Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated? - PubMed (original) (raw)
Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated?
M A Marletta. Trends Biochem Sci. 2001 Sep.
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.
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