{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T19:03:05Z","timestamp":1780599785214,"version":"3.54.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1996,5,15]]},"abstract":"<jats:p>The transforming growth factor \u03b2 (TGF-\u03b2) family of growth factors control proliferation, extracellular matrix synthesis and\/ or differentiation in a wide variety of cells. However, the molecular mechanisms governing ligand binding, receptor oligomerization and signal transduction remain incompletely understood. In this study, we utilized a set of antibodies selective for the extracellular and intracellular domains of the TGF-\u03b2 type-II receptor as probes to investigate the intrinsic kinase activity of this receptor and its physical association in multimeric complexes with type-I and type-III receptors. The type-II receptor immunoprecipitated from human osteosarcoma cells exhibited autophosphorylation and casein kinase activity that was markedly stimulated by polylysine yet was insensitive to heparin. Affinity cross-linking of 125I-TGF-\u03b21 ligand to cellular receptors followed by specific immunoprecipitation demonstrated that type-II receptors form stable complexes with both type-I and type-III receptors expressed on the surfaces of both human osteosarcoma cells and rabbit chondrocytes. Pretreatment of the cultured cells with an antibody directed against a distinct extracellular segment of the type-II receptor (anti-TGF-\u03b2-IIR-NT) effectively blocked the 125I-TGF-\u03b2 labelling of type-I receptors without preventing the affinity labelling of type-II or type-III receptors, indicating a selective disruption of the type-I\/type-II hetero-oligomers. The anti-TGF-\u03b2-IIR-NT antibodies also blocked the TGF-\u03b2-dependent induction of the plasminogen activator inhibitor (PAI-1) promoter observed in mink lung epithelial cells. However, the same anti-TGF-\u03b2-IIR-NT antibodies did not prevent the characteristic inhibition of cellular proliferation by TGF-\u03b21, as determined by [3H]thymidine incorporation into DNA. The selective perturbation of PAI-1 promoter induction versus cell-cycle-negative regulation suggests that strategic disruption of TGF-\u03b2 type-I and -II receptor interactions can effectively alter specific cellular responses to TGF-\u03b2 signalling.<\/jats:p>","DOI":"10.1042\/bj3160303","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:49:22Z","timestamp":1439243362000},"page":"303-310","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Transforming growth factor-<i>\u03b2<\/i> type-II receptor signalling: intrinsic\/associated casein kinase activity, receptor interactions and functional effects of blocking antibodies"],"prefix":"10.1042","volume":"316","author":[{"given":"Frederick L.","family":"HALL","sequence":"first","affiliation":[{"name":"Departments of Surgery and Pediatrics, Childrens Hospital Los Angeles Research Institute, Los Angeles, CA 90027, U.S.A."},{"name":"Department of Molecular Pharmacology and Toxicology, University of Southern California School of Pharmacy, Los Angeles, CA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul D.","family":"BENYA","sequence":"additional","affiliation":[{"name":"J. Vernon Luck Orthopedic Research Center, Orthopaedic Hospital of Los Angeles and Department of Orthopedics, University of Southern California School of Medicine, Los Angeles, CA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia R.","family":"PADILLA","sequence":"additional","affiliation":[{"name":"J. Vernon Luck Orthopedic Research Center, Orthopaedic Hospital of Los Angeles and Department of Orthopedics, University of Southern California School of Medicine, Los Angeles, CA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Denise","family":"CARBONARO-HALL","sequence":"additional","affiliation":[{"name":"Departments of Surgery and Pediatrics, Childrens Hospital Los Angeles Research Institute, Los Angeles, CA 90027, U.S.A."},{"name":"Department of Molecular Pharmacology and Toxicology, University of Southern California School of Pharmacy, Los Angeles, CA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"WILLIAMS","sequence":"additional","affiliation":[{"name":"Departments of Surgery and Pediatrics, Childrens Hospital Los Angeles Research Institute, Los Angeles, CA 90027, U.S.A."},{"name":"Department of Molecular Pharmacology and Toxicology, University of Southern California School of Pharmacy, Los Angeles, CA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sue","family":"BUCKLEY","sequence":"additional","affiliation":[{"name":"Departments of Surgery and Pediatrics, Childrens Hospital Los Angeles Research Institute, Los Angeles, CA 90027, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"WARBURTON","sequence":"additional","affiliation":[{"name":"Departments of Surgery and Pediatrics, Childrens Hospital Los Angeles Research Institute, Los Angeles, CA 90027, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/316\/1\/303\/620199\/bj3160303.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/316\/1\/303\/620199\/bj3160303.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T00:11:53Z","timestamp":1637712713000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/316\/1\/303\/32788\/Transforming-growth-factor-type-II-receptor"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,5,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1996,5,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3160303","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,5,15]]}}}