{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,26]],"date-time":"2023-10-26T05:04:44Z","timestamp":1698296684169},"reference-count":32,"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":3475,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1995,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>A 39 kDa protein copurifies with the low density lipoprotein receptor\u2010related protein (LRP) and regulates ligand interactions with LRP. In our recent studies on the clearance of the 39 kDa protein in vivo, we demonstrated that once the liver LRP receptors were saturated, the kidney necame the major organ responsible for the 39 kDa protein clearance (Warshawsky et al., 1993, J. Clin. Invest., 92:937\u2010944). The current study was undertaken in order to investigate the potential binding and cellular processing of the 39 kDa protein by kidney\u2010derived MDBK cells. Herein we demonstrate specific, high\u2010affinity, saturable, and Ca<jats:sup>2+<\/jats:sup>\u2010dependent binding of the <jats:sup>125<\/jats:sup>I\u201039 kDa protein to MDBK cells (K<jats:sub>d<\/jats:sub> \u223c 10\u201015 nM, 50\u201070,000 bindings sites per cell). Cellular uptake and degradation of the <jats:sup>125<\/jats:sup>I\u201039 kDa protein by MDBK cells was also demonstrated with kinetics typical of receptor\u2010mediated endocytosis. Using chemical crosslinking we show that LRP in part mediates the binding of <jats:sup>125<\/jats:sup>I\u201039 kDa protein to the MDBK cell surface. In addition, the presence of functional LRP on the MDBK cell surface was confirmed by the specific binding of activated \u03b1<jats:sub>2<\/jats:sub>\u2010macroglobulin, another ligand of LRP. Our data thus demonstrate the ability of kidney\u2010derived MDBK cells to specifically bind, endocytose, and degrade the 39 kDa protein. \u00a9 1995 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcp.1041640225","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T04:33:51Z","timestamp":1109392431000},"page":"441-447","source":"Crossref","is-referenced-by-count":1,"title":["Binding and endocytosis of 39 kDa protein by mdbk cells"],"prefix":"10.1002","volume":"164","author":[{"given":"Kim","family":"Vettenranta","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guojun","family":"Bu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alan L.","family":"Schwartz","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":"10.1083\/jcb.110.4.1041"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/341162a0"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.19.8342"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1097\/00041433-199104000-00002"},{"key":"e_1_2_1_6_1","first-page":"259","volume-title":"The Liver: Biology and Pathobiology","author":"Bu G.","year":"1994"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.16.7427"},{"key":"e_1_2_1_8_1","doi-asserted-by":"crossref","first-page":"15595","DOI":"10.1016\/S0021-9258(19)49578-1","article-title":"Identification and partial characterization by chemical crosslinking of a binding protein for tissue\u2010type plasminogen activator (t\u2010PA) on rat hepatoma cells: A plasminogen activator inhibitor\u2010type 1 independent t\u2010PA receptor","volume":"267","author":"Bu G.","year":"1992","journal-title":"J. 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