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. 2019 Aug 14;9:11861. doi: 10.1038/s41598-019-47891-1

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© The Author(s) 2019

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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ER-INP binds to PHD2, inhibits hydroxylation of HIF-1α and increases HIF-1α accumulation. (A) Co-immunoprecipitation assay. HEK293 cells were transfected with control vector or intrabody ER-INP for 48 hours and subsequently lysed. Co-immunoprecipitation and western blot assays were performed on the cell lysis. ER-INP recognized and bound to PHD2 in HEK293 cells (n = 3). (B) Western blot analysis to measure the effect of ER-INP on HIF-1α and its hydroxylation level in transfected HEK293 and RAW264.7 cells pre-treated with MG132 (upper panel) and the protein ratio to β-actin loading control by ImageJ densitometry analysis (lower panel; n = 3). (C) Immunofluorescence assay. Expression of ER-INP increases HIF-1α accumulation in RAW264.7 cells. Cells were stained with anti-HIF-1α antibody and DAPI and then visualized and photographed under immunofluorescence microscopy (left), and mean fluorescence intensity of HIF-1α versus the mean fluorescence intensity of nuclear DAPI staining is displayed (right). Data represent the mean ± SD of 3 independent slides.