{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T22:26:35Z","timestamp":1759616795492},"reference-count":0,"publisher":"Canadian Science Publishing","issue":"6","license":[{"start":{"date-parts":[[1991,6,1]],"date-time":"1991-06-01T00:00:00Z","timestamp":675734400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Can. J. Physiol. Pharmacol."],"published-print":{"date-parts":[[1991,6,1]]},"abstract":"<jats:p> Binding of [<jats:sup>125<\/jats:sup>I-Tyr<jats:sup>8<\/jats:sup>]bradykinin (BK) was measured in homogenates of epithelial and smooth muscle layers of the guinea pig ileum. Binding assays were performed at 4 \u00b0C for 40\u2002min (smooth muscle) or 90\u2002min (epithelium) in 25\u2002mM PIPES buffer at pH 6.8 in the presence of 1\u2002mM 1,10-phenanthroline, 140\u2002\u03bcg\/mL bacitracin, 1\u2002mM captopril, 1\u2002mM dithiothreitol, and 0.1% bovine serum albumin. Specific binding of [<jats:sup>125<\/jats:sup>I-Tyr<jats:sup>8<\/jats:sup>]BK (0.32\u2002nM) to epithelial and smooth muscle cell membranes was linearly related to protein concentration between 0.05 and 0.5\u2002mg\/mL. Equilibrium experiments showed that specific binding of [<jats:sup>125<\/jats:sup>I-Tyr<jats:sup>8<\/jats:sup>]BK was saturable and Scatchard analysis indicated the presence of a high affinity site with a K<jats:sub>d<\/jats:sub> value of 1.6\u2002nM and a B<jats:sub>max<\/jats:sub>. of 156\u2002fmol\/mg of protein in the epithelial cell membranes. In smooth muscle membranes, K<jats:sub>d<\/jats:sub> was 1.8\u2002nM and the maximum number of binding sites was 58\u2002fmol\/mg of protein. Unlabelled peptides, namely bradykinin, [Tyr<jats:sup>8<\/jats:sup>]BK, [Hyp<jats:sup>3<\/jats:sup>]BK, D-Arg[Hyp<jats:sup>3<\/jats:sup>]BK, [Hyp<jats:sup>3<\/jats:sup>,Tyr(Me<jats:sup>8<\/jats:sup>)]BK, and kallidin displaced [<jats:sup>125<\/jats:sup>I-Tyr<jats:sup>8<\/jats:sup>]BK binding while other peptides, angiotensin II and substance P, had no effect. A series of B<jats:sub>2<\/jats:sub>-receptor antagonists displaced [<jats:sup>125<\/jats:sup>I-Tyr<jats:sup>8<\/jats:sup>]BK from specific binding sites with IC<jats:sub>50<\/jats:sub> values ranging from 16 to 152\u2002nM on epithelial cell membranes; similar values were obtained from smooth muscle cell membranes. These findings suggest that the binding sites in both preparations are of the B<jats:sub>2<\/jats:sub> type. B<jats:sub>1<\/jats:sub>-receptor agonists and antagonists were found to be inactive at concentrations up to 10<jats:sup>\u22124<\/jats:sup>\u2002M. Results obtained in the two preparations were compared and a positive highly significant correlation was demonstrated between the two sets of data. It is therefore concluded that B<jats:sub>2<\/jats:sub> receptors found in the epithelium and the smooth muscle membranes of the guinea pig ileum are identical. These sites are similar to the functional receptor mediating the myotropic effect of bradykinin in the ileum.Key words: kinins, epithelium, smooth muscle, guinea pig ileum, binding and biological assays. <\/jats:p>","DOI":"10.1139\/y91-123","type":"journal-article","created":{"date-parts":[[2011,4,24]],"date-time":"2011-04-24T08:58:18Z","timestamp":1303635498000},"page":"818-825","source":"Crossref","is-referenced-by-count":18,"title":["Characterization of kinin binding sites: identity of B<sub>2<\/sub> receptors in the epithelium and the smooth muscle of the guinea pig ileum"],"prefix":"10.1139","volume":"69","author":[{"given":"C.","family":"Tousignant","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Guillemette","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Barab\u00e9","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N.-E.","family":"Rhaleb","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.","family":"Regoli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"155","container-title":["Canadian Journal of Physiology and Pharmacology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/pdf\/10.1139\/y91-123","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,1,5]],"date-time":"2020-01-05T15:23:58Z","timestamp":1578237838000},"score":1,"resource":{"primary":{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/10.1139\/y91-123"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,6,1]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1991,6,1]]}},"alternative-id":["10.1139\/y91-123"],"URL":"https:\/\/doi.org\/10.1139\/y91-123","relation":{},"ISSN":["0008-4212","1205-7541"],"issn-type":[{"value":"0008-4212","type":"print"},{"value":"1205-7541","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,6,1]]}}}