| pubmed-article:11489261 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C0242643 | lld:lifeskim |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C0000097 | lld:lifeskim |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C0000098 | lld:lifeskim |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C0600688 | lld:lifeskim |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C2347946 | lld:lifeskim |
| pubmed-article:11489261 | lifeskim:mentions | umls-concept:C0205198 | lld:lifeskim |
| pubmed-article:11489261 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11489261 | pubmed:dateCreated | 2001-8-7 | lld:pubmed |
| pubmed-article:11489261 | pubmed:abstractText | The vesicular monoamine transporter 2 (VMAT2) has sequence homology with bacterial multidrug transporters which in turn share homology with mammalian P-glycoprotein (P-GP). Both VMAT2 and P-GP can detoxify cells. 1-Methyl-4-phenylpyridinium (MPP(+)), the toxic metabolite of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), is a substrate for VMAT2 that has several structural features in common with P-GP substrates and inhibitors. The present studies investigated whether P-GP is responsible for the elimination of MPP(+) from the brain. Additionally, VMAT2 and P-GP are inhibited by many of the same compounds. Thus we also investigated whether VMAT2 inhibitors could block P-GP in vitro and vice versa whether P-GP inhibitors could block VMAT2 mediated transport of [3H]-DA into synaptic vesicles. In mice treated with MPTP and a P-GP inhibitor (quinidine, trans-flupentixol or cyclosporine A), the elimination of MPP(+) from the striatum was significantly delayed. However, in experiments using various cell lines expressing either mouse or human P-GP, MPP(+) did not reverse the P-GP mediated resistance to vincristine, suggesting that MPP(+) is a poor substrate for P-GP. Additional experiments were performed using mdr1a/b double knockout mice which lack functional P-GP encoded by these two genes. Data from mdr1a/b knockout mice treated with MPTP also suggest that MPP(+) is not extruded from the brain by P-GP. In other studies, we demonstrated that the VMAT2 inhibitors tetrabenazine and Ro 4-1284 inhibit P-GP and that the P-GP inhibitors trans-flupentixol and quinidine inhibit VMAT2. Thus, several new drugs can be added to the list of compounds that are able to inhibit both VMAT2 and P-GP, providing further evidence of the similarity between these two transporters. | lld:pubmed |
| pubmed-article:11489261 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11489261 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11489261 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11489261 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11489261 | pubmed:issn | 0006-8993 | lld:pubmed |
| pubmed-article:11489261 | pubmed:author | pubmed-author:HaitW NWN | lld:pubmed |
| pubmed-article:11489261 | pubmed:author | pubmed-author:YangJ MJM | lld:pubmed |
| pubmed-article:11489261 | pubmed:author | pubmed-author:SonsallaP KPK | lld:pubmed |
| pubmed-article:11489261 | pubmed:author | pubmed-author:StaalR GRG | lld:pubmed |
| pubmed-article:11489261 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11489261 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:11489261 | pubmed:volume | 910 | lld:pubmed |
| pubmed-article:11489261 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11489261 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11489261 | pubmed:pagination | 116-25 | lld:pubmed |
| pubmed-article:11489261 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11489261 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11489261 | pubmed:articleTitle | Interactions of 1-methyl-4-phenylpyridinium and other compounds with P-glycoprotein: relevance to toxicity of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. | lld:pubmed |
| pubmed-article:11489261 | pubmed:affiliation | Department of Neurology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854-4535, USA. | lld:pubmed |
| pubmed-article:11489261 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11489261 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
