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. 2019 Sep 11;9:13090. doi: 10.1038/s41598-019-49482-6

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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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Downregulation of PrP^C aggregates β1-integrin and upregulates laminin and its receptor. (a) Silencing of PrP^C in human TM cells followed by immunostaining with antibody specific for activated β1-integrin shows clustering of activated β1-integrin on the plasma membrane in the absence of PrP^C (arrowheads) (panels 1–4). Cells transfected with PrP-siRNA and reacted with mouse IgG and respective secondary antibody do not show any reaction (panel 5). Scale bar: 25 µm. (b) Probing of TM cell lysates for PrP^C shows the expected glycoforms in control cells transfected with scrambled siRNA, and minimal reaction in cells exposed to PrP-siRNA (lanes 1 & 2). Probing for laminin and laminin receptor (LR) shows significant upregulation in the absence of PrP^C relative to control (lanes 1 & 2). (c) Quantification by densitometry after normalization with β-actin shows 2-fold upregulation of laminin and LR due to downregulation of PrP^C. Values are mean ± SEM of the indicated n. *p < 0.05. Full-length blots are included in the Supplementary Fig. S2.