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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-12-8
pubmed:abstractText
Tissue factor pathway inhibitor (TFPI) is a primary regulator of the initiation of blood coagulation. TFPI is internalized and degraded by HepG2 cells through the low-density-lipoprotein receptor-related protein (LRP) but also binds another molecule present on the cell surface at approx. 10-fold the abundance of LRP [Warshawsky, Broze and Schwartz (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 6664-6668]. When HepG2 cells are washed with heparin or dextran sulphate, a substance that binds TFPI is removed from the cell surface and can be detected in a slot-blot assay. Preincubation with trypsin destroys the reactivity of the TFPI-binding component in the slot-blot assay, suggesting that it is a protein. In addition, when the sulphation of glycosaminoglycans (GAGs) is prevented by growing the HepG2 cells in the presence of 30 mM sodium chlorate, TFPI binding is unaffected, whereas the binding of bovine lipoprotein lipase, a protein known to associate with cell-surface GAGs, falls to 50% of control levels. Dextran sulphate washes of HepG2 cells grown in sodium chlorate have an equal reactivity in slot-blot experiments to that of non-treated cells, suggesting that GAGs are not totally responsible for the binding activity observed. By using the slot blot to follow binding activity and conventional protein purification techniques, a protein species that migrates at 40 kDa after reduction was identified in the HepG2 cell wash. The binding of this protein to TFPI was confirmed with immobilized TFPI. Amino acid sequence analysis identified this protein species as a proteolytic fragment of glypican-3 (also called OCI-5), a member of the glypican family of glycosylphosphatidylinositol-anchored proteoglycans.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-1420819, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-1514170, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-1562726, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-1885587, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2070076, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2070077, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2148568, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2521485, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2827342, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2927510, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-2951371, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-3026396, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-3031657, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-3185547, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-3413731, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-6448850, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7487896, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7517557, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7592967, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7657705, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7691821, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7706485, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-7841311, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8259548, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8280090, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8292716, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8294498, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8589713, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8609163, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8621621, http://linkedlifedata.com/resource/pubmed/commentcorrection/9359432-8948051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chlorates, http://linkedlifedata.com/resource/pubmed/chemical/Dextran Sulfate, http://linkedlifedata.com/resource/pubmed/chemical/Fibrinolytic Agents, http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans, http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols, http://linkedlifedata.com/resource/pubmed/chemical/Glypicans, http://linkedlifedata.com/resource/pubmed/chemical/Heparan Sulfate Proteoglycans, http://linkedlifedata.com/resource/pubmed/chemical/Heparin, http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate, http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin, http://linkedlifedata.com/resource/pubmed/chemical/lipoprotein-associated coagulation..., http://linkedlifedata.com/resource/pubmed/chemical/sodium chlorate
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
327 ( Pt 2)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
577-83
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9359432-Humans, pubmed-meshheading:9359432-Animals, pubmed-meshheading:9359432-Cattle, pubmed-meshheading:9359432-Heparin, pubmed-meshheading:9359432-Trypsin, pubmed-meshheading:9359432-Chlorates, pubmed-meshheading:9359432-Peptide Fragments, pubmed-meshheading:9359432-Lipoproteins, pubmed-meshheading:9359432-Kinetics, pubmed-meshheading:9359432-Fibrinolytic Agents, pubmed-meshheading:9359432-Glycosaminoglycans, pubmed-meshheading:9359432-Lipoprotein Lipase, pubmed-meshheading:9359432-Cell Membrane, pubmed-meshheading:9359432-Tumor Cells, Cultured, pubmed-meshheading:9359432-Amino Acid Sequence, pubmed-meshheading:9359432-Binding Sites, pubmed-meshheading:9359432-Molecular Sequence Data, pubmed-meshheading:9359432-Carrier Proteins, pubmed-meshheading:9359432-Cloning, Molecular, pubmed-meshheading:9359432-Sequence Alignment, pubmed-meshheading:9359432-Chromatography, Affinity, pubmed-meshheading:9359432-Heparitin Sulfate
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