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Deficiency of endothelial sirtuin1 in mice stimulates skeletal muscle insulin sensitivity by modifying the secretome. | LitMetric

AI Article Synopsis

  • Downregulation of endothelial Sirtuin1 (Sirt1) leads to vascular dysfunction, but its deficiency in endothelial cells surprisingly enhances insulin sensitivity in skeletal muscle.
  • Male mice lacking endothelial Sirt1 show increased glucose utilization, better insulin sensitivity, and improved Akt signaling, compared to normal mice.
  • The improved insulin sensitivity in these mice can be transferred to normal mice through the bloodstream, with the mechanism involving increased secretion of thymosin beta-4 (Tβ4) from Sirt1-deficient endothelial cells that boosts insulin signaling in muscle cells.

Article Abstract

Downregulation of endothelial Sirtuin1 (Sirt1) in insulin resistant states contributes to vascular dysfunction. Furthermore, Sirt1 deficiency in skeletal myocytes promotes insulin resistance. Here, we show that deletion of endothelial Sirt1, while impairing endothelial function, paradoxically improves skeletal muscle insulin sensitivity. Compared to wild-type mice, male mice lacking endothelial Sirt1 (E-Sirt1-KO) preferentially utilize glucose over fat, and have higher insulin sensitivity, glucose uptake, and Akt signaling in fast-twitch skeletal muscle. Enhanced insulin sensitivity of E-Sirt1-KO mice is transferrable to wild-type mice via the systemic circulation. Endothelial Sirt1 deficiency, by inhibiting autophagy and activating nuclear factor-kappa B signaling, augments expression and secretion of thymosin beta-4 (Tβ4) that promotes insulin signaling in skeletal myotubes. Thus, unlike in skeletal myocytes, Sirt1 deficiency in the endothelium promotes glucose homeostasis by stimulating skeletal muscle insulin sensitivity through a blood-borne mechanism, and augmented secretion of Tβ4 by Sirt1-deficient endothelial cells boosts insulin signaling in skeletal muscle cells.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10495425PMC
http://dx.doi.org/10.1038/s41467-023-41351-1DOI Listing

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