D-dimer: An Overview of Hemostasis and Fibrinolysis, Assays, and Clinical Applications

Advances in Clinical Chemistry

Volumn 69, Issue , 2015, Pages 1-46

  Olson, John D ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

D dimer; Deep venous thrombosis; Disseminated intravascular coagulation; Fibrinolysis; Pulmonary embolus

Indexed keywords

BIOLOGICAL MARKER; FIBRIN DEGRADATION PRODUCT; FIBRIN FRAGMENT D; PLASMIN; PLASMINOGEN;

AGE; BLOOD; BLOOD SAMPLING; DISSEMINATED INTRAVASCULAR CLOTTING; FEMALE; FIBRINOLYSIS; HEMOSTASIS; HUMAN; METABOLISM; PHYSIOLOGY; PREGNANCY; VENOUS THROMBOEMBOLISM; VERY ELDERLY;

AGE FACTORS; AGED, 80 AND OVER; BIOMARKERS; BLOOD SPECIMEN COLLECTION; DISSEMINATED INTRAVASCULAR COAGULATION; FEMALE; FIBRIN FIBRINOGEN DEGRADATION PRODUCTS; FIBRINOLYSIN; FIBRINOLYSIS; HEMOSTASIS; HUMANS; PLASMINOGEN; PREGNANCY; VENOUS THROMBOEMBOLISM;

EID: 84945466730     PISSN: 00652423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.acc.2014.12.001     Document Type: Chapter

References (167)

