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. 2018 Sep 17;8:13932. doi: 10.1038/s41598-018-32163-1

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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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(A) Comparison of contraction displacement between myofiber sheets cultured in the fibrin-based gels with (w/ Mtr) and without Matrigel (w/o Mtr). (n = 5) (**P < 0.01) (B,C) Laminin structure shown in the gel containing Matrigel (w/ Mtr). Myofibers are aligned (B) or randomly oriented in the gel (C). (D) No laminin formation observed in the gel without Matrigel (w/o Mtr). The aligned cells produced no laminin structure in the gel. (E,F) Formation of anisotropic and isotropic structures of type IV collagen in the Matrigel-containing gels with (E) aligned and (F) randomly oriented myofibers. (G) No formation of type IV collagen in the gel containing Matrigel, but without cells. (H) Laminin surrounding a myofiber in the myofiber sheet. (red: laminin, green: myosin heavy chain (MHC), blue: nuclei) (I) Type IV collagen surrounding a myofiber (blue: Type IV collagen, red: F-actin, green: myogenin (myoG)) Scale bars: 100 μm (B–G), 10 μm (H,I).