title: Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated?
abstract: 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.
authors.affiliation: Department of Chemistry, University of California, Berkeley, 94720 1460, USA. marletta@cchem.berkeley.edu
authors.forename: M A
authors.initials: MA
authors.lastname: Marletta
mesh_terms: D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D004789:Enzyme Activation; D006801:Humans; D008246:Lysophospholipids; D009569:Nitric Oxide / Q000378:metabolism; D019001:Nitric Oxide Synthase / Q000378:metabolism*; D052250:Nitric Oxide Synthase Type III; D015398:Signal Transduction; D013107:Sphingolipids / Q000378:metabolism*; D013110:Sphingosine / Q000031:analogs & derivatives / Q000378:metabolism
chemical_list: D008246:Lysophospholipids; D013107:Sphingolipids; C060506:sphingosine 1-phosphate; D009569:Nitric Oxide; C496314:NOS3 protein, human; D019001:Nitric Oxide Synthase; D052250:Nitric Oxide Synthase Type III; D013110:Sphingosine; D001920:Bradykinin