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. 2020 Oct 20;147(2):361–371. doi: 10.1007/s00432-020-03428-y

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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/.

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Fig. 5 — Protein levels of ITGB3 in exosomes. a Levels of ITGB3 in exosomes isolated from plasma of healthy rats (exo 1) and from plasma of rats with breast cancer skeletal metastasis (exo 2 and exo 3). The latter exosomes show higher levels of this protein. b ITGB3 in MDA-MB-231 breast cancer cells incubated with exo 1 or exo 2 for 72 h. The levels of this protein were increased after incubating the cells with exosomes isolated from plasma of rats with breast cancer lesions (exo 2). c ITGB3 levels in exosomes isolated in vitro from: (1) parent cell clone, cultivated in medium with doxycycline (+ dox control), (2) I5 cells cultivated in medium with dox (+ dox, specific control), (3) parent cell clone, cultivated in medium without dox (-dox control), (4) I5 cells cultivated in medium without dox (-dox, anti-ITGB3 effects). ITGB3 decreased twofold in exosomes derived from cells with conditional integrin β3 knockdown