Carnosine as a regulator of soluble guanylate cyclase
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Activation of soluble guanylate cyclase by NO donors (sodium nitroprusside, a furoxan derivative), by a non-NO-donor furazan analogue and by protoporphyrin IX in the presence of carnosine.
What the authors reported
Carnosine inhibited activation of soluble guanylate cyclase by sodium nitroprusside and by a furoxan NO donor. It had no effect on stimulation by the non-NO-donor furazan analogue or on activation by protoporphyrin IX, whose action is not linked to the enzyme's haem. The authors attribute the inhibition to carnosine interacting with haem iron to form a chelate complex, and describe carnosine as a selective inhibitor of NO-dependent activation.
Limits of this study
In vitro enzyme study. Full text not read.
Source
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.