Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme.

• C J Lowenstein

  Department of Neuroscience, Johns Hopkins Medical Institutions, Baltimore, MD 21205.

• C S Glatt

  Department of Neuroscience, Johns Hopkins Medical Institutions, Baltimore, MD 21205.

• D S Bredt

  Department of Neuroscience, Johns Hopkins Medical Institutions, Baltimore, MD 21205.

• S H Snyder

  Department of Neuroscience, Johns Hopkins Medical Institutions, Baltimore, MD 21205.

Abstract

Nitric oxide (NO) is a messenger molecule of macrophages, endothelial cells in blood vessels, and neurons. A neuronal form of NO synthase (NOS) has been previously cloned. We now report the molecular cloning of macrophage NOS. The macrophage enzyme displays 50% sequence identity to the neuronal enzyme. Like neuronal NOS, macrophage NOS has recognition sites for FAD, FMN, and NADPH and also has a consensus calmodulin binding site. Macrophage NOS mRNA is strikingly inducible; it is absent in quiescent macrophages or spleen but is prominent 2-6 hr after endotoxin treatment.

Journal

• Proceedings of the National Academy of Sciences

  Proceedings of the National Academy of Sciences 89 (15), 6711-6715, 1992-08

  Proceedings of the National Academy of Sciences

Keywords

• Multidisciplinary

Details

• CRID: 1360011145988999808
• NII Article ID: 80006617531
• DOI: 10.1073/pnas.89.15.6711
• ISSN: 10916490
• ISSN: 00278424
• ISSN: http://id.crossref.org/issn/00278424
• Web Site: https://pnas.org/doi/pdf/10.1073/pnas.89.15.6711
• Data Source:
  • Crossref
  • CiNii Articles