Source:http://linkedlifedata.com/resource/pubmed/id/11352645
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2001-5-15
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pubmed:abstractText |
The internalization of [3H]propionyl[Met(O2)11]SP(7-11) which binds one binding site and of [3H][Pro9]SP which binds the two binding sites associated with the NK-1 receptor has been examined in CHO cells. The quantity of [3H][Pro9]SP measured inside the cytoplasm in kinetic experiments is fully temperature-dependent. In contrast, [3H]propionyl[Met(O2)11]SP(7-11) internalization reaches the same extent whatever the temperature, although the rate slowed down with lower temperature. The extent of internalization of [3H][Pro(9)]SP relative to the total specific bound is biphasic, when the extent of internalization of [3H]propionyl[Met(O2)11]SP(7-11) remains constant. For [3H][Pro9]SP, a high-affinity high-yield component inhibited in the presence of propionyl[Met(O2)11]SP(7-11) and a low-affinity low-yield component in the internalization process could be determined. Saturation studies show that [3H][Pro9]SP-binding parameters are insensitive to both phenylarsine oxide and monensin treatment, whereas [3H]propionyl[Met(O2)11]SP(7-11) maximal binding is decreased in both cases. Altogether, these data suggest that the two radiolabeled peptides should not follow the same internalization pathway.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arsenicals,
http://linkedlifedata.com/resource/pubmed/chemical/Monensin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurokinin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Substance P,
http://linkedlifedata.com/resource/pubmed/chemical/oxophenylarsine,
http://linkedlifedata.com/resource/pubmed/chemical/propionyl-(Met(O2)11)substance...,
http://linkedlifedata.com/resource/pubmed/chemical/substance P, Pro(9)-
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
958-64
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:11352645-Animals,
pubmed-meshheading:11352645-Arsenicals,
pubmed-meshheading:11352645-CHO Cells,
pubmed-meshheading:11352645-Cricetinae,
pubmed-meshheading:11352645-Endocytosis,
pubmed-meshheading:11352645-Kinetics,
pubmed-meshheading:11352645-Models, Biological,
pubmed-meshheading:11352645-Monensin,
pubmed-meshheading:11352645-Peptide Fragments,
pubmed-meshheading:11352645-Receptors, Neurokinin-1,
pubmed-meshheading:11352645-Substance P,
pubmed-meshheading:11352645-Temperature,
pubmed-meshheading:11352645-Transfection
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pubmed:year |
2001
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pubmed:articleTitle |
Internalization of [3H]substance P analogues in NK-1 receptor transfected CHO cells.
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pubmed:affiliation |
Unité Mixte de Recherches CNRS 7613, Chimie Organique Biologique, Université Pierre & Marie Curie, Aile 44-45, Bo $$;ite courrier 182, 4 place Jussieu, Paris cedex 05, 75252, France. sagan@ccr.jussieu.fr
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pubmed:publicationType |
Journal Article
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