Key result
Murine macrophages express NAP110, a 110-kDa protein that directly interacts with the amino terminus of NOS2 and inhibits its catalytic activity by preventing homodimer formation.
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The discovery of NAP110 reveals a novel post-translational mechanism by which macrophages may regulate iNOS activity and protect themselves from nitric oxide toxicity.
A variety of transcriptional and post-transcriptional mechanisms regulate the expression of the inducible nitric-oxide synthase (iNOS, or NOS2). Although neurons and endothelial cells express proteins that interact with and inhibit neuronal NOS and endothelial NOS, macrophage proteins that inhibit NOS2 have not been identified. We show that murine macrophages express a 110-kDa protein that interacts with NOS2, which we call NOS-associated protein-110 kDa (NAP110). NAP110 directly interacts with the amino terminus of NOS2, and inhibits NOS catalytic activity by preventing formation of NOS2 homodimers. Expression of NAP110 may be a mechanism by which macrophages expressing NOS2 protect themselves from cytotoxic levels of nitric oxide.
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Ratovitski et al. (1999) studied this question. NAP110 expression was evaluated on NOS2 homodimer formation and catalytic activity. Murine macrophages express NAP110, a 110-kDa protein that directly interacts with the amino terminus of NOS2 and inhibits its catalytic activity by preventing homodimer formation.
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