{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T10:18:18Z","timestamp":1760782698463},"reference-count":20,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":5454,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1990,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In previous autoradiographic studies on the sites of catabolism of rat serum albumin (RSA) in the rat, fibroblasts in skin and muscle were shown to accumulate degradation product from RSA labeled with the residualizing label dilactitol\u2010<jats:sup>125<\/jats:sup>I\u2010tyramine (<jats:sup>125<\/jats:sup>I\u2010DLT) (Strobel et al., 1986 J. Biol. Chem., <jats:italic>261:<\/jats:italic>7989\u20147994). Residualizing labels remain at the cellular site of degradation of the carrier protein because of their size, hydrophilicity, and resistance to lysosomal hydrolases. This study was designed to evaluate whether fibroblasts might retain labeled degradation products more efficiently than other cell types. The uptake of <jats:sup>125<\/jats:sup>I\u2010DLT\u2010RSA and release of its degradation products and of a second non\u2010biodegradable probe, fluorescein isothiocyanate (FITC)\u2010dextran, were studied in fibroblasts, endothelial cells, and macrophages, all cell types previously implicated in the catabolism of albumin in vivo. The rates of uptake of labeled protein and dextran were comparable in all cell types and consistent with fluid phase endocytosis. The rate of release of both intact protein (30\u201435% of total radioactivity released) and radioactively labeled degradation products followed similar kinetics and had half\u2010lives ranging from 26 to 37 hr. The rate of release of FITC\u2010dextran was slower than that of radioactivity, with a half\u2010life of 42\u2014125 hr. Thus, although there were differences between the rates of release of the fluorescent and radioactive materials in vitro, there were no significant differences in the disposition of protein\u2010derived catabolites among these three cell types.<\/jats:p>","DOI":"10.1002\/jcp.1041420318","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T09:56:21Z","timestamp":1109411781000},"page":"581-585","source":"Crossref","is-referenced-by-count":4,"title":["Intracellular processing of residualizing labels in different cell types in vitro"],"prefix":"10.1002","volume":"142","author":[{"given":"Karen L.","family":"Lucas","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John W.","family":"Baynes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Suzanne R.","family":"Thorpe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(88)90647-1"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.85.3.660"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.91.3.716"},{"key":"e_1_2_1_5_1","doi-asserted-by":"crossref","first-page":"9469","DOI":"10.1016\/S0021-9258(18)47957-4","article-title":"Degradation and regurgitation of extracellular proteins by cultured mouse peritoneal macrophages and baby hamster kidney fibroblasts","volume":"262","author":"Buktenica S.","year":"1987","journal-title":"J. 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