{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T21:53:59Z","timestamp":1762898039791},"reference-count":28,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":6762,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1986,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The fate of <jats:sup>125<\/jats:sup>I\u2010labeled transforming growth factor\u2010\u03b2 (<jats:sup>125<\/jats:sup>I\u2010TGF\u03b2) after binding to its cells surface receptor has been investigated in BALB\/c 3T3 mouse fibroblasts. Binding of <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 to cellular receptors at 4\u00b0C is pH\u2010sensitive, being markedly decreased at pH &lt; 6. Most (\u223c 90%) of the <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 bound to cells at 4\u00b0C can be removed by a brief treatment with acidic medium but is converted into an acid\u2010resistant state rapidly after shifting the cells to 37\u00b0C. Cell\u2010bound <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 is degraded at 37\u00b0C and the degradation products are released into the medium. The lysosomotropic bases chloroquine, methylamine, and ammonium and the carboxylic ionophore monensin inhibit the degradation and release of <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 from the cells. Cells allowed to accumulate <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 intracellularly by the action of chloroquine or monensin were treated with the bifunctional agent disuccinimidyl suberate in the presence of detergent Triton X\u2010100; this treatment caused the cross\u2010linking of internalized <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 with the 280\u2010kilodalton TGF\u03b2 receptor component. Under conditions in which sustained binding and degradation of saturating <jats:sup>125<\/jats:sup>I\u2010TGF\u03b2 concentrations occurs, there is no marked decrease in the binding capacity of the cells even when protein synthesis is blocked with cycloheximide. These results indicate that after TGF\u03b2 binding the TGF\u03b2:receptor complex becomes rapidly internalized and that TGF\u03b2 is directed towards lysosomes where it is degraded and released. However, the cell surface is replenished with TGF\u03b2 receptors recycled after internalization or supplied by a large intracellular pool.<\/jats:p>","DOI":"10.1002\/jcp.1041280212","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T12:32:15Z","timestamp":1109421135000},"page":"216-222","source":"Crossref","is-referenced-by-count":72,"title":["Internalization of transforming growth factor\u2010\u03b2 and its receptor in BALB\/c 3T3 fibroblasts"],"prefix":"10.1002","volume":"128","author":[{"given":"Joan","family":"Massagu\u00e9","sequence":"first","affiliation":[]},{"given":"Brenda","family":"Kelly","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(85)90212-0"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(81)90340-8"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(83)90052-1"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"5313","DOI":"10.1073\/pnas.79.17.5312","article-title":"Serum contains a platelet\u2010derived transforming growth factor","volume":"79","author":"Childs C. 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