Fig. 1: NPs induce β-catenin stabilization and nuclear translocation and affect DA neuron markers and PD-related survival factors in SHSY5Y cells. | Cell Death Discovery

Fig. 1: NPs induce β-catenin stabilization and nuclear translocation and affect DA neuron markers and PD-related survival factors in SHSY5Y cells.

From: Natriuretic peptides are neuroprotective on in vitro models of PD and promote dopaminergic differentiation of hiPSCs-derived neurons via the Wnt/β-catenin signaling

Fig. 1

A Structure of the human natriuretic peptides. Pro-ANP and pro-BNP are proteolytically cleaved to the mature forms by the membrane-associated protease Corin [43], which extracellular region, that contains the structural domains essential the processing, includes the Wnt signaling receptors Fzd1 and Fzd2 [44]. Differently, the processing of pro-CNP to its mature form occurs through the action of the intracellular serine endoprotease furin [45], which generates the 53aa biologically active peptide (CNP-53), the main active form of CNP at the tissue level. CNP-53 is then further cleaved by an unknown protease to a shorter 22aa form (CNP-22), which is the dominant form in the systemic circulation [46]. The structure of the prepro-hormones for ANP, BNP, and CNP are reported on the left of each panel, while the final amino acid sequence and structure of the mature and biologically active peptides are shown on the right. The sites of cleavage operated by Corin (for ANP and BNP) and by Furin (for CNP) are also indicated. B Confocal microscopic images showing the intracellular distribution of β-catenin in control and NPs treated cells after 6 and 24 h of culture. Bars 25 µm. C WB analyses of total and phosphorylated β-catenin (pβ-cateninT41/S65), total and phosphorylated GSK-3β (pGSK-3βSer9), TH, Nurr-1, and DJ-1 levels in total cell lysates from NPs treated SHSY5Y cells, compared to the untreated control, after 6 and 24 h of treatment. D, E Densitometric analysis of total and phosphorylated β-catenin and GSK-3β (D), and of TH, Nurr-1, and DJ-1 (E) using the ImageJ processing program; values were normalized to β-actin, or vs. the total levels of each protein for the phosphorylated forms. Results are the mean ± SD from three independent experiments (n = 3). Significance vs. untreated relative control (one-way mANOVA + Tukey multiple comparison test): **p < 0.01, ***p < 0.001. Additional results from the one‐way ANOVA test used to analyze the differences between groups are reported in Supplementary Data.

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