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. 2020 Aug 20;20:784. doi: 10.1186/s12885-020-07273-7

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 5 — ADM induced phosphorylation of HSL. a-b, ADM increased phosphorylation of HSL. Protein expression and phosphorylation were measured in hMADS-adipocytes (panel a) or breast adipocytes (panel b) grown in the differentiation medium. They were stimulated with 100 nM ADM for the indicated time. Expressions of pHSL (upper panel) and Tubulin-βI (lower panel) used as a loading control were analyzed by Western blot using specific antibodies. A positive control condition with cells stimulated for 4 h with forskolin is shown. Representative Western blots are shown. Full-length blots are presented in Supplementary Figure 9. c-d, Quantification of the signals. Expression and phosphorylation of the proteins were quantified using the Quantity One Program and compared to the expression of Tubulin-βI. The means ± SEM were calculated from four independent experiments. (*p < 0.05)