Nitric oxide synthase in cerebrovascular endothelial cells is inhibited by brefeldin A.
Nitric oxide synthase (NOS) is present within cerebrovascular endothelial cells in a distinct membrane-bound juxtanuclear location. The enzyme product, nitric oxide, causes vasodilation as well as stimulation of ADP-ribosylations of some proteins. The activity of specific stimulatory ADP-ribosylation factors, associated with the Golgi complex (GC), has been shown to be blocked by brefeldin A (BFA). We present evidence that BFA disperses the GC, disrupts NOS/NADPH diaphorase staining and inhibits NOS activity in addition to its previously described activities.
Stanboli
A
A
Neurology Research Laboratory, Veterans Administration Medical Center, Sepulveda, CA 91343.
Morin
A M
AM
D000594:Amino Acid Oxidoreductases / Q000037:antagonists & inhibitors*; D000818:Animals; D020126:Brefeldin A; D002417:Cattle; D002560:Cerebrovascular Circulation / Q000502:physiology*; D002956:Citrulline / Q000096:biosynthesis; D003517:Cyclopentanes / Q000494:pharmacology*; D004730:Endothelium, Vascular / Q000201:enzymology*; D006056:Golgi Apparatus / Q000187:drug effects / Q000201:enzymology; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000378:metabolism; D019001:Nitric Oxide Synthase; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology*
D003517:Cyclopentanes; D009419:Nerve Tissue Proteins; D011500:Protein Synthesis Inhibitors; D020126:Brefeldin A; D002956:Citrulline; D019001:Nitric Oxide Synthase; D000594:Amino Acid Oxidoreductases