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. 2018 Sep 17;9(10):938. doi: 10.1038/s41419-018-0970-6

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© The Author(s) 2018

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. 2 — a A protein corresponding to 150 kDa (arrow) along with HSP60 (arrowhead) existed in HSP60 immunoprecipitates. Images of cell lysate indicate equal load of specimens for electrophoresis. b Tandem mass spectrum and c attributes of peptide homologous to RPTOR. d Weak HSP60 (green) and RPTOR (red) immunofluorescence in glucocorticoid-stressed osteoblasts. Scale bars, 16 μm. e Increasing HSP60 attenuated the glucocorticoid-induced loss of RPTOR mRNA expression and protein levels. f Images of HSP60 and RPTOR-ligated complexes. Forced HSP60 expression increased HSP60 and RPTOR ligation reaction in osteoblasts, whereas HSP60 knockdown reduced the reaction. Scale bar, 16 μm. Experiments results are expressed as mean ± standard error. Asterisks (*) resemble a significant difference (P < 0.05) vs. scramble group, and hashtag (#) indicates a distinguishable difference (P < 0.05) vs. glucocorticoid-treated group