Intracellular translocation of endothelial nitric oxide synthase by lysophosphatidylcholine.
The amphiphile lysophosphatidylcholine (LPC) modulates the activity of membrane-associated enzymes such as phospholipase A2, adenylate and guanylate cyclases and ATPase. LPC also relaxes vascular smooth muscle through production of nitric oxide. On the basis of reports that bradykinin translocates nitric oxide synthase (NOS) from the membrane to the cytosol, we investigated whether a similar translocation occurs with LPC. It was found that LPC translocated NOS from the membrane to the cytosolic fraction. Total NOS activity remained at the control level.
Dudek
R
R
Department of Experimental Cardiology, Huntington Medical Research Institutes, Pasadena, CA 91101, USA.
Wildhirt
S
S
Suzuki
H
H
Winder
S
S
Bing
R J
RJ
D000594:Amino Acid Oxidoreductases / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D001011:Aorta; D001692:Biological Transport / Q000187:drug effects; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D003600:Cytosol / Q000201:enzymology; D004730:Endothelium, Vascular / Q000187:drug effects / Q000378:metabolism*; D004789:Enzyme Activation; D008244:Lysophosphatidylcholines / Q000494:pharmacology*; D019001:Nitric Oxide Synthase
D008244:Lysophosphatidylcholines; D019001:Nitric Oxide Synthase; D000594:Amino Acid Oxidoreductases