Expression of constitutive endothelial nitric oxide synthase in human blood platelets.
Nitric oxide (NO) activates the soluble isoform of guanylate cyclase in platelets and inhibits platelet function. Several studies suggest the existence of a pathway for NO synthesis in platelets as a form of feedback inhibition, but the identity of the NO synthase (NOS) isoform present within platelets is unknown. We isolated human platelets, and synthesized cDNA from platelet RNA for analysis by PCR. Primers for human neuronal or inducible NOS failed to yield a PCR signal. However, primers specific for endothelial NOS (ecNOS) amplified a DNA band of the expected size. Analysis of nucleotide sequence revealed that the amplified DNA is ecNOS. NOS enzyme activity was detected in the platelet particulate subcellular fraction, as previously demonstrated for ecNOS in other cells. Thus, ecNOS is present in human platelets, and may play a role in the regulation of platelet function by an endogenous NO pathway.
D001483:Base Sequence; D001792:Blood Platelets / Q000201:enzymology*; D006152:Cyclic GMP / Q000096:biosynthesis; D004730:Endothelium, Vascular / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D009569:Nitric Oxide / Q000096:biosynthesis; D019001:Nitric Oxide Synthase / Q000235:genetics / Q000378:metabolism*; D016133:Polymerase Chain Reaction
D009569:Nitric Oxide; D019001:Nitric Oxide Synthase; D006152:Cyclic GMP