Literature DB >> 2111742

Quantitation of venous clot lysis with the D-dimer immunoassay during fibrinolytic therapy requires correction for soluble fibrin degradation.

B Brenner1, C W Francis, S Totterman, C M Kessler, A K Rao, R Rubin, H C Kwaan, K R Gabriel, V J Marder.   

Abstract

Plasma cross-linked fibrin-degradation products were analyzed using a D-dimer (DD) immunoassay in patients with deep vein thrombosis (DVT) or acute myocardial infarction (MI) treated with fibrinolytic therapy, and the results were correlated with clot lysis documented angiographically. In 13 patients with DVT, the mean DD concentration increased 10-fold (1,074 +/- 252 to 10,333 +/- 1,004 ng/ml) during therapy, but neither the peak level nor the DD concentration integrated over the course of therapy correlated with clot lysis. Since plasma DD can derive from degradation of soluble plasma fibrin as well as from thrombi, the contribution of the former was estimated by in vitro incubation of the pretreatment plasma with plasminogen activator. Subtraction of this value from the measured posttreatment DD concentration provided a "corrected" level that represented DD originating from lysis of thrombi. This modification resulted in improved correlation of DD levels with clot lysis. The mean corrected peak DD was higher in patients with successful thrombolysis (8,780 +/- 1,352 ng/ml) compared with patients without lysis (3,075 +/- 589 ng/ml, p less than 0.001). There was a moderate correlation between the volume of clot lysed and the corrected peak DD (r = 0.62) and a higher correlation with the corrected DD integrated over the course of treatment (r = 0.97). By contrast, the corrected DD concentrations were near zero in patients treated for MI with or without thrombolytic reperfusion, suggesting that fibrin in small coronary thrombi did not contribute significantly to total plasma DD during therapy.(ABSTRACT TRUNCATED AT 250 WORDS)

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 2111742     DOI: 10.1161/01.cir.81.6.1818

Source DB:  PubMed          Journal:  Circulation        ISSN: 0009-7322            Impact factor:   29.690


  4 in total

1.  Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition.

Authors:  L D Zydowsky; F A Etzkorn; H Y Chang; S B Ferguson; L A Stolz; S I Ho; C T Walsh
Journal:  Protein Sci       Date:  1992-09       Impact factor: 6.725

2.  Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A.

Authors:  H Ke; Y Zhao; F Luo; I Weissman; J Friedman
Journal:  Proc Natl Acad Sci U S A       Date:  1993-12-15       Impact factor: 11.205

3.  Time-dependent inhibition of peptidylprolyl cis-trans-isomerases by FK506 is probably due to cis-trans isomerization of the inhibitor's imide bond.

Authors:  T Zarnt; K Lang; H Burtscher; G Fischer
Journal:  Biochem J       Date:  1995-01-01       Impact factor: 3.857

4.  (More than) doubling down: Effective fibrinolysis at a reduced rt-PA dose for catheter-directed thrombolysis combined with histotripsy.

Authors:  Samuel A Hendley; Aarushi Bhargava; Christy K Holland; Geoffrey D Wool; Osman Ahmed; Jonathan D Paul; Kenneth B Bader
Journal:  PLoS One       Date:  2022-01-04       Impact factor: 3.240

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.