| pubmed-article:2119264 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C0163275 | lld:lifeskim |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C0302148 | lld:lifeskim |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C0024348 | lld:lifeskim |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C0014441 | lld:lifeskim |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C0079809 | lld:lifeskim |
| pubmed-article:2119264 | lifeskim:mentions | umls-concept:C2349101 | lld:lifeskim |
| pubmed-article:2119264 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2119264 | pubmed:dateCreated | 1990-10-26 | lld:pubmed |
| pubmed-article:2119264 | pubmed:abstractText | Concentrations of cross-linked fibrin degradation products (XL-FDPs) in plasma, measured by enzyme-linked immunosorbent assays (ELISAs) based on monoclonal antibodies (MAbs) raised against fragment D-dimer of cross-linked fibrin, increase when patients are given fibrinolytic agents. Whether XL-FDPs derive from circulating cross-linked fibrin polymers in plasma, compared with clot-associated fibrin, has been questioned because increases in XL-FDP are measured by some assays after fibrinolysis in vitro in the absence of clot. We characterized the source of XL-FDP immunoreactivity in plasma of patients with acute myocardial infarction and ischemic heart disease and the response to plasminogen activation in vitro induced by pharmacological concentrations of tissue-type plasminogen activator (t-PA) and streptokinase. XL-FDPs were measured with two different ELISA. One, "pan-specific tag ELISA," was based on a capture MAb specific for XL-FDP and a tag MAb that recognizes an epitope exposed in the fragment D region of both fibrin and fibrinogen, whereas the other, "fibrin-specific tag ELISA," was based on a capture and tag MAbs both specific for fibrin. After plasminogen activation was induced in vitro in plasma from patients with myocardial infarction, increased concentrations of XL-FDP were measured by the pan-specific tag ELISA; however, concentrations measured with the fibrin-specific tag ELISA were not increased. To determine the mechanism for this discrepancy, plasma was subjected to immunoadsorption with a MAb specific for fragment D-dimer before and after in vitro activation of the fibrinolytic system and immunoblotting with a fragment D-dimer-specific MAb and with the pan-specific MAb. Increased concentrations of fragment D-dimer, as well as fibrinogen fragment D at high concentrations, were recognized by the specific MAb. Non-cross-linked fragments were also shown by immunoblotting with the pan-specific MAb to coprecipitate with cross-linked fibrin fragments. This suggested the increased concentrations of XL-FDP measured by the pan-specific tag ELISA after in vitro activation of the fibrinolytic system were due to detection of non-cross-linked fibrinogen fragments. However, fibrin fragment D-dimer concentrations were found to increase in plasma of 15 patients given t-PA for acute myocardial infarction. We conclude fragment D-dimer in plasma of patients during thrombolysis does not originate from circulating soluble cross-linked fibrin but rather is a marker of solid-phase fibrin dissolution, which may be quantitated with assays based on capture and tag antibodies that do not detect fibrinogen or its degradation products. | lld:pubmed |
| pubmed-article:2119264 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2119264 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:2119264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2119264 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2119264 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2119264 | pubmed:issn | 0009-7322 | lld:pubmed |
| pubmed-article:2119264 | pubmed:author | pubmed-author:CollenDD | lld:pubmed |
| pubmed-article:2119264 | pubmed:author | pubmed-author:JaffeA SAS | lld:pubmed |
| pubmed-article:2119264 | pubmed:author | pubmed-author:BovillE GEG | lld:pubmed |
| pubmed-article:2119264 | pubmed:author | pubmed-author:EisenbergP... | lld:pubmed |
| pubmed-article:2119264 | pubmed:author | pubmed-author:StumpD CDC | lld:pubmed |
| pubmed-article:2119264 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2119264 | pubmed:volume | 82 | lld:pubmed |
| pubmed-article:2119264 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2119264 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2119264 | pubmed:pagination | 1159-68 | lld:pubmed |
| pubmed-article:2119264 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:meshHeading | pubmed-meshheading:2119264-... | lld:pubmed |
| pubmed-article:2119264 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2119264 | pubmed:articleTitle | Validity of enzyme-linked immunosorbent assays of cross-linked fibrin degradation products as a measure of clot lysis. | lld:pubmed |
| pubmed-article:2119264 | pubmed:affiliation | Cardiovascular Division, Washington University School of Medicine, St. Louis, Missouri 63110. | lld:pubmed |
| pubmed-article:2119264 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2119264 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2119264 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2119264 | lld:pubmed |
