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. 2023 Feb 10;43:11. doi: 10.1186/s41232-023-00258-6

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© The Author(s) 2023

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. 1 — Construction of the Wnt3a-diCARs and their signal transduction property in mouse ES cells. A A schematic illustration of wild-type and the chimeric antigen receptors for Wnt3a (Wnt3a-diCAR). Wnt3a-diCAR consists of the single-chain Fv region (scFv) of an anti-fluorescein (FL) antibody and the transmembrane/cytoplasmic domains of LRP6 and Frizzled8 (FZD8). B Molecular structures of wild-type and chimeric LRP6 and FZD8 proteins. An immunoglobulin heavy chain secretion signal sequence (Sig) is placed upstream of each chimera for cell surface expression. The EGF repeats 1–4 (E1–E4), LDLR repeats 1–3 (L1–3), cysteine-rich domain (CRD), and transmembrane domain (TM) are indicated. C TCF/β-catenin-dependent transcriptional activities were measured by luciferase reporter assays in mouse ES cells transiently transfected with various combinations of chimeric LRP6 and FZD8. The signal was normalized to the vehicle-treated mock-transfected cells, which was set to 1. The data represent the mean of duplicates and standard deviation from one representative experiment