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New insight into the functioning of nitric oxide-receptive guanylyl cyclase: physiological and pharmacological implications
Abstract
The cellular counterpart of the "soluble" guanylyl cyclase found in tissue homogenates over 30 years ago is now recognized as the physiological receptor for nitric oxide (NO). The ligand-binding site is a prosthetic haem group that, when occupied by NO, induces a conformational change in the protein that propagates to the catalytic site, triggering conversion of GTP into cGMP. This review focuses on recent research that takes this basic information forward to the beginnings of a quantitative depiction of NO signal transduction, analogous to that achieved for other major transmitters. At its foundation is an explicit enzyme-linked receptor mechanism for NO-activated guanylyl cyclase that replicates all its main properties. In cells, NO signal transduction is subject to additional, activity-dependent modifications, notably through receptor desensitization and changes in the activity of cGMP-hydrolyzing phosphodiesterases. The measurement of these parameters under varying conditions in rat platelets has made it possible to formulate a cellular model of NO-cGMP signaling. The model helps explain cellular responses to NO and their modification by therapeutic agents acting on the guanylyl cyclase or phosphodiesterase limbs of the pathway.
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“The high affinity and rapid binding to ferrous heme are important biologically for the activation of sGC to generate the second messenger cGMP and the regulation of mitochondrial respiration at CcOx (9–16).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [14]
In the citing paper
“The high affinity and rapid binding to ferrous heme are important biologically for the activation of sGC to generate the second messenger cGMP and the regulation of mitochondrial respiration at CcOx (9–16).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [14]
In the citing paper
“Notably, CcOx is considerably less sensitive to NO-mediated inhibition than sGC is to NO-dependent activation (14, 43).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [14]
In the citing paper
“Of these three interactions of NO with ferrous heme proteins, it is widely accepted that binding sGC satisfies all of the requirements for cell signaling, including regulation and amplification of the signaling pathway (14, 15).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [14]
In the citing paper
“For instance, sGC does not bind O2 but does form 5-coordinate Fe2+·NO complexes, which subsequently activate the enzyme and are responsible for the cGMP-dependent effects of NO.”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [14]
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Metadata
- Authors
- Garthwaite, J.
- Affiliations
- University College London (GB)
- Corresponding author
- Garthwaite, John
- ORCID
- Garthwaite, John
- Venue
- Molecular and Cellular Biochemistry
- Published
- 2009-12-11
- Volume
- 334
- Issue
- 1-2
- Pages
- 221-232
- ISSN
- 0300-8177 (ISSN-L)
- 1573-4919
- OpenAlex
- W2006132439
- Cited by
- 102
- References
- 99
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 4 · 2018: 9 · 2017: 6 · 2016: 9 · 2015: 9 · 2014: 8 · 2013: 8 · 2012: 11
- FWCI
- 0.84
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Molecular and Cellular Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust (081512/Z/06/Z)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Phosphodiesterase function and regulation
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- soluble guanylate cyclase, nitric oxide signaling, cyclic GMP, conformational change, receptor desensitization, phosphodiesterase, platelets
- MeSH terms
- Soluble Guanylyl Cyclase, Animals, Cyclic GMP, Guanylate Cyclase, Signal Transduction, Receptors, Cytoplasmic and Nuclear, Rats
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