Probing the presence of the ligand‐binding haem in cellular nitric oxide receptors
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Background and purpose: Nitric oxide (NO) acts on receptors coupled to guanylyl cyclase (GC), leading to cGMP accumulation. The NO binding site is a haem group, oxidation or loss of which diminishes NO‐stimulated activity. Agonists reportedly engaging both these NO‐insensitive forms have emerged. Here we characterize the effect of a prototype compound (BAY 58‐2667) and use it to assess the haem status of cellular GC. Experimental approach: GC activity measurements were made on the purified protein and on rat platelets. Key results: Experiments on purified GC showed that the target for BAY 58‐2667 is the haem‐free GC, not the haem‐oxidized form. The efficacy of BAY 58‐2667 was about half that shown normally by NO. In platelets, BAY 58‐2667 was a potent GC activator (EC 50 ∼15 nM) but the maximum effect was only about 1% of that achievable with NO. Nevertheless, it was enough to evoke cGMP‐dependent protein phosphorylation. Profound (85 %) desensitization of NO‐evoked GC activity did not alter the effectiveness of BAY 58‐2667. Haem oxidation, however, increased the efficacy of BAY 58‐2667 by 22‐fold, implying that about half the cellular GC was then haem‐free. Oxidation appeared to enhance the rate of haem dissociation from purified GC. Conclusions and implications: Compounds such as BAY 58‐2667 are useful for probing the occupancy of the haem pocket of NO receptors in cells but not for distinguishing oxidized from reduced haem. In vivo, such compounds are likely to be particularly effective in conditions where there is deficient haem incorporation or enhanced haem loss. British Journal of Pharmacology (2008) 153, 1495–1504; doi:10.1038/sj.bjp.0707687; published online 21 January 2008
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Most cells have intracellular l-arginine concentrations manyfold higher than the eNOS KM value.
“This finding was rather surprising, as most cells have intracellular l-arginine concentrations manyfold higher than the eNOS KM value, and thus, this observation has been termed the “arginine paradox” (12, 797).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [797]
Direct supplementation of l-arginine increases NO production in cells.
“The direct supplementation of l-arginine was shown to increase NO production in cells.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [797]
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Jahandideh, F., Panahi, S., Noble, R. M. N., Gragasin, F. S., Khadaroo, R. G., Macala, K. F., & Bourque, S. L. (2022) · Biomedicines · doi:10.3390/biomedicines10020470 · Cited by 2 · see citing works
Nitric Oxide and Synaptic Transmission in the Cerebellum
Collado‐Alsina, A., Rampérez, A., Sánchez‐Prieto, J., & Torres, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-23810-0_112 · Cited by 2 · see citing works
Tetrahydrobiopterin protects soluble guanylate cyclase against oxidative inactivation
Schmidt, K., Werner, E. R., & Mayer, B. (2013) · Pteridines · doi:10.1515/pterid-2013-0015 · Cited by 1 · see citing works
Cardioprotection afforded by targeting guanylyl cyclase during early reperfusion
Bice, J. S. (2012) · ORCA Online Research @Cardiff (Cardiff University)
Ferreira, P. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2017.tde-16052017-114902
Pathophysiology of Pulmonary Hypertension
Gao, Y., & Raj, J. U. (2017) · Colloquium Series on Integrated Systems Physiology From Molecule to Function · doi:10.4199/c00158ed1v01y201710isp078
Nitric Oxide and Synaptic Transmission in the Cerebellum
Collado‐Alsina, A., Rampérez, A., Sánchez‐Prieto, J., & Torres, M. (2019) · Springer eBooks · doi:10.1007/978-3-319-97911-3_112-1
- Authors
- Roy, B., Mo, E., Vernon, J., & Garthwaite, J.
- Affiliations
- University College London (GB)
- Corresponding author
- Garthwaite, J
- ORCID
- Garthwaite, J
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2008-04
- Volume
- 153
- Issue
- 7
- Pages
- 1495-1504
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- PMC
- PMC2437902
- OpenAlex
- W1540798144
- Cited by
- 62
- References
- 39
- Citations by year
- 2025: 1 · 2022: 3 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 4 · 2016: 4 · 2015: 4 · 2014: 5 · 2013: 3 · 2012: 7
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- British Journal of Pharmacology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust
- Medical Research Council
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- nitric oxide receptors, guanylate cyclase, haem group, BAY 58-2667, platelets, receptor desensitization
- MeSH terms
- Soluble Guanylyl Cyclase, Animals, Benzoates, Binding Sites, Blood Platelets, Cattle, Dose-Response Relationship, Drug, Cyclic GMP, Guanylate Cyclase, Heme, Ligands, Nitric Oxide, Oxidation-Reduction, Phosphorylation, Drug Delivery Systems, Receptors, Cytoplasmic and Nuclear, Rats
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