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In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
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In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
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In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
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Journal Article
In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
2000
Overview
Caveolin-1, the primary coat protein of caveolae, has been implicated as a regulator of signal transduction through binding of its “scaffolding domain” to key signaling molecules. However, the physiological importance of caveolin-1 in regulating signaling has been difficult to distinguish from its traditional functions in caveolae assembly, transcytosis, and cholesterol transport. To directly address the importance of the caveolin scaffolding domain
in vivo
, we generated a chimeric peptide with a cellular internalization sequence fused to the caveolin-1 scaffolding domain (amino acids 82–101). The chimeric peptide was efficiently taken up into blood vessels and endothelial cells, resulting in selective inhibition of acetylcholine (Ach)-induced vasodilation and nitric oxide (NO) production, respectively. More importantly, systemic administration of the peptide to mice suppressed acute inflammation and vascular leak to the same extent as a glucocorticoid or an endothelial nitric oxide synthase (eNOS) inhibitor. These data imply that the caveolin-1 scaffolding domain can selectively regulate signal transduction to eNOS in endothelial cells and that small-molecule mimicry of this domain may provide a new therapeutic approach.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Animals
/ Anti-Inflammatory Agents - pharmacology
/ Biomedical and Life Sciences
/ Capillary Permeability - drug effects
/ Cellular signal transduction
/ Control
/ Male
/ Medicine
/ Mice
/ Nitric Oxide Synthase - metabolism
/ Peptide Fragments - pharmacology
/ Peptides
/ Proteins
