VEGF-induced retinal angiogenic signaling is critically dependent on Ca²⁺ signaling by Ca²⁺/calmodulin-dependent protein kinase II

Invest Ophthalmol Vis Sci. 2011 May 11;52(6):3103-11. doi: 10.1167/iovs.10-6574.

Abstract

Purpose: The authors conducted an in vitro investigation of the role of Ca(2+)-dependent signaling in vascular endothelial growth factor (VEGF)-induced angiogenesis in the retina.

Methods: Bovine retinal endothelial cells (BRECs) were stimulated with VEGF in the presence or absence of 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid-acetoxymethyl ester (BAPTA-AM; intracellular Ca(2+) chelator), U73122 (phospholipase C (PLC) inhibitor), xestospongin C (Xe-C), and 2-aminoethoxydiphenyl borate (2APB) (inhibitors of inositol-1,4,5 triphosphate (IP(3)) signaling). Intracellular Ca(2+) concentration ([Ca(2+)](i)) was estimated using fura-2 Ca(2+) microfluorometry, Akt phosphorylation quantified by Western blot analysis, and angiogenic responses assessed using cell migration, proliferation, tubulogenesis, and sprout formation assays. The effects of the Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) inhibitor KN93 were also evaluated on VEGF-induced Akt signaling and angiogenic activity.

Results: Stimulation of BRECs with 25 ng/mL VEGF induced a biphasic increase in [Ca(2+)](i), with an initial transient peak followed by a sustained plateau phase. VEGF-induced [Ca(2+)](i) increases were almost completely abolished by pretreating the cells with BAPTA-AM, U73122, Xe-C, or 2APB. These agents also inhibited VEGF-induced phosphorylation of Akt, cell migration, proliferation, tubulogenesis, and sprouting angiogenesis. KN93 was similarly effective at blocking the VEGF-induced activation of Akt and angiogenic responses.

Conclusions: VEGF increases [Ca(2+)](i) in BRECs through activation of the PLC-IP(3) signal transduction pathway. VEGF-induced phosphorylation of the proangiogenic protein Akt is critically dependent on this increase in [Ca(2+)](i) and the subsequent activation of CaMKII. Pharmacologic inhibition of Ca(2+)-mediated signaling in retinal endothelial cells blocks VEGF-induced angiogenic responses. These results suggest that the PLC/IP(3)/Ca(2+)/CaMKII signaling pathway may be a rational target for the treatment of angiogenesis-related disorders of the eye.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Boron Compounds / pharmacology
  • Calcium / metabolism*
  • Calcium Signaling / physiology*
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / antagonists & inhibitors
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2 / metabolism*
  • Cattle
  • Cell Movement / physiology
  • Cell Proliferation
  • Egtazic Acid / analogs & derivatives
  • Egtazic Acid / pharmacology
  • Endothelium, Vascular / drug effects*
  • Endothelium, Vascular / metabolism
  • Enzyme Inhibitors / pharmacology
  • Enzyme-Linked Immunosorbent Assay
  • Estrenes / pharmacology
  • Inositol 1,4,5-Trisphosphate / antagonists & inhibitors
  • Inositol 1,4,5-Trisphosphate / metabolism
  • Macrocyclic Compounds / pharmacology
  • Neovascularization, Physiologic / drug effects
  • Neovascularization, Physiologic / physiology*
  • Oxazoles / pharmacology
  • Phosphorylation
  • Proto-Oncogene Proteins c-akt / antagonists & inhibitors
  • Proto-Oncogene Proteins c-akt / metabolism
  • Pyrrolidinones / pharmacology
  • Retinal Vessels / cytology
  • Type C Phospholipases / antagonists & inhibitors
  • Type C Phospholipases / metabolism
  • Vascular Endothelial Growth Factor A / pharmacology*

Substances

  • Boron Compounds
  • Enzyme Inhibitors
  • Estrenes
  • Macrocyclic Compounds
  • Oxazoles
  • Pyrrolidinones
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • xestospongin C
  • 1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione
  • 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester
  • Egtazic Acid
  • Inositol 1,4,5-Trisphosphate
  • 2-aminoethoxydiphenyl borate
  • Proto-Oncogene Proteins c-akt
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Type C Phospholipases
  • Calcium