An inducible nitric-oxide synthase (NOS)-associated protein inhibits NOS dimerization and activity

Edward A. Ratovitski, Clare Bao, Richard A. Quick, Audrey McMillan, Chaim Kozlovsky, Charles J. Lowenstein

Research output: Contribution to journalArticlepeer-review

74 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)30250-30257
Number of pages8
JournalJournal of Biological Chemistry
Issue number42
StatePublished - Oct 15 1999

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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