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Effect of Hoe 140, a new B2 noncompetitive antagonist, on guinea pig tracheal bradykinin receptors.
J Pharmacol Exp Ther. 1992 Dec; 263(3):1377-82.JP

Abstract

We investigated the effect of the new B2 antagonist D-Arg0[Hyp3,Thi5, D-Tic7, Oic8]bradykinin (BK) (Hoe 140) on the binding of [3H]BK to membranes from guinea pig trachea with respect to the presence of the epithelium. Scatchard analysis of equilibrium data with [3H]BK revealed a single class of binding sites in the epithelium denuded trachea membrane preparation (E-) with a dissociation constant (Kd) of 55 pM and a Bmax of 0.71 fmol.mg tissue-1. When intact trachea (E+) was used, two binding sites were detected: a saturable high-affinity one (Kd of 40 pM and Bmax of 0.69 fmol.mg tissue-1) and a low-affinity one, not really saturable, with a Kd over 180 nM and a Bmax over 18 fmol.mg tissue-1. In guinea pig ileum, a tissue thought to contain B2 receptors, one class of binding sites was detected with a Kd of 209.3 pM and a Bmax of 16.2 fmol.mg tissue-1. In competition experiments ([3H]BK from 0.3 to 0.5 nM), similar results were obtained in (E +/-) and in ileum membrane preparations. B1 ligands did not displace [3H]BK binding, demonstrating the lack of B1 receptors. BK and B2 antagonist, except Hoe 140, fully displaced [3H]BK with Hill coefficients close to the unity. In competition studies only the high-affinity site was labeled by [3H]BK, in the (E+) preparation, as suggested by the inhibition constant value of unlabeled BK. Hoe 140 fully displaced [3H]BK in competition experiments, but with a Hill coefficient significantly less than unity, suggesting the presence of two binding sites for this compound in the three preparations used.(ABSTRACT TRUNCATED AT 250 WORDS)

Authors+Show Affiliations

Laboratoire de Neuroimmunopharmacologie, Université Louis Pasteur Strasbourg I, Illkirch, France.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

1335064

Citation

Trifilieff, A, et al. "Effect of Hoe 140, a New B2 Noncompetitive Antagonist, On Guinea Pig Tracheal Bradykinin Receptors." The Journal of Pharmacology and Experimental Therapeutics, vol. 263, no. 3, 1992, pp. 1377-82.
Trifilieff A, Da Silva A, Landry Y, et al. Effect of Hoe 140, a new B2 noncompetitive antagonist, on guinea pig tracheal bradykinin receptors. J Pharmacol Exp Ther. 1992;263(3):1377-82.
Trifilieff, A., Da Silva, A., Landry, Y., & Gies, J. P. (1992). Effect of Hoe 140, a new B2 noncompetitive antagonist, on guinea pig tracheal bradykinin receptors. The Journal of Pharmacology and Experimental Therapeutics, 263(3), 1377-82.
Trifilieff A, et al. Effect of Hoe 140, a New B2 Noncompetitive Antagonist, On Guinea Pig Tracheal Bradykinin Receptors. J Pharmacol Exp Ther. 1992;263(3):1377-82. PubMed PMID: 1335064.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Effect of Hoe 140, a new B2 noncompetitive antagonist, on guinea pig tracheal bradykinin receptors. AU - Trifilieff,A, AU - Da Silva,A, AU - Landry,Y, AU - Gies,J P, PY - 1992/12/1/pubmed PY - 1992/12/1/medline PY - 1992/12/1/entrez SP - 1377 EP - 82 JF - The Journal of pharmacology and experimental therapeutics JO - J Pharmacol Exp Ther VL - 263 IS - 3 N2 - We investigated the effect of the new B2 antagonist D-Arg0[Hyp3,Thi5, D-Tic7, Oic8]bradykinin (BK) (Hoe 140) on the binding of [3H]BK to membranes from guinea pig trachea with respect to the presence of the epithelium. Scatchard analysis of equilibrium data with [3H]BK revealed a single class of binding sites in the epithelium denuded trachea membrane preparation (E-) with a dissociation constant (Kd) of 55 pM and a Bmax of 0.71 fmol.mg tissue-1. When intact trachea (E+) was used, two binding sites were detected: a saturable high-affinity one (Kd of 40 pM and Bmax of 0.69 fmol.mg tissue-1) and a low-affinity one, not really saturable, with a Kd over 180 nM and a Bmax over 18 fmol.mg tissue-1. In guinea pig ileum, a tissue thought to contain B2 receptors, one class of binding sites was detected with a Kd of 209.3 pM and a Bmax of 16.2 fmol.mg tissue-1. In competition experiments ([3H]BK from 0.3 to 0.5 nM), similar results were obtained in (E +/-) and in ileum membrane preparations. B1 ligands did not displace [3H]BK binding, demonstrating the lack of B1 receptors. BK and B2 antagonist, except Hoe 140, fully displaced [3H]BK with Hill coefficients close to the unity. In competition studies only the high-affinity site was labeled by [3H]BK, in the (E+) preparation, as suggested by the inhibition constant value of unlabeled BK. Hoe 140 fully displaced [3H]BK in competition experiments, but with a Hill coefficient significantly less than unity, suggesting the presence of two binding sites for this compound in the three preparations used.(ABSTRACT TRUNCATED AT 250 WORDS) SN - 0022-3565 UR - https://www.unboundmedicine.com/medline/citation/1335064/Effect_of_Hoe_140_a_new_B2_noncompetitive_antagonist_on_guinea_pig_tracheal_bradykinin_receptors_ L2 - https://jpet.aspetjournals.org/cgi/pmidlookup?view=long&pmid=1335064 DB - PRIME DP - Unbound Medicine ER -