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J Biol Chem, Vol. 274, Issue 29, 20265-20270, July 16, 1999

Inhibition of Endothelial Nitric-oxide Synthase by Ceruloplasmin

Andrea Bianchini, Giovanni Musci^§, and Lilia Calabrese^¶

From the  Department of Biochemical Sciences, University La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy,^§ Department of Organic and Biological Chemistry, University of Messina, Salita Sperone 31, 98166 S. Agata Messina, Italy, ^¶ Department of Biology, University Roma Tre, Viale Marconi 446, 00146 Rome, Italy, and  CNR Center of Molecular Biology, University La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy

The plasma copper protein ceruloplasmin (CP) was found to inhibit endothelial nitric-oxide synthase activation in cultured endothelial cells, in line with previous evidence showing that the endothelium-dependent vasorelaxation of the aorta is impaired by physiological concentrations of ceruloplasmin. The data presented here indicate a direct relationship between the extent of inhibition of agonist-triggered endothelial nitric oxide synthase activation and CP-induced enrichment of the copper content of endothelial cells. Copper discharged by CP was mainly localized in the soluble fraction of cells. The subcellular distribution of the metal seems to be of relevance to the inhibitory effect of CP, because it was mimicked by copper chelates, like copper-histidine, able to selectively enrich the cytosolic fraction of cells, but not by copper salts, which preferentially located the metal to the particulate fraction.

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