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. 2019 Sep 2;9:12628. doi: 10.1038/s41598-019-48992-7

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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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HSP60 knockdown disrupts mitochondria integrity and decreases protein synthesis. (A) Numbers of upregulated and downregulated proteins in mostly changed (with the largest absolute values of z-score and p-values < 0.05) canonical pathways according to ingenuity pathway analysis. Among these pathways, oxidative phosphorylation was the most inhibited (z-score = −3.5, p-value < 0.05) in HSP60-KD A2780 cells compared with control cells. (B) Comparative analysis of the z-scores of mostly changed pathways in clinical ovarian samples and HSP60-KD A2780 cells. (C) Fourteen and 11 subunits of mitochondrial complex I were downregulated in HSP60-KD1 and -KD2 A2780 cells, respectively. (D) Seventeen and 38 mitochondrial ribosomal proteins were downregulated in HSP60-KD1 and -KD2 A2780 cells, respectively. Data were analyzed by the Student’s t-test. p < 0.05 was considered as statistically significant. Error bars represent ± SEM.