{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T11:59:35Z","timestamp":1791115175538,"version":"4.1.0"},"reference-count":26,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":6519,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1987,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Scatchard analysis of binding of <jats:sup>125<\/jats:sup>l\u2010basic fibroblast growth factor (FGF) to baby hamster kidney (BHK) cells revealed the presence of two binding sites: a high affinity site with K<jats:sub>D<\/jats:sub> of 20 pM and 80,000 sites per cell and a low affinity site with K<jats:sub>D<\/jats:sub> of about 2 nM and 600,000 sites per cell. The binding to the two sites could be separated by first washing the cells with 2 M NaCl at pH 7.5 which released the low affinity binding and then extracting the cells with 0.5% Triton X\u2010100 to recover the <jats:sup>125<\/jats:sup>l\u2010basic FGF bound to high affinity sites. The binding to the high affinity site was acid sensitive, suggesting that it represented binding to the receptor. Binding to the low affinity site could be competed strongly by heparin and less strongly by heparan sulfate but not by chondroitin sulfate, dermatan sulfate, or keratan sulfate. Treatment of BHK cells with heparinase abolished 62% of the low affinity binding, suggesting that the low affinity binding represented binding to cell\u2010associated, heparin\u2010like molecules. A variety of other cell types, including bovine capillary endothelial (BCE) cells, also demonstrated both low and high affinity binding sites. To test whether the low affinity binding might play a role in the basic FGF stimulation of plasminogen activator (PA) production by BCE cells, heparin was added to BCE cultures at concentrations which totally blocked binding of <jats:sup>125<\/jats:sup>l\u2010basic FGF to the low affinity sites. Addition of the heparin did not diminish the increased PA production induced by basic FGF. This suggests that the low affinity binding has no direct role in the stimulation of PA production in BCE cells.<\/jats:p>","DOI":"10.1002\/jcp.1041310118","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T11:43:39Z","timestamp":1109418219000},"page":"123-130","source":"Crossref","is-referenced-by-count":502,"title":["High and low affinity binding sites for basic fibroblast growth factor on cultured cells: Absence of a role for low affinity binding in the stimulation of plasminogen activator production by bovine capillary endothelial cells"],"prefix":"10.1002","volume":"131","author":[{"given":"David","family":"Moscatelli","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)34650-7"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(78)91316-5"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.19.6507"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1720443"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/249123a0"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.22.6963"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1041270116"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.95.3.974"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1041270220"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.23.8044"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00321a001"},{"key":"e_1_2_1_14_1","doi-asserted-by":"crossref","first-page":"7507","DOI":"10.1016\/S0021-9258(17)38421-1","article-title":"Cloned bovine aortic endothelial cells synthesize anticoagulantly active heparan sulfate proteoglycan","volume":"261","author":"Marcum J. 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