| pubmed-article:10702266 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0008524 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C1517377 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0528200 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0332206 | lld:lifeskim |
| pubmed-article:10702266 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:10702266 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:10702266 | pubmed:dateCreated | 2000-4-3 | lld:pubmed |
| pubmed-article:10702266 | pubmed:abstractText | To determine the intracellular signaling mechanism of the 5-HT(2C) receptor endogenously expressed in choroid plexus epithelial cells, we implemented a strategy of targeted disruption of protein-protein interactions. This strategy entails the delivery of conjugated membrane-permeable peptides that disrupt domain interaction at specific steps in the signaling cascade. As proof of concept, two peptides targeted against receptor-G protein interaction domains were examined. Only G(q)CT, which targets the receptor-G(q) protein interacting domain, disrupted 5-HT(2C) receptor-mediated phosphatidylinositide hydrolysis. G(s)CT, targeting the receptor-G(s) protein, disrupted beta2 adrenergic receptor-mediated activation of cAMP but not 5-HT(2C) receptor-mediated phosphatidylinositide hydrolysis. The peptide MPS-PLCbeta1M, mimicking the domain of phospholipase Cbeta1 (PLCbeta1) interacting with active Galpha(q), also blocked 5-HT(2C) receptor activation. In contrast, peptides PLCbeta2M and Phos that bind to and sequester free Gbetagamma subunits were ineffective at blocking 5-HT(2C) receptor-mediated phosphoinositol turnover. However, both peptides disrupted Gbetagamma-mediated alpha(2A) adrenergic receptor activation of mitogen-activated protein kinase. These results provide the first direct demonstration that active Galpha(q) subunits mediate endogenous 5-HT(2C) receptor activation of PLCbeta and that Gbetagamma subunits released from Galpha(q) heterotrimeric proteins are not involved. Comparable results were obtained with metabotropic glutamate receptor 5 expressed in astrocytes. Thus, conjugated, membrane-permeable peptides are effective tools for the dissection of intracellular signals. | lld:pubmed |
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| pubmed-article:10702266 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10702266 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10702266 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10702266 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10702266 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10702266 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10702266 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10702266 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10702266 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10702266 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10702266 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10702266 | pubmed:author | pubmed-author:Sanders-BushE... | lld:pubmed |
| pubmed-article:10702266 | pubmed:author | pubmed-author:TamJ PJP | lld:pubmed |
| pubmed-article:10702266 | pubmed:author | pubmed-author:ChangMM | lld:pubmed |
| pubmed-article:10702266 | pubmed:author | pubmed-author:ZhangLL | lld:pubmed |
| pubmed-article:10702266 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10702266 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:10702266 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10702266 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10702266 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10702266 | pubmed:pagination | 7021-9 | lld:pubmed |
| pubmed-article:10702266 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10702266 | pubmed:meshHeading | pubmed-meshheading:10702266... | lld:pubmed |
| pubmed-article:10702266 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10702266 | pubmed:articleTitle | Dissecting G protein-coupled receptor signaling pathways with membrane-permeable blocking peptides. Endogenous 5-HT(2C) receptors in choroid plexus epithelial cells. | lld:pubmed |
| pubmed-article:10702266 | pubmed:affiliation | Department of Pharmacology and Center for Molecular Neuroscience, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA. | lld:pubmed |
| pubmed-article:10702266 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10702266 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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