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. 2022 Oct 11;27(20):6787. doi: 10.3390/molecules27206787

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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IBC induced necroptosis in human triple-negative breast MDA-MB-231 cancer cells. (A) Cell viability following treatment with IBC (40 µM) for 24 h alone or with the necroptosis inhibitor Nec-1 (20 µM) pre-treatment as measured by the MTT assay. (B) Annexin V-FITC/PI analysis following treatment with IBC with or without pre-treatment with Nec-1. (C) Western blotting analysis of necroptosis-related proteins (RIP1, RIP3, p-RIP3, and MLKL). (D) The cells were treated with IBC and incubated overnight with the primary antibodies at 4 °C. The localization of RIP3 and MLKL was assessed by immunofluorescence staining. Nuclei were stained with DAPI. * p < 0.05 compared between the groups of IBC and IBC with Nec-1.

IBC induced necroptosis in human triple-negative breast MDA-MB-231 cancer cells. (A) Cell viability following treatment with IBC (40 µM) for 24 h alone or with the necroptosis inhibitor Nec-1 (20 µM) pre-treatment as measured by the MTT assay. (B) Annexin V-FITC/PI analysis following treatment with IBC with or without pre-treatment with Nec-1. (C) Western blotting analysis of necroptosis-related proteins (RIP1, RIP3, p-RIP3, and MLKL). (D) The cells were treated with IBC and incubated overnight with the primary antibodies at 4 °C. The localization of RIP3 and MLKL was assessed by immunofluorescence staining. Nuclei were stained with DAPI. * p < 0.05 compared between the groups of IBC and IBC with Nec-1.