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rdf:type |
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lifeskim:mentions |
umls-concept:C0006100,
umls-concept:C0007634,
umls-concept:C0022709,
umls-concept:C0107053,
umls-concept:C0182400,
umls-concept:C0205177,
umls-concept:C0441513,
umls-concept:C0678594,
umls-concept:C1527177,
umls-concept:C1527178,
umls-concept:C1705938
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pubmed:issue |
5
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pubmed:dateCreated |
1989-6-2
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pubmed:abstractText |
The peptides bradykinin and kallidin are released in response to noxious stimuli and mediate various physiological effects, including a direct stimulation of nociceptive afferent neurones. The nature of the receptor molecules through which these ligands act is presently unknown. We synthesised an iodinatable photoaffinity probe, N epsilon-4-azidosalicylylkallidin, and used it in an attempt to identify candidate bradykinin receptors on the NG108-15 neuroblastoma X glioma hybrid cell line. The ligand bound in subdued light to a particulate fraction of NG108-15 tumours and could be displaced by bradykinin with an IC50 of 0.33 nM. In a physiological assay, it behaved as an agonist equipotent with bradykinin. Gel analysis of the labelled products after photolysis of the iodinated ligand in the presence of NG108-15 cells or tumour membranes revealed bradykinin-blockable labelling of a glycoprotein with an Mr of 166,000. The probe was also able to label purified commercial angiotensin converting enzyme. The band labelled in NG108-15 cells was immunoprecipitable with a polyclonal antiserum to angiotensin converting enzyme, an enzyme shown to be present in low amounts in these preparations by direct binding using the iodinatable specific ligand MK351A.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin-Converting Enzyme...,
http://linkedlifedata.com/resource/pubmed/chemical/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Kallidin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl-Dipeptidase A,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurotransmitter,
http://linkedlifedata.com/resource/pubmed/chemical/compound 351 A
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-3042
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1508-16
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2540273-Affinity Labels,
pubmed-meshheading:2540273-Angiotensin-Converting Enzyme Inhibitors,
pubmed-meshheading:2540273-Azides,
pubmed-meshheading:2540273-Bradykinin,
pubmed-meshheading:2540273-Calcium,
pubmed-meshheading:2540273-Dipeptides,
pubmed-meshheading:2540273-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2540273-Glioma,
pubmed-meshheading:2540273-Hybrid Cells,
pubmed-meshheading:2540273-Immunosorbent Techniques,
pubmed-meshheading:2540273-Iodine Radioisotopes,
pubmed-meshheading:2540273-Kallidin,
pubmed-meshheading:2540273-Molecular Structure,
pubmed-meshheading:2540273-Molecular Weight,
pubmed-meshheading:2540273-Neuroblastoma,
pubmed-meshheading:2540273-Peptide Hydrolases,
pubmed-meshheading:2540273-Peptidyl-Dipeptidase A,
pubmed-meshheading:2540273-Photolysis,
pubmed-meshheading:2540273-Receptors, Bradykinin,
pubmed-meshheading:2540273-Receptors, Neurotransmitter,
pubmed-meshheading:2540273-Tumor Cells, Cultured
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pubmed:year |
1989
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pubmed:articleTitle |
Construction of a physiologically active photoaffinity probe based on the structure of bradykinin: labelling of angiotensin converting enzyme but not candidate bradykinin receptors on NG108-15 cells.
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pubmed:affiliation |
Sandoz Institute for Medical Research, London, England.
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pubmed:publicationType |
Journal Article,
Comparative Study
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