Alpha-lipoic acid inhibits proliferation and migration of human vascular endothelial cells through downregulating HSPA12B/VEGF signaling axis

Cell Stress Chaperones. 2020 May;25(3):455-466. doi: 10.1007/s12192-020-01086-0. Epub 2020 Mar 27.

Abstract

Endothelial cells play essential roles in angiogenesis. Heat shock protein A12B (HSPA12B), a novel member of the multigene Hsp70 family, expresses specifically in endothelial cells. Alpha-lipoic acid (LA) has been used for the treatment of human diabetic complications for more than 20 years. However, little is known whether LA impacts endothelial proliferation and migration. To address these questions, primary human umbilical vein endothelial cells (HUVECs) were isolated and treated with LA. We found that LA reduced viable HUVECs but not caused LDH leakage and nuclear condensation, suggesting an inhibitory effect of LA on HUVEC proliferation. We also noticed that LA impeded wound closure of HUVEC monolayers. The expressions of C-Myc, VEGF, and eNOS and phosphorylation of focal adhesion kinase were reduced by LA. Moreover, LA decreased the expression of heat shock protein A12B (HSPA12B). Notably, overexpression of HSPA12B in endothelial cells prevented the LA-induced loss of VEGF. More importantly, HSPA12B overexpression attenuated the LA-induced inhibition of endothelial proliferation and migration. Collectively, the results demonstrated that LA inhibited proliferative and migratory abilities in human vascular endothelial cells through the downregulation of the HSPA12B/VEGF signaling axis. The data suggest that besides the treatment in diabetic complications, LA might represent a viable therapeutic potential for human diseases that involve high angiogenic activities such as cancers.

Keywords: Alpha-lipoic acid; Endothelial cells; HSPA12B; Migration; Proliferation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Movement / drug effects
  • Cell Proliferation / drug effects
  • Cells, Cultured
  • Down-Regulation
  • Focal Adhesion Kinase 1 / metabolism
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / metabolism
  • Human Umbilical Vein Endothelial Cells / cytology
  • Human Umbilical Vein Endothelial Cells / drug effects
  • Human Umbilical Vein Endothelial Cells / physiology
  • Humans
  • Nitric Oxide Synthase Type III / metabolism
  • Signal Transduction / drug effects
  • Thioctic Acid / pharmacology*
  • Vascular Endothelial Growth Factor A / metabolism*

Substances

  • HSP70 Heat-Shock Proteins
  • HSPA12B protein, human
  • Heat-Shock Proteins
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Thioctic Acid
  • NOS3 protein, human
  • Nitric Oxide Synthase Type III
  • Focal Adhesion Kinase 1
  • PTK2 protein, human