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. 2018 Feb 27;8:3689. doi: 10.1038/s41598-018-21853-5

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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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Compression induces degradation of mitochondria by autophagy. (a) to (e) show the comparison of animals (WT, Bak^−/−, Bax^fl/flBak^−/−, and Bax^−/−Bak^−/− mice in this order) by Western blots for (a) amounts of p62 and LC3-II/I ratio (n = 6 mice/group), (b) Beclin-1, Bcl-2, phosphorylated Bcl-2 at Ser87, immunoprecipitated Bcl-2, and immunoprecipitated Beclin-1 proteins (n = 4 mice/group), (c) Parkin, Bnip3 and PGC-1α proteins (n = 6 mice/group), (d) mitochondrial Parkin and Bnip3, (e) mitochondrial complexes (n = 4 mice/group), including complexes I-V, and (f) AMPK and Akt protein phosphorylation status in control (“−” or clear bars) and compressed (“+” or shaded black bars) muscle tissues. Pairwise comparison was performed with Student’s t-test, *P < 0.05, **P < 0.01.