Work

An Inducible Nitric-oxide Synthase (NOS)-associated Protein Inhibits NOS Dimerization and Activity

Year: 1999

Type: article

Abstract: 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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.274.42.30250

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

Institutions: Johns Hopkins University, Johns Hopkins Medicine

Language: English

Topic: Nitric Oxide and Endothelin Effects

Subfield: Physiology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430