| pubmed-article:8113404 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8113404 | lifeskim:mentions | umls-concept:C0032143 | lld:lifeskim |
| pubmed-article:8113404 | lifeskim:mentions | umls-concept:C2717940 | lld:lifeskim |
| pubmed-article:8113404 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:8113404 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8113404 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:8113404 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8113404 | pubmed:dateCreated | 1994-3-30 | lld:pubmed |
| pubmed-article:8113404 | pubmed:abstractText | The glycoprotein tissue-type plasminogen activator (t-PA) is subject to hepatic clearance in humans. Here, the interaction of t-PA with a well-differentiated hepatoma cell line (HepG2) was examined. Suspended HepG2 cells bound 125I-t-PA in a specific, saturable, and reversible fashion through a Ca(2+)-dependent, active site-independent mechanism. Binding isotherms indicated a high affinity system with a single class of saturable binding sites (Kd 39 nM; maximum binding capacity 493,000 sites per cell). Bound t-PA was rapidly degraded at 37 degrees C in a manner inhibited by lysosomotropic agents or metabolic inhibitors. Pretreatment of t-PA with monoclonal antibodies against the EGF/fibronectin finger domain, but not kringle 2 or kringle 1, reduced total binding by 86%. Binding of 125I-t-PA to HepG2 cells was inhibited by monosaccharides fucose and galactose and by the neoglycoprotein fucosyl-albumin. Enzymatic removal of alpha-fucose residues, but not alpha-galactose, high mannose, or complex oligosaccharide from 125I-t-PA, reduced specific binding by 60 +/- 5%. Binding was also inhibited by high, but not low, molecular weight urokinase, which contains an EGF-based threonine-linked alpha-fucose homologous to that of t-PA. These data suggest that EGF-associated O-linked alpha-fucose may mediate t-PA binding and degradation by HepG2 cells. This mechanism may be relevant to other proteins with analogous structures. | lld:pubmed |
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| pubmed-article:8113404 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8113404 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8113404 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:8113404 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8113404 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8113404 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8113404 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:8113404 | pubmed:author | pubmed-author:ReynoldsC MCM | lld:pubmed |
| pubmed-article:8113404 | pubmed:author | pubmed-author:HajjarK AKA | lld:pubmed |
| pubmed-article:8113404 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8113404 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8113404 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8113404 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8113404 | pubmed:pagination | 703-10 | lld:pubmed |
| pubmed-article:8113404 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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