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http://purl.uniprot.org/citations/9228013http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9228013http://www.w3.org/2000/01/rdf-schema#comment"Endothelial nitric-oxide synthase (eNOS) and caveolin-1 are associated within endothelial plasmalemmal caveolae. It is not known, however, whether eNOS and caveolin-1 interact directly or indirectly or whether the interaction affects eNOS activity. To answer these questions, we have cloned the bovine caveolin-1 cDNA and have investigated the eNOS-caveolin-1 interaction in an in vitro binding assay system using glutathione S-transferase (GST)-caveolin-1 fusion proteins and baculovirus-expressed bovine eNOS. We have also mapped the domains involved in the interaction using an in vivo yeast two-hybrid system. Results obtained using both in vitro and in vivo protein interaction assays show that both N- and C-terminal cytosolic domains of caveolin-1 interact directly with the eNOS oxygenase domain. Interaction of eNOS with GST-caveolin-1 fusion proteins significantly inhibits enzyme catalytic activity. A synthetic peptide corresponding to caveolin-1 residues 82-101 also potently and reversibly inhibits eNOS activity by interfering with the interaction of the enzyme with Ca2+/calmodulin (CaM). Regulation of eNOS in endothelial cells, therefore, may involve not only positive allosteric regulation by Ca2+/CaM, but also negative allosteric regulation by caveolin-1."xsd:string
http://purl.uniprot.org/citations/9228013http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.30.18522"xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/author"Ju H."xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/author"Venema V.J."xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/author"Venema R.C."xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/author"Zou R."xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/pages"18522-18525"xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/title"Direct interaction of endothelial nitric-oxide synthase and caveolin-1 inhibits synthase activity."xsd:string
http://purl.uniprot.org/citations/9228013http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9228013http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9228013
http://purl.uniprot.org/citations/9228013http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9228013
http://purl.uniprot.org/uniprot/#_E9Q9X4-mappedCitation-9228013http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9228013
http://purl.uniprot.org/uniprot/#_P70313-mappedCitation-9228013http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9228013
http://purl.uniprot.org/uniprot/#_Q8C5P3-mappedCitation-9228013http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9228013
http://purl.uniprot.org/uniprot/P70313http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9228013
http://purl.uniprot.org/uniprot/Q8C5P3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9228013
http://purl.uniprot.org/uniprot/E9Q9X4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9228013