----------------- INFORMACIÓN GENERAL ------------------- 1. Título del dataset: Soluble sST2 isoform is related to cardiotoxicity 2. Autoría: Nombre:Antonio Manuel Lax Pérez Institución: Universidad de Murcia Correo electrónico: alax@um.es ORCID: 0000-0001-5452-8781 Nombre: Maria del Carmen Asensio López Institución: Centro Nacional de investigaciones Cardiovasculares (CNIC) Correo electrónico: mal24027@um.es ORCID: 0000-0002-8043-6925 3. 4. Fecha de depósito de los datos: 19/07/2023 5. Idioma del conjunto de datos: Inglés ------------------------ INFORMACIÓN METODOLÓGICA ------------------------ ------------------------ ESCTRUCTURA DE LOS ARCHIVOS --------------------------- 1. Nombres de archivos : Soluble sST2 isoform is related to ACT 2. Formato de los archivos: pdf ------------------------ MÁS INFORMACIÓN ------------------------ Soluble sST2 isoform is related to ACT. Led by the PL team, preliminary data have identified for first time a relationship between higher sST2 levels and YY1 with CIC, using an in vitro translational model. (a-c; experimental assays in hiPsCMs). The combination of siYY1+Dox treatment was able to prevent Dox-induced YY1 and sST2 up-regulation (panels a-b), leading to decreased c-TnT levels and improved cell viability (panel c). Further, exogenous administration of sST2 combined with YY1 silencing (sST2/Fc+siYY1) restored the parameters associated with cardiac damage demonstrating a causal relationship between sST2 and YY1 in CIC (in term of cTnT and cell viability; panel c). (d, e; experimental assays in human BCCs). The human breast cancer (HER+) isolated form cancer patients by sorting (CD44+), over-expressed YY1 and sST2, which was prevented by treatment with the siYY1 sequence. (f, g; Co-culture assay). The sST2 secreted by human BCCs has a toxic effect on human myocytes, in term of less contractility (panel f). Here, when the expression of sST2 in hBCCs was blocked using our siYY1 sequence, the contractility of the hiPsCMs was increased. As described above, exogenous administration of sST2 combined with YY1 silencing (sST2/Fc+siYY1) was able to prevent the cardioprotective role of siYY1 on human myocytes´s contractility. Quantifications are derived from n = 6 clones/group. All quantitative data are presented as mean ± SEM. *p<0.001, relative to siCtrl+Dox group; & p<0.001, relative to siYY1+Dox treated group, determined by twoway ANOVA followed by Bonferroni post hoc test. Abbreviations: c-TnT, cardiac troponin T; siCtrl, si-control; Dox, doxorubicin; sST2/Fc: sST2-Fc fusion protein