Gastrin releasing peptide-preferring bombesin binding sites in human lung.
Characterization of bombesin binding sites in healthy human lung was performed through direct binding techniques. There was limited binding in the absence of trypsin and chymotrypsin inhibitors, suggesting important activities of both enzymes in human lung and/or increased sensitivity of the bombesin sites toward them. In human lung membranes, bombesin, gastrin releasing peptide (GRP) and GRP-preferring bombesin receptor antagonists displaced [125I-Tyr4]bombesin binding with high affinities (36-177 nM), whereas neuromedin B possessed a lower affinity of 2878 nM. [D-F5Phe6,D-Ala11]bombesin-(6-13)-methyl ester, the most active GRP-preferring bombesin antagonist as yet reported, had the highest affinity among all antagonists tested whereas neuromedin B had the lowest affinity. These data demonstrate that the bombesin binding sites in the human lung are of the GRP-preferring type.
Lach
E
E
Laboratoire de Neuroimmunopharmacologie Pulmonaire, INSERM CJF 9105, Université Louis Pasteur-Strasbourg I, Faculté de Pharmacie, Illkirch, France.
Coy
D H
DH
Dumont
P
P
Landry
Y
Y
Gies
J P
JP
D001665:Binding Sites; D001667:Binding, Competitive; D001839:Bombesin / Q000031:analogs & derivatives / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002277:Carcinoma / Q000378:metabolism / Q000601:surgery; D019886:Gastrin-Releasing Peptide; D006801:Humans; D008168:Lung / Q000187:drug effects / Q000378:metabolism*; D008175:Lung Neoplasms / Q000378:metabolism / Q000601:surgery; D015287:Neurokinin B / Q000031:analogs & derivatives / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D010455:Peptides / Q000378:metabolism* / Q000494:pharmacology
D010446:Peptide Fragments; D010455:Peptides; C071101:bombesin (6-13), Phe(6) methyl ester-; C035891:bombesin, Tyr(4)-; D019886:Gastrin-Releasing Peptide; D015287:Neurokinin B; C038393:neuromedin B; D001839:Bombesin