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      Signals through gp130 upregulate Wnt5a and contribute to cell adhesion in cardiac myocytes.

      Febs Letters
      Animals, Antigens, CD, metabolism, Cadherins, genetics, Cell Adhesion, drug effects, Cell Aggregation, Cell Line, Cells, Cultured, Cytokine Receptor gp130, Cytokines, pharmacology, DNA-Binding Proteins, Humans, Interleukin-6, Leukemia Inhibitory Factor, Membrane Glycoproteins, Myocytes, Cardiac, cytology, Proteins, RNA, Messenger, Rats, STAT3 Transcription Factor, Signal Transduction, Trans-Activators, Up-Regulation, Wnt Proteins

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          Abstract

          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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