1. Owen C.A., Bowie E.J.W., Thompson J.H. The Diagnosis of Bleeding Disorders 1975, 1. Little Brown and Company Inc., Boston, MA. second ed.
2. Michiels C. Endothelial cell functions. J. Cell. Physiol. 2003, 196:430-443.
3. Ware J.A., Heistad D.D. Platelet-endothelium interactions. N. Engl. J. Med. 1993, 328:628-635.
4. Marcus A.L., Brockman M.J., Drosopoulos J.H.F., et al. The endothelial cell ecto-ADPase responsible for inhibition of platelet function is CD 39. J. Clin. Invest. 1997, 99:1351-1360.
5. Marcus A.J., Saffer L.B., Broekman M.J., et al. Thrombosis and inflammation as multicellular processes: significance of cell-cell interactions. Thromb. Haemost. 1995, 74:213-217.
6. Higgins R.A., Kitchen S., Olson J.D. Hemostasis. Tietz Textbook of Clinical Chemistry and Molecular Diagnostics 2012, 2083-2128. Elsevier Saunders, St. Louis, MO. C.A. Burtis, E.R. Ashwood, D.E. Burns (Eds.).
7. Cruz M.A., Diacovo T.G., Emsley J., et al. Mapping the glycoprotein lb-binding site in the von Willebrand factor Al domain. J. Biol. Chem. 2000, 275:19098-19105.
8. Ruggeri Z.M., De Marco L., Gatti L., et al. Platelets have more than one binding site for von Willebrand factor. J. Clin. Invest. 1983, 72:1-12.
9. Varga-Szabo D., Pleines I., Nieswandt B. Cell adhesion mechanisms in platelets. Arterioscler. Thromb. Vasc. Biol. 2008, 28:403-412.
10. Cruz M.A., Handin R.I., Wise R.J. The interaction of the von Willebrand factor-Al domain with platelet glycoprotein Ib/IX. The role of glycosylation and disulfide bonding in a monomeric reconbinant Al domain protein. J. Biol. Chem. 1993, 268:21238-21245.
11. Sadler J.E. Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem. 1998, 67:394-424.
12. Sixma J.J., Sakariassen K.S., Stel H.V., et al. Functional domains of von Willebrand factor. Recognition of discrete tryptic fragments by monoclonal antibodies that inhibit interactions of von Willebrand factor with platelets and collagen. J. Clin. Invest. 1984, 74:736-744.
13. Kottke-Marchant K. Platelet structure and function. An Algorithmic Approach to Hemostasis Testing 2008, 13-27. College of American Pathologists, Northfield, IL. K. Kottke-Marchant (Ed.).
14. White J.G. The dense bodies of human platelets. The Platelet Amine Storage Granule 1992, 31-50. CRC Press, Boca Raton, FL. K.M. Meyers, C.D. Barnes (Eds.).
15. White J.G. Platelet structure. Platelets 2007, 45-73. Elsevier, Boston, MA. A.D. Michelson (Ed.).
16. Johnson S.A., Balboa R.S., Dessel B.H., Monto R.W., Siegesmund K.A., Greenwalt T.J. The mechanism of the endothelial supporting function of intact platelets. Exp. Mol. Pathol. 1964, 34:115-127.
17. Mann K.G. Biochemistry and physiology of blood coagulation. Thromb. Haemost. 1999, 82:165-174.
18. Mann K.G., Nesheim M.E., Church W.R., et al. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 1990, 76:1-16.
19. Doolittle R.E. Structural aspects of the fibrinogen to fibrin conversion. Adv. Protein Chem. 1973, 27:1-109.
20. Medved L., Weisel J.W. Recommendations for nomenclature on fibrinogen and fibrin. J. Thromb. Haemost. 2009, 7:355.
21. McKee P.A., Rogers L.A., Marler E., et al. The subunit polypeptides of human fibrinogen. Arch. Biochem. Biophys. 1966, 116:271.
22. Mutch N.J., Booth N.A. Plasminogen activation and regulation of fibrinolysis. Hemostasis and Thrombosis: Basic Principles and Clinical Practice 2013, 314-333. Lippincott Williams and Wilkins, Philadelphia, PA. sixth ed. V.J. Marder, W.C. Aird, J.S. Bennett, S. Schulman, G.C. White (Eds.).
23. Gaffney P.J. Fibrin degradation products. A review of structures found in vitro and in vivo. Ann. N. Y. Acad. Sci. 2001, 936:594-610.
24. Bannach F.G., Gutierrez A., Fowler B.J., et al. Localization of regulatory elements mediating constitutive and cytokine-stimulated plasminogen gene expression. J. Biol. Chem. 2002, 277:38579-38588.
25. Walker J.B., Nesheim M.E. The molecular weights, mass distribution, chain composition, and structure of soluble fibrin degradation products released from a fibrin dot perfused with plasmin. J. Biol. Chem. 1999, 274:5201-5212.
26. Dano K., Andreasen P.A., Grondahl-Hansen J., et al. Plasminogen activators, tissue degradation, and cancer. Adv. Cancer Res. 1985, 44:139-266.
27. Duffy M.J. The urokinase plasminogen activator system: role in malignancy. Curr. Pharm. Des. 2004, 10:39-49.
28. Melchor J.P., Strickland S. Tissue plasminogen activator in central nervous system physiology and pathology. Thromb. Haemost. 2005, 93:655-660.
29. Blasi F., Sidenius N. The uroldnase receptor: focused cell surface proteolysis, cell adhesion and signaling. FEBS Lett. 2010, 584:1923-1930.
30. Nicoloso G., Hauert J., Kruirhof E.K., et al. Fibrinolysis in normal subjects-comparison between plasminogen activator inhibitor and other components of the fibrinolytic system. Thromb. Haemost. 1988, 59:299-303.
31. Camiolo S.M., Thorsen S., Astrup T. Fibrinogenolysis and fibrinolysis with tissue plasminogen activator, urokinase, streptokinase-activated human globulin, and plasmin. Proc. Soc. Exp. Biol. Med. 1971, 138:277-280.
32. Husain S.S., Gurewich V., Lipinski B. Purification and partial characterization of a single-chain high-molecular-weight form of urokinase from human urine. Arch. Biochem. Biophys. 1983, 220:31-38.
33. Wun T.C., Schleuning W.D., Reich E. Isolation and characterization of urokinase from human plasma. J. Biol. Chem. 1982, 257:3276-3283.
