Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.

<h4>Background</h4> <p>PWhether neuronal nitric-oxide synthase (nNOS) plays a role in the endothelial NOS (eNOS)-dependent negative inotropic effect of β3-adrenergic stimulation remains to be established.</p> <h4>Results</h4> <p>nNOS knock-out or inhibition...

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Main Authors: Idigo, W, Reilly, S, Zhang, M, Zhang, Y, Jayaram, R, Carnicer, R, Crabtree, M, Balligand, J, Casadei, B
Format: Journal article
Language:English
Published: American Society of Biochemistry and Molecular Biology 2012
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author Idigo, W
Reilly, S
Zhang, M
Zhang, Y
Jayaram, R
Carnicer, R
Crabtree, M
Balligand, J
Casadei, B
author_facet Idigo, W
Reilly, S
Zhang, M
Zhang, Y
Jayaram, R
Carnicer, R
Crabtree, M
Balligand, J
Casadei, B
author_sort Idigo, W
collection OXFORD
description <h4>Background</h4> <p>PWhether neuronal nitric-oxide synthase (nNOS) plays a role in the endothelial NOS (eNOS)-dependent negative inotropic effect of β3-adrenergic stimulation remains to be established.</p> <h4>Results</h4> <p>nNOS knock-out or inhibition leads to increased superoxide production, eNOS uncoupling, and abrogation of β3-adrenergic responses.</p> <h4>Conclusion</h4> <p>Disabling nNOS disrupts eNOS function and downstream signaling.</p> <h4>Significance</h4> <p>nNOS plays a crucial role in preserving myocardial nitroso-redox balance and coupled eNOS activity.</p>
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spelling oxford-uuid:cf26ec82-a4cd-4196-b108-a4ff720441472022-03-27T07:40:40ZRegulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cf26ec82-a4cd-4196-b108-a4ff72044147EnglishSymplectic Elements at OxfordAmerican Society of Biochemistry and Molecular Biology2012Idigo, WReilly, SZhang, MZhang, YJayaram, RCarnicer, RCrabtree, MBalligand, JCasadei, B <h4>Background</h4> <p>PWhether neuronal nitric-oxide synthase (nNOS) plays a role in the endothelial NOS (eNOS)-dependent negative inotropic effect of β3-adrenergic stimulation remains to be established.</p> <h4>Results</h4> <p>nNOS knock-out or inhibition leads to increased superoxide production, eNOS uncoupling, and abrogation of β3-adrenergic responses.</p> <h4>Conclusion</h4> <p>Disabling nNOS disrupts eNOS function and downstream signaling.</p> <h4>Significance</h4> <p>nNOS plays a crucial role in preserving myocardial nitroso-redox balance and coupled eNOS activity.</p>
spellingShingle Idigo, W
Reilly, S
Zhang, M
Zhang, Y
Jayaram, R
Carnicer, R
Crabtree, M
Balligand, J
Casadei, B
Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.
title Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.
title_full Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.
title_fullStr Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.
title_full_unstemmed Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.
title_short Regulation of endothelial nitric-oxide synthase (NOS) S-glutathionylation by neuronal NOS: evidence of a functional interaction between myocardial constitutive NOS isoforms.
title_sort regulation of endothelial nitric oxide synthase nos s glutathionylation by neuronal nos evidence of a functional interaction between myocardial constitutive nos isoforms
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