| Autor: |
McDonald, Kelly K., Zharikov, Sergei, Block, Edward R., Kilberg, Michael S. |
| Zdroj: |
Journal of Biological Chemistry; December 1997, Vol. 272 Issue: 50 p31213-31216, 4p |
| Abstrakt: |
Immunohistochemistry of porcine pulmonary artery endothelial cells (PAEC) with antibodies specific for caveolin, endothelial nitric-oxide synthase (eNOS), and the arginine transporter (CAT1) demonstrates that all of these proteins co-localize in plasma membrane caveolae. When incubated with solubilized PAEC plasma membrane proteins, eNOS-specific antibody immunoprecipitates CAT1-mediated arginine transport. These results document the existence of a caveolar complex between CAT1 and eNOS in PAEC that provides a mechanism for the directed delivery of substrate arginine to eNOS. Direct transfer of extracellular arginine to membrane-bound eNOS accounts for the “arginine paradox” and explains why caveolar localization of eNOS is required for optimal nitric oxide production by endothelial cells. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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