presentation of HGF secretion analysis with ELISA. Conditioned media of HCC cells cultured in no- and high-glucose supplemented conditions were analyzed with sandwich ELISA. Crosslinking-immunoprecipitation assay for analyzing c-Met homodimerization under no- and high-glucose (25 mM) conditions in (g) HuH-7, (h) SNU-449, (i) HepG2 and (j) SK-HEP-1 cells. After starvation and indicated treatments for 16 h, proteins were crosslinked with Sulfo-EGS, c-Met was immunoprecipitated and immunoblotted with c-Met targeting primary antibody. Full length blots are presented in Supplementary. Column graph was generated using GraphPad Prism version 8.2.1 for MacOS, GraphPad Software, San Diego, California USA, https://www.graphpad.com.