Myristoylation of endothelial cell nitric oxide synthase is important for extracellular release of nitric oxide - PubMed (original) (raw)

. 1995 Nov 22;152(2):143-8.

doi: 10.1007/BF01076076.

Affiliations

Myristoylation of endothelial cell nitric oxide synthase is important for extracellular release of nitric oxide

T Sakoda et al. Mol Cell Biochem. 1995.

Abstract

Endothelial cell nitric oxide synthase (NOS) is known to have a N-myristoylation consensus sequence. Such a consensus sequence is not evident in the macrophage, smooth muscle and neuronal NOS. A functional role for this N-terminal myristoylation is not clear yet. In the present study, we examined the effect of N-terminal myristoylation on the NOS activity determined by the conversion of L-[3H]arginine to L-[3H]citrulline and extracellular NO release determined by nitrite production in the conditioned medium from the COS-7 cells transfected with wild-type bovine aortic endothelial cell (BAEC) NOS cDNA or non-myristoylated BAEC-NOS mutant cDNA. NOS activity of wild type BAEC-NOS in COS-7 cells was localized in the particulate fraction and that of mutant NOS was in the cytosolic fraction. In contrast, nitrite production from COS-7 cells transfected with wild type BAEC-NOS cDNA was greater than that of mutant cDNA in a time dependent and a concentration dependent manner. These results suggest that membrane localization of NOS with myristoylation facilitates extracellular transport of NO and leads to enhanced NO signaling on the vascular smooth muscle cells and the intravascular blood cells including neutrophils, macrophages and platelets.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Virology. 1978 Dec;91(2):423-33 - PubMed
    1. J Biol Chem. 1993 Apr 25;268(12):8410-3 - PubMed
    1. Anal Biochem. 1976 May 7;72:248-54 - PubMed
    1. J Clin Invest. 1992 Nov;90(5):2092-6 - PubMed
    1. Mol Cell Biol. 1990 Jun;10(6):2645-52 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources