ArticleBritish journal of pharmacology1994
Bradykinin binding sites in healthy and carcinomatous human lung.
Article in British journal of pharmacology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 18 citations in OpenAlex.
- Minireview: functional roles of tissue kallikrein, kinins, and kallikrein-related peptidases in lung cancer.Medical oncology (Northwood, London, England) · 2023Review
- Characterization of the bradykinin receptor in the human nasal airway using the binding of [125I]-Hoe 140.British journal of pharmacology · 1996Article
- Pharmacological and functional characterization of bradykinin receptors in canine cultured tracheal epithelial cells.British journal of pharmacology · 1996Article
- Pharmacological characterization of bradykinin receptors in canine cultured tracheal smooth muscle cells.British journal of pharmacology · 1995Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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