{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,14]],"date-time":"2026-04-14T15:03:41Z","timestamp":1776179021523,"version":"3.50.1"},"reference-count":0,"publisher":"American Society for Cell Biology (ASCB)","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[1992,11]]},"abstract":"<jats:p> Transforming growth factor-beta (TGF-beta) is a potential mediator of placental trophoblast functions, including differentiation, hormone production, endometrial invasion, and immunosuppression. Equilibrium binding and affinity-labeling assays were used to investigate the binding characteristics of TGF-beta 1 and TGF-beta 2 on an established human choriocarcinoma trophoblastic cell line (BeWo). The equilibrium binding experiments indicated that the BeWo cells exhibited similar average affinities and total number of binding sites for TGF-beta 1 and TGF-beta 2. The Kd values obtained from Scatchard analyses were approximately 65 pM for 125I-TGF-beta 1 and approximately 40 pM for 125I-TGF-beta 2, with 70,000 and 85,000 sites per cell, respectively. Competitive equilibrium binding experiments indicated that TGF-beta 1 and TGF-beta 2 were equipotent (apparent half maximal inhibition [IC50] approximately 70 pM) and that all binding sites were capable of recognizing both isoforms. Affinity-labeling studies with 125I-TGF-beta 1 and 125I-TGF-beta 2 and the chemical cross-linking agent bis(sulfosuccinimidyl)suberate (BS3) revealed a predominant type III\/betaglycan receptor, a low level of apparently heterogeneous type I and II receptors and an additional novel 38-kDa TGF-beta binding glycoprotein that was present both under reducing and nonreducing conditions on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Affinity-labeling saturation and competition studies indicated that the type III\/betaglycan component appears to have a 7-fold higher capacity for TGF-beta 1 than for -beta 2 yet exhibits a 5- to 10-fold higher affinity for TGF-beta 2 than for -beta 1. The 38-kDa TGF-beta binding component, an N-linked glycoprotein, exhibits a higher affinity for TGF-beta 2 than for -beta 1 that is strikingly similar to that of the type III\/betaglycan receptor. This 38-kDa binding protein appears to be upregulated after methotrexate-induced differentiation of the BeWo cells. <\/jats:p>","DOI":"10.1091\/mbc.3.11.1295","type":"journal-article","created":{"date-parts":[[2013,8,16]],"date-time":"2013-08-16T18:48:41Z","timestamp":1376678921000},"page":"1295-1307","source":"Crossref","is-referenced-by-count":23,"title":["Characterization of transforming growth factor-beta (TGF-beta) receptors on BeWo choriocarcinoma cells including the identification of a novel 38-kDa TGF-beta binding glycoprotein."],"prefix":"10.1091","volume":"3","author":[{"given":"E J","family":"Mitchell","sequence":"first","affiliation":[{"name":"Biotechnology Research Institute, National Research Council, Canada, Montreal, Quebec."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K","family":"Lee","sequence":"additional","affiliation":[{"name":"Biotechnology Research Institute, National Research Council, Canada, Montreal, Quebec."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M D","family":"O'Connor-McCourt","sequence":"additional","affiliation":[{"name":"Biotechnology Research Institute, National Research Council, Canada, Montreal, Quebec."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1076","container-title":["Molecular Biology of the Cell"],"original-title":[],"language":"en","deposited":{"date-parts":[[2019,7,14]],"date-time":"2019-07-14T09:01:08Z","timestamp":1563094868000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.molbiolcell.org\/doi\/10.1091\/mbc.3.11.1295"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,11]]},"references-count":0,"journal-issue":{"issue":"11","published-print":{"date-parts":[[1992,11]]}},"alternative-id":["10.1091\/mbc.3.11.1295"],"URL":"https:\/\/doi.org\/10.1091\/mbc.3.11.1295","relation":{},"ISSN":["1059-1524","1939-4586"],"issn-type":[{"value":"1059-1524","type":"print"},{"value":"1939-4586","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,11]]}}}