Key result
Stimulation of gp130 with leukemia inhibitory factor upregulates Wnt5a through STAT3, promoting N-cadherin-mediated cell adhesion in cultured cardiomyocytes.
Signals through gp130 upregulate Wnt5a via STAT3, promoting N-cadherin-mediated cell adhesion in cardiomyocytes.
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Suggests a gp130-STAT3 adhesion mechanism in cardiomyocytes; leaves open in vivo relevance to cardiac disease.
Glycoprotein 130 (gp130), a common receptor of IL-6 family cytokines, plays critical roles in cardiac functions. Here, we demonstrate that the stimulation of gp130 with leukemia inhibitory factor (LIF) promoted cell adhesion in a cadherin-dependent manner in cultured cardiomyocytes. Wnt5a was upregulated by the stimulation of gp130 with IL-6 family cytokines, accompanied by N-cadherin protein upregulation. Wnt5a was not induced by LIF in cardiomyocytes expressing dominant-negative STAT3. Ablation of Wnt5a by antisense cDNA inhibited LIF-induced cell adhesion. Collectively, signals through gp130 upregulate Wnt5a through STAT3, promoting the N-cadherin-mediated cell adhesion.
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Fujio et al. (2004) studied Cultured cardiomyocytes. Stimulation of gp130 with leukemia inhibitory factor (LIF) was evaluated on Cell adhesion and Wnt5a/N-cadherin upregulation. Stimulation of gp130 with leukemia inhibitory factor upregulates Wnt5a through STAT3, promoting N-cadherin-mediated cell adhesion in cultured cardiomyocytes.
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