Biomaterial Database

Bradykinin binding sites in healthy and carcinomatous human lung. 1994

A Trifilieff, and E Lach, and P Dumont, and J P Gies

Laboratoire de Neuroimmunopharmacologie-Pulmonaire INSERM CJF-9105, Université Louis Pasteur-Strasbourg I, Illkirch, France.

1. Direct ligand binding techniques have been used to compare bradykinin receptors in squamous- or adeno-carcinoma and healthy lung membranes removed from patients during operations. 2. The binding of [3H]-bradykinin to healthy lung membrane is time-dependent and saturable with a KD value of 1.08 +/- 08 nM and a Bmax value of 46.1 +/- 3.1 fmol mg-1 protein (n = 10). In squamous-carcinoma tissue (n = 8) the same amount of receptors are present, Bmax = 52.2 +/- 3.3 fmol mg-1 protein (P = 0.22) but the KD value is significantly higher 2.57 +/- 0.40 nM (P = 0.004). Similar measurements were obtained for adeno-carcinoma tissue (n = 3), KD = 2.80 +/- 0.29 mM (P = 0.001) and Bmax = 49.8 +/- 2.1 fmol mg-1 protein (P = 0.56). 3. In both healthy and squamous-carcinoma preparations, bradykinin analogues displace [3H]-bradykinin binding with the following relative order of potency: Hoe 140 > bradykinin > kallidin > D-Arg0[Hyp3,D-Phe7]bradykinin >>> des-Arg9-bradykinin. Of the analogues used, bradykinin and D-Arg0[Hyp3,D-Phe7]bradykinin appear to be able to differentiate the bradykinin receptors present in both preparations. 4. It is concluded that bradykinin receptors present in healthy and carcinomatous human lung are of the B2 type.

UI	MeSH Term	Description	Entries
D008168	Lung	Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.	Lungs
D008175	Lung Neoplasms	Tumors or cancer of the LUNG.	Cancer of Lung,Lung Cancer,Pulmonary Cancer,Pulmonary Neoplasms,Cancer of the Lung,Neoplasms, Lung,Neoplasms, Pulmonary,Cancer, Lung,Cancer, Pulmonary,Cancers, Lung,Cancers, Pulmonary,Lung Cancers,Lung Neoplasm,Neoplasm, Lung,Neoplasm, Pulmonary,Pulmonary Cancers,Pulmonary Neoplasm
D001920	Bradykinin	A nonapeptide messenger that is enzymatically produced from KALLIDIN in the blood where it is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from MAST CELLS during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter.	Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg,Bradykinin Acetate, (9-D-Arg)-Isomer,Bradykinin Diacetate,Bradykinin Hydrochloride,Bradykinin Triacetate,Bradykinin, (1-D-Arg)-Isomer,Bradykinin, (2-D-Pro)-Isomer,Bradykinin, (2-D-Pro-3-D-Pro-7-D-Pro)-Isomer,Bradykinin, (2-D-Pro-7-D-Pro)-Isomer,Bradykinin, (3-D-Pro)-Isomer,Bradykinin, (3-D-Pro-7-D-Pro)-Isomer,Bradykinin, (5-D-Phe)-Isomer,Bradykinin, (5-D-Phe-8-D-Phe)-Isomer,Bradykinin, (6-D-Ser)-Isomer,Bradykinin, (7-D-Pro)-Isomer,Bradykinin, (8-D-Phe)-Isomer,Bradykinin, (9-D-Arg)-Isomer,Arg Pro Pro Gly Phe Ser Pro Phe Arg
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D018002	Receptors, Bradykinin	Cell surface receptors that bind BRADYKININ and related KININS with high affinity and trigger intracellular changes which influence the behavior of cells. The identified receptor types (B-1 and B-2, or BK-1 and BK-2) recognize endogenous KALLIDIN; t-kinins; and certain bradykinin fragments as well as bradykinin itself.	Bradykinin Receptors,Bradykinin Receptor,Receptor, Bradykinin