Inhibition of the voltage-gated potassium channel Kv1.5 by hydrogen sulfide attenuates remodeling through S-nitrosylation-mediated signaling Article Swipe
Moza M. Al‐Owais
,
Nishani T. Hettiarachchi
,
Mark Dallas
,
Jason L. Scragg
,
Jonathan D. Lippiat
,
Arun V. Holden
,
Derek S. Steele
,
Chris Peers
·
YOU?
·
· 2023
· Open Access
·
· DOI: https://doi.org/10.1038/s42003-023-05016-5
YOU?
·
· 2023
· Open Access
·
· DOI: https://doi.org/10.1038/s42003-023-05016-5
The voltage-gated K + channel plays a key role in atrial excitability, conducting the ultra-rapid rectifier K + current (I Kur ) and contributing to the repolarization of the atrial action potential. In this study, we examine its regulation by hydrogen sulfide (H 2 S) in HL-1 cardiomyocytes and in HEK293 cells expressing human Kv1.5. Pacing induced remodeling resulted in shorting action potential duration, enhanced both Kv1.5 channel and H 2 S producing enzymes protein expression in HL-1 cardiomyocytes. H 2 S supplementation reduced these remodeling changes and restored action potential duration through inhibition of Kv1.5 channel. H 2 S also inhibited recombinant hKv1.5, lead to nitric oxide (NO) mediated S-nitrosylation and activated endothelial nitric oxide synthase (eNOS) by increased phosphorylation of Ser1177, prevention of NO formation precluded these effects. Regulation of I kur by H 2 S has important cardiovascular implications and represents a novel and potential therapeutic target.
Related Topics
Concepts
Nitric oxide
Enos
Chemistry
Potassium channel
Repolarization
Cell biology
Voltage-gated potassium channel
Nitric oxide synthase
HEK 293 cells
Soluble guanylyl cyclase
Nitric Oxide Synthase Type III
Phosphorylation
Electrophysiology
Internal medicine
Biochemistry
Biophysics
Biology
Medicine
Receptor
Guanylate cyclase
Organic chemistry
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s42003-023-05016-5
- https://www.nature.com/articles/s42003-023-05016-5.pdf
- OA Status
- gold
- Cited By
- 8
- References
- 101
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4381189703
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W4381189703Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s42003-023-05016-5Digital Object Identifier
- Title
-
Inhibition of the voltage-gated potassium channel Kv1.5 by hydrogen sulfide attenuates remodeling through S-nitrosylation-mediated signalingWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2023Year of publication
- Publication date
-
2023-06-19Full publication date if available
- Authors
-
Moza M. Al‐Owais, Nishani T. Hettiarachchi, Mark Dallas, Jason L. Scragg, Jonathan D. Lippiat, Arun V. Holden, Derek S. Steele, Chris PeersList of authors in order
- Landing page
-
https://doi.org/10.1038/s42003-023-05016-5Publisher landing page
- PDF URL
-
https://www.nature.com/articles/s42003-023-05016-5.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.nature.com/articles/s42003-023-05016-5.pdfDirect OA link when available
- Concepts
-
Nitric oxide, Enos, Chemistry, Potassium channel, Repolarization, Cell biology, Voltage-gated potassium channel, Nitric oxide synthase, HEK 293 cells, Soluble guanylyl cyclase, Nitric Oxide Synthase Type III, Phosphorylation, Electrophysiology, Internal medicine, Biochemistry, Biophysics, Biology, Medicine, Receptor, Guanylate cyclase, Organic chemistryTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
8Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 3, 2024: 5Per-year citation counts (last 5 years)
- References (count)
-
101Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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