| Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated? |
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| 引用本文： | Marletta MA. Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated?[J]. Trends in biochemical sciences, 2001, 26(9): 519-521. DOI: 10.1016/S0968-0004(01)01937-5 |
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| 作者姓名： | Marletta MA |
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| 摘 要： |
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Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated? |
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| Marletta M A. Another activation switch for endothelial nitric oxide synthase: why does it have to be so complicated?[J]. Trends in biochemical sciences, 2001, 26(9): 519-521. DOI: 10.1016/S0968-0004(01)01937-5 |
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| Authors: | Marletta M A |
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| Affiliation: | Department of Chemistry, University of California, Berkeley, 94720 1460, USA. marletta@cchem.berkeley.edu |
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| 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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