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

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Glatt, C. S. Bredt, D. S. Snyder, S. H. Lowenstein, C. J.
Description	Author Affiliation: Lowenstein CJ ( 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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acid Oxidoreductases Genetics Brain Enzymology Isoenzymes Macrophages Neurons Metabolism Amino Acid Sequence Animals Cell Line Cloning, Molecular Kinetics Mice Mice, Inbred BALB C Molecular Sequence Data Nitric Oxide Synthase Oligonucleotides, Antisense Polymerase Chain Reaction RNA, Messenger Biosynthesis Recombinant Proteins Sequence Homology, Nucleic Acid Spleen Transfection Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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