Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1996-9-20
|
| pubmed:abstractText |
The human NK-1 receptor transfected in Chinese hamster ovary (CHO) cells was studied with use of different tachykinin analogs: Substance P, [Pro9]SP, [Sar9, Met(O2)11]SP, [Gly9 psi (CH2CH2) Leu10]SP, Ac-Arg-septide, septide, [Gly9 psi (CH2CH2) Gly10]SP, NKA, [pGlu6]SP(6-11) and [Lys5]NKA(4-10). Binding experiments with [3H][Pro9]SP discriminated two classes of peptides with either high affinity (K iota in the nanomolar range) for the human NK-1 receptor or with low affinity (K iota in the micromolar range); this second group of peptides included NKA and [pGlu6]SP(6-11). In spite of these differences, both peptide families evoked potent stimulation of phosphatidylinositol hydrolysis (EC50 in the nanomolar range). In contrast, only NK-1 agonists, with high affinity, stimulated with great potency cyclic AMP formation (EC50 from 8 to 50 nM), whereas the second family of peptides were only weak agonists (EC50 in the micromolar range). RP 67580, CP 96345 and GR 94800, a NK-2 antagonist, were either competitive or uncompetitive inhibitors of inositol phosphates or cyclic AMP formations induced by [Pro9]SP, septide or NKA, independently of the agonist or the response studied. Thus, NKA, the presumed NK-2 endogenous peptide that may be co-released with SP, and the enzymatically produced C-terminal fragment of SP, [pGlu6]SP(6-11), may trigger specific pharmacological responses via the NK-1 receptor, at nanomolar concentrations, and thus regulate the action of SP at the NK-1 receptor.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0022-3565
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
276
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1039-48
|
| pubmed:dateRevised |
2005-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:8786533-Animals,
pubmed-meshheading:8786533-Binding, Competitive,
pubmed-meshheading:8786533-CHO Cells,
pubmed-meshheading:8786533-Cells, Cultured,
pubmed-meshheading:8786533-Cricetinae,
pubmed-meshheading:8786533-Dose-Response Relationship, Drug,
pubmed-meshheading:8786533-Forskolin,
pubmed-meshheading:8786533-Receptors, Neurokinin-1,
pubmed-meshheading:8786533-Second Messenger Systems,
pubmed-meshheading:8786533-Substance P,
pubmed-meshheading:8786533-Tachykinins
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Tachykinin peptides affect differently the second messenger pathways after binding to CHO-expressed human NK-1 receptors.
|
| pubmed:affiliation |
Laboratoire de Chimie Organique Biologique, Université P. & M. Curie, Paris, France.
|
| pubmed:publicationType |
Journal Article
|