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Related Concept Videos

Nitric Oxide Signaling Pathway01:28

Nitric Oxide Signaling Pathway

Nitric oxide (NO), an inorganic gas, acts as a potent second messenger in most animal and plant tissues. NO diffuses out of the cells that produce it and enters the neighboring cells to generate a downstream response. NO synthase (NOS) catalyzes NO production by the deamination of the amino acid arginine. There are three isoforms of NOS. Endothelial cells have endothelial NOS (eNOS), nerve and muscle cells have neuronal NOS (nNOS), and macrophages produce inducible NOS (iNOS) upon exposure to...
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Related Experiment Video

Updated: May 9, 2026

Application of Genetically Encoded Fluorescent Nitric Oxide (NO•) Probes, the geNOps, for Real-time Imaging of NO• Signals in Single Cells
08:32

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Published on: March 16, 2017

Decoding the substrate supply to human neuronal nitric oxide synthase.

Alexandra Simon1, Susanne Karbach, Alice Habermeier

  • 1Department of Pharmacology, University Medical Centre of the Johannes Gutenberg University, Mainz, Germany.

Plos One
|July 23, 2013
PubMed
Summary
This summary is machine-generated.

Controlling nitric oxide (NO) production is crucial for neurological health. This study reveals how arginine supply, from extracellular sources or protein breakdown, impacts neuronal nitric oxide synthase (nNOS) activity in brain cells.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Nitric oxide (NO) is a vital neurotransmitter in the central nervous system, regulating various functions.
  • Dysregulated NO production is implicated in neurodegenerative diseases like Alzheimer's and Parkinson's.
  • Understanding substrate supply to neuronal nitric oxide synthase (nNOS) is key to controlling NO levels.

Purpose of the Study:

  • To investigate how substrate availability influences human nNOS activity.
  • To identify the sources of arginine that nourish nNOS in neuroepithelioma and neuroblastoma cells.

Main Methods:

  • Bioactive NO was measured using cGMP formation in reporter cells.
  • Arginine pools (extracellular and intracellular) were manipulated and their effects on NO synthesis assessed.
  • The role of protein breakdown and citrulline conversion in arginine supply was examined.

Main Results:

  • Extracellular arginine efficiently fuels nNOS in both cell types.
  • Intracellular arginine, primarily from protein breakdown, sustains NO synthesis when extracellular arginine is depleted.
  • Citrulline-to-arginine conversion supports nNOS only in neuroblastoma cells.
  • Histidine inhibits nNOS by depleting the exchangeable arginine pool.

Conclusions:

  • nNOS activity is significantly modulated by its substrate supply.
  • Targeting arginine transport and intracellular sources offers potential strategies to control nNOS activity.
  • Cell-type specific differences exist in arginine metabolism impacting nNOS function.