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Icariside II (ICA II) protects against palmitic acid-induced endothelial dysfunction by binding to serine-arginine protein kinase 1 (SRPK1). This interaction restores nitric oxide (NO) production and cell viability via the SRPK1-Akt-eNOS pathway.

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Area of Science:

  • Vascular Biology and Endothelial Function
  • Molecular Signaling Pathways
  • Pharmacology and Natural Products

Background:

  • Endothelial dysfunction, characterized by reduced nitric oxide (NO) production and sensitivity, is central to vascular diseases.
  • Saturated free fatty acids, like palmitic acid (PA), induce endothelial dysfunction.
  • Serine-arginine protein kinase 1 (SRPK1) regulates alternative splicing and its role in endothelial cells is unclear; Icariside II (ICA II) may offer protection.

Purpose of the Study:

  • To elucidate the role of SRPK1 in endothelial cell biology.
  • To investigate the protective mechanism of ICA II against PA-induced endothelial dysfunction.

Main Methods:

  • Human umbilical vein endothelial cells (HUVECs) were treated with PA to induce dysfunction.
  • Western Blotting assessed protein expression and phosphorylation in the SRPK1-Akt-eNOS pathway.
  • Cell viability was measured using CCK-8 and Ki-67 assays; NO production was detected by DAF-FM DA; protein interactions were confirmed via pull-down assays.

Main Results:

  • PA treatment downregulated eNOS, Akt, and SRPK1 expression in HUVECs.
  • SRPK1 inhibition (SPHINX31) or knockdown (shRNA) reduced cell viability and downstream signaling proteins.
  • ICA II directly bound to SRPK1 and attenuated PA-induced endothelial dysfunction, restoring cell viability through the SRPK1-Akt-eNOS pathway.

Conclusions:

  • ICA II directly interacts with SRPK1.
  • ICA II mitigates PA-induced endothelial dysfunction in HUVECs.
  • The protective effects of ICA II are mediated via the SRPK1-Akt-eNOS signaling pathway.