Interaction of Neuronal Nitric-oxide Synthase with Caveolin-3 in Skeletal Muscle
Open accessAbstract
Neuronal nitric-oxide synthase (nNOS) has been shown previously to interact with alpha1-syntrophin in the dystrophin complex of skeletal muscle. In the present study, we have examined whether nNOS also interacts with caveolin-3 in skeletal muscle. nNOS and caveolin-3 are coimmunoprecipitated from rat skeletal muscle homogenates by antibodies directed against either of the two proteins. Synthetic peptides corresponding to the membrane-proximal caveolin-3 residues 65-84 and 109-130 and homologous caveolin-1 residues 82-101 and 135-156 potently inhibit the catalytic activity of purified, recombinant nNOS. Purified nNOS also binds to a glutathione S-transferase-caveolin-1 fusion protein in in vitro binding assays. In vitro binding is completely abolished by preincubation of nNOS with either of the two caveolin-3 inhibitory peptides. Interactions between nNOS and caveolin-3, therefore, appear to be direct and to involve two distinct caveolin scaffolding/inhibitory domains. Other caveolin-interacting enzymes, including endothelial nitric-oxide synthase and the c-Src tyrosine kinase, are also potently inhibited by each of the four caveolin peptides. Inhibitory interactions mediated by two different caveolin domains may thus be a general feature of enzyme docking to caveolin proteins in plasmalemmal caveolae.
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The BH4/BH2 ratio gives a more precise estimation of endothelial function than the relative amount of BH2.
“Thus, rather than the relative amount of BH2, the BH4/BH2 ratio gives a more precise estimation of the endothelial function (190, 192, 974).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [974]
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- Authors
- Venema, V. J., Ju, H., Zou, R., & Venema, R. C.
- Affiliations
- Augusta University (US)
- Corresponding author
- Venema, Virginia J.
- Venema, Richard C.
- ORCID
- Zou, Rong
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-11
- Volume
- 272
- Issue
- 45
- Pages
- 28187-28190
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2081617200
- Cited by
- 256
- References
- 27
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 1 · 2022: 7 · 2021: 2 · 2020: 4 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 4 · 2015: 3 · 2014: 4 · 2013: 5 · 2012: 7
- FWCI
- 7.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL57201)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- neuronal nitric oxide synthase, caveolin-3, caveolin-1, protein-protein interaction, skeletal muscle, caveolae, peptide inhibitors, enzyme inhibition, caveolin scaffolding domain, nitric oxide synthase
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Calcium-Binding Proteins, Humans, Membrane Proteins, Molecular Sequence Data, Muscle Proteins, Neurons, Muscle, Skeletal, Nitric Oxide Synthase, Caveolins, Caveolin 3, Rats
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