Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1983-5-27
|
pubmed:abstractText |
The mast cell degranulating capacity of neurotensin and three of its fragments was examined. In Tyrode solution (137 mM NaCl, 2.7 mM KCl, 0.4 mM NaH2PO4, 1.4 mM CaCl2, 1 mM MgCl2, 10 mM Hepes, 5.6 mM glucose, pH 7.4), neither intact neurotensin nor its C-terminal tripeptide (Tyr-Ile-Leu) caused any release of histamine. Concentrations of neurotensin exceeding 10(-4)M did cause histamine release but through lysis of the cells. The C-terminal hexa- and octapeptides of neurotensin (Arg-Arg-Pro-Tyr-Ile-Leu and Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu, respectively) induced a non-cytolytic release of histamine with the latter peptide being more active (ED50 = 90 microM for the hexapeptide and 13 microM for the octapeptide). This release was not affected by the C-terminal tripeptide. It was found to be calcium-dependent and was inhibited by the anti-allergic drug, disodium cromoglycate. Phosphatidylserine did not enhance release of histamine and saturation of the immunoglobulin E (IgE) receptors did not inhibit it.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotensin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0028-3908
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
22
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
197-201
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:6188072-Animals,
pubmed-meshheading:6188072-Calcium,
pubmed-meshheading:6188072-Cytoplasmic Granules,
pubmed-meshheading:6188072-Histamine Release,
pubmed-meshheading:6188072-Immunoglobulin E,
pubmed-meshheading:6188072-L-Lactate Dehydrogenase,
pubmed-meshheading:6188072-Male,
pubmed-meshheading:6188072-Mast Cells,
pubmed-meshheading:6188072-Neurotensin,
pubmed-meshheading:6188072-Peptide Fragments,
pubmed-meshheading:6188072-Phosphatidylserines,
pubmed-meshheading:6188072-Rats,
pubmed-meshheading:6188072-Rats, Inbred Strains,
pubmed-meshheading:6188072-Structure-Activity Relationship
|
pubmed:year |
1983
|
pubmed:articleTitle |
Structure-activity relationship in the mast cell degranulating capacity of neurotensin fragments.
|
pubmed:publicationType |
Journal Article,
In Vitro
|