Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated?

Trends Biochem Sci. 2001 Sep;26(9):519-21. doi: 10.1016/s0968-0004(01)01937-5.


Regulation of the endothelial isoform of nitric oxide synthase (eNOS) appears to be much more complex in comparison to that of other NOS isoforms. A recent paper has expanded the regulation of the enzyme to the realm of sphingolipid signaling, specifically implicating that sphingosine 1-phosphate, endothelial differentiation gene (Edg) receptors and Akt kinase induce a signal transduction pathway via phosphorylation of a serine residue in eNOS. Bradykinin, a nonapeptide formed by enzymatic cleavage of a plasma protein precursor, activates eNOS by an independent pathway that does not require serine phosphorylation, suggesting a complex interplay of signals in the control of endothelial formation of nitric oxide.

Publication types

  • News

MeSH terms

  • Animals
  • Bradykinin / metabolism
  • Enzyme Activation
  • Humans
  • Lysophospholipids*
  • Nitric Oxide / metabolism
  • Nitric Oxide Synthase / metabolism*
  • Nitric Oxide Synthase Type III
  • Signal Transduction
  • Sphingolipids / metabolism*
  • Sphingosine / analogs & derivatives
  • Sphingosine / metabolism


  • Lysophospholipids
  • Sphingolipids
  • sphingosine 1-phosphate
  • Nitric Oxide
  • NOS3 protein, human
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type III
  • Sphingosine
  • Bradykinin