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Bradykinin binding sites in healthy and carcinomatous human lung
Author(s) -
Trifilieff Alexandre,
Lach Estelle,
Dumont Pascal,
Gies JeanPierre
Publication year - 1994
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1994.tb14876.x
Subject(s) - bradykinin , kallidin , receptor , endocrinology , medicine , chemistry , squamous carcinoma , lung , bradykinin receptor , biology , carcinoma , kinin
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 [ 3 H]‐bradykinin to healthy lung membrane is time‐dependent and saturable with a K D value of 1.08 ± 0.18 n m and a B max 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, B max = 52.2 ± 3.3 fmol mg −1 protein ( P = 0.22) but the K D value is significantly higher 2.57 ± 0.40 n m ( P = 0.004). Similar measurements were obtained for adeno‐carcinoma tissue ( n = 3), K D = 2.80 ± 0.29 m m ( P = 0.001) and B max = 49.8 ± 2.1 fmol mg −1 protein ( P = 0.56). 3 In both healthy and squamous‐carcinoma preparations, bradykinin analogues displace [ 3 H]‐bradykinin binding with the following relative order of potency: Hoe 140 > bradykinin > kallidin > d ‐Arg 0 [Hyp 3 , d ‐Phe 7 ]bradykinin >>>des‐Arg 9 ‐bradykinin. Of the analogues used, bradykinin and d ‐Arg 0 [Hyp 3 , d ‐Phe 7 ]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 B 2 type.