CALCIUM-DEPENDENT NITRIC-OXIDE SYNTHESIS IN ENDOTHELIAL CYTOSOL IS MEDIATED BY CALMODULIN
CALCIUM-DEPENDENT NITRIC-OXIDE SYNTHESIS IN ENDOTHELIAL CYTOSOL IS MEDIATED BY CALMODULIN
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DOI：
10.1016/0014-5793(90)80902-u
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发表时间：
1990-06-04
期刊：
影响因子：
3.5
通讯作者：
MULSCH, A
中科院分区：
文献类型：
--
作者：
BUSSE, R;MULSCH, A
We investigated whether calmodulin mediates the stimulating effect of Ca2+on nitric oxide synthase in the cytosol of porcine aortic endothelial cells. Nitric oxide was quantified by activation of a purified soluble guanylate cyclase. The Ca2+‐sensitivity of nitric oxide synthase was lost after anion exchange chromatography of the endothelial cytosol and could only be reconstituted by addition of calmodulin or heat‐denatured endothelial cytosol. The Ca2+‐dependent activation of nitric oxide synthase in the cytosol was inhibited by the calmodulin‐binding peptides/proteins melittin, mastoparan, and calcineurin (IC50450, 350 and 60 nM, respectively), but not by the calmodulin antagonist, calmidazolium. In contrast, Ca2+‐calmodulin‐reconstituted nitric oxide synthase was inhibited with similar potency by melittin and calmidazolium. The results suggest that the Ca2+‐dependent activation of nitric oxide synthase in endothelial cells is mediated by calmodulin.
