eNOS Polyclonal Antiserum

eNOS catalyzes the formation of NO from L-arginine in many cell types including vascular endothelium, bronchiolar epithelium, cardiac myocytes, spleen, and kidney.^1,2,3 Although eNOS was initially characterized as a constitutive enzyme, expression of eNOS mRNA is altered by many factors including shear stress, fibroblast growth factor, hypoxia, and LPS.^4,5,6 eNOS is myristoylated and palmitoylated at the N-terminus, modifications which are required for localization to the plasmalalemmal caveolae of endothelial cells.^7,8,9,10,11 Additionally, eNOS is phosphorylated on Ser¹¹⁷⁹ by protein kinase Akt resulting in an increase in NOS activity.^12,13,14

WARNING This product is not for human or veterinary use.

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2. Shaul, P.W., North, A.J., Wu, L.C., et al. Endothelial nitric oxide synthase is expressed in cultured human bronchiolar epithelium. J. Clin. Invest. 94(6), 2231-2236 (1994).

3. Balligand, J.L., Kobzik, L., Han, X., et al. Nitric oxide-dependent parasympathetic signaling is due to activation of constitutive endothelial (type III) nitric oxide synthase in cardiac myocytes. The Journal of Biological Chemisty 270(24), 14582-14586 (1995).

4. Xiao, Z., Zhang, Z., and Diamond, S.L. Shear stress induction of the endothelial nitric oxide synthase gene is calcium-dependent but not calcium-activated. J. Cell. Physiol. 171(2), 205-211 (1997).

5. Arnett, U.A., McMillan, A., Dinerman, J.L., et al. Regulation of endothelial nitric-oxide synthase during hypoxia. The Journal of Biological Chemisty (251)271, 15069-15073 (1996).

6. Lu, J.L., Schmiege, L.M., III, Kuo, L., et al. Downregulation of endothelial constitutive nitric oxide synthase expression by lipopolysaccharide. Biochem. Biophys. Res. Commun. 225(1), 1-5 (1996).

7. Busconi, L., and Michel, T. Endothelial nitric oxide synthase. N-terminal myristoylation determines subcellular localization. The Journal of Biological Chemisty 268(12), 8410-8413 (1993).

8. Robinson, L.J., and Michel, T. Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting. Proc. Natl. Acad. Sci. USA 92(25), 11776-11780 (1995).

9. Feron, O., Saldana, F., Michel, J.B., et al. The endothelial nitric-oxide synthase-caveolin regulatory cycle. The Journal of Biological Chemisty 273(6), 3125-3128 (1998).

10. García-Cardeña, G., Oh, P., Liu, J., et al. Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling. Proc. Natl. Acad. Sci. USA 93(13), 6448-6453 (1996).

11. Feron, O., Belhassen, L., Kobzik, L., et al. Endothelial nitric oxide synthase targeting to caveolae. Specific interactions with caveolin isoforms in cardiac myocytes and endothelial cells. The Journal of Biological Chemisty 271(37), 22810-22814 (1996).

12. Corson, M.A., James, N.L., Latta, S.E., et al. Phosphorylation of endothelial nitric oxide synthase in response to fluid shear stress. Circ. Res. 79(5), 984-991 (1996).

13. Dimmeler, S., Fleming, I., Fisslthaler, B., et al. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399(6736), 601-605 (1999).

14. Fulton, D., Gratton, J.P., McCabe, T.J., et al. Regulation of endothelium-derived nitric oxide production by the protein kinase Akt. Nature 399(6736), 597-601 (1999).