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Nitric oxide synthase (NOS), a cell-type specific enzyme, catalyzes the synthesis of nitric oxide (NO). NO is a short-lived radical that transmits cellular signals involved in vasorelaxation, neurotransmission, and cytotoxicity. In neurons and endothelial cells, constitutive NOS (cNOS) is activated by agonists that increase intracellular Ca2 levels and enhance calmodulin binding. Neuronal NOS (nNOS or bNOS) and endothelial NOS (ECNOS) have recognition sites for NADPH, FAD, FMN, and calmodulin and are regulated in a similar manner. However, both have been shown to be distinct gene products of about 155kDa and 140kDa, respectively, and the human forms show 52% amino acid identity. Neuronal NOS and induced macrophage NOS (iNOS) share 51% amino acid homology with the greatest degree of divergence in the calmodulin binding domain. Neuronal NOS, a cytosolic protein present mainly in neural tissues, has been purified and characterized from rat cerebellum. The NO synthesized by this enzyme acts as a neurotransmitter. ECNOS has been cloned from human vascular endothelium as well as from bovine aortic endothelial cells (BAEC) and has a unique N-myristylation consensus sequence that may explain its membrane localization.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
