| Autor: |
Sessa, W C, García-Cardeña, G, Liu, J, Keh, A, Pollock, J S, Bradley, J, Thiru, S, Braverman, I M, Desai, K M |
| Zdroj: |
Journal of Biological Chemistry; July 1995, Vol. 270 Issue: 30 p17641-4, 4p |
| Abstrakt: |
The particulate enzyme, endothelial nitric oxide synthase (eNOS), produces nitric oxide to maintain normal vasodilator tone in blood vessels. In this study, we demonstrate that eNOS is a Golgi-associated protein in cultured endothelial cells and intact blood vessels. Using a heterologous expression system in HEK 293 cells, we show that wild-type myristoylated and palmitoylated eNOS, but not mutant, non-acylated eNOS targets to the Golgi. More importantly, HEK 293 cells expressing wild-type eNOS release substantially more NO than cells expressing the mutant, non-acylated enzyme. Thus, eNOS is a novel Golgi-associated protein, and Golgi compartmentalization is necessary for the enzyme to respond to intracellular signals and produce NO. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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