34. Darras V., Thienpont M., Stump D.C., et al. Measurement of urokinase-type plasminogen activator (u-PA) with an enzyme-linked immunosorbent assay (ELISA) based on three murine monoclonal antibodies. Thromb. Haemost. 1986, 56:411-414.
35. Larsson L.I., Skriver L., Nielsen L.S., et al. Distribution of urokinase-type plasminogen activator immunoreactivity in the mouse. J. Cell Biol. 1984, 98:894-903.
36. Grau E., Moroz L.A. Fibrinolytic activity of normal human blood monocytes. Thromb. Res. 1989, 53:145-162.
37. Manchanda N., Schwartz B.S. Lipopolysaccharide-induced modulation of human monocyte urokinase production and activity. J. Immunol. 1990, 145:4174-4180.
38. Ellis V., Scully M.F., Kakkar V.V. Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes. J. Biol. Chem. 1989, 264:2185-2188.
39. Manchanda N., Schwartz B.S. Single chain urokinase. Augmentation of enzymatic activity upon binding to monocytes. J. Biol. Chem. 1991, 266:14580-14584.
40. Blasi F., Sidenius N. The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling. FEBS Lett. 2010, 584:1923-1930.
41. Dane K., Behrendt N., Hoyer-Hansen G., et al. Plasminogen activation and cancer. Thromb. Haemost. 2005, 93:676-681.
42. Shore J.D., Day D.E., Bock P.E., et al. Acceleration of surface-dependent auto-catalytic activation of blood coagulation factor XII by divalent metal ions. Biochemistry 1987, 26:2250-2258.
43. Schousboe I. The inositol-phospholipid-accelerated activation of prekallikrein by activated factor XII at physiological ionic strength requires zinc ions and high-Mr kininogen. Eur. J. Biochem. 1990, 193:495-499.
44. Bernardo M.M., Day D.E., Olson S.T., et al. Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement. Eur. J. Biochem. 1993, 268:12468-12476.
45. Greengard J.S., Griffin J.H. Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry 1984, 23:6863-6869.
46. Zini J.M., Schmaier A.H., Cines D.B. Bradykinin regulates the expression of kininogen binding sites on endothelial cells. Blood 1993, 81:2936-2946.
47. Herwald H., Morgelin M., Svensson H.G., et al. Zinc-dependent conformational changes in domain D5 of high molecular mass kininogen modulate contact activation. Eur. J. Biochem. 2001, 268:396-404.
48. McMullen B.A., Fujikawa K. Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). J. Biol. Chem. 1985, 260:5328-5341.
49. Tans G., Rosing J. Structural and functional characterization of factor XII. Semin. Thromb. Hemost. 1987, 13:1-14.
50. Bock S. Antithrombin and the serpin family. Hemostasis and Thrombosis: Basic Principles and Clinical Practice 2013, 286-299. Lippincott Williams and Wilkins, Philadelphia, PA. sixth ed. V.J. Marder, W.C. Aird, J.S. Bennett, S. Schulman, G.C. White (Eds.).
51. Murano G., Williams L., Miller-Anderson M., et al. Some properties of antithrombin III and its concentration in human plasma. Thromb. Res. 1980, 18:259-262.
52. Peterson C., Blackburn M. Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. J. Biol. Chem. 1985, 260:610-615.
53. Bennett B., Booth N.A., Croll A., et al. The bleeding disorder in acute promyelocytic leukaemia: fibrinolysis due to u-PA rather than defibrination. Br. J. Haematol. 1989, 71(4):511-517.
54. Sottrup-Jensen L., Lonblad P.B., Jones C.M., et al. Primary structure of human alpha 2-macroglobulin. II. Primary structure of eight CNBr fragments located in the NH2-terminal half of alpha 2-macroglobulin, accounting for 603 amino acid residues. J. Biol. Chem. 1984, 259(13):8304-8309.
55. Kan C.C., Solomon E., Belt K.T., et al. Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and assignment of the chromosomal locus. Proc. Natl. Acad. Sci. U.S.A. 1985, 82(8):2282-2286.
56. Morrissey J.H., Brose G.J. Tissue factor and initiation and regulation (TFPI) of coagulation. Hemostasis and Thrombosis: Basic Principles and Clinical Practice 2013, 163-178. Lippincott Williams and Wilkins, Philadelphia, PA. sixth ed. V.J. Marder, W.C. Aird, J.S. Bennett, S. Schulman, G.C. White (Eds.).
57. Novotny W.R., Girard T.J., Miletich J.P., et al. Purification and characterization of lipoprotein-associated coagulation inhibitor from human plasma. J. Biol. Chem. 1989, 264:18832-18837.
58. Sandset P.M., Lund H., Norseth J., et al. Treatment with hydroxymethylglutaryl-coenzyme A reductase inhibitors in hypercholesterolemia induces changes in the components of the extrinsic coagulation system. Arterioscler. Thromb. Vasc. Biol. 1991, 11:138-145.
59. Hansen I.B., Huseby N.E., Sandset P.M., et al. Tissue-factor pathway inhibitor and lipoproteins. Evidence for association with and regulation by LDL in human plasma. Arterioscler. Thromb. Vasc. Biol. 1994, 14:223-229.
60. Piro O., Broze G.J. Comparison of cell-surface TFPI alpha and beta. J. Thromb. Haemost. 2005, 3:2677-2683.
61. Castoldi E., Simioni P., Tormene D., et al. Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma. J. Thromb. Haemost. 2009, 8:294-300.
62. Mosnier L.O., Griffin J.H. Protein C, protein S, thrombomodulin and entothelial protein C receptor pathways. Hemostasis and Thrombosis: Basic Principles and Clinical Practice 2013, 300-313. Lippincott Williams and Wilkins, Philadelphia, PA. sixth ed. V.J. Marder, W.C. Aird, J.S. Bennett, S. Schulman, G.C. White (Eds.).
63. Esmon C.T. The protein C pathway. Chest 2003, 124:26S-32S.
64. Liaw P.C.Y., Mather T., Oganesyan N., et al. Identification of the protein C/protein C binding sites on the endothelial cell protein C receptor. Implications for a novel mode of ligand recognition by a major histocompatibility complex class 1-type receptor. J. Biol. Chem. 2001, 276(11):8364-8370.
65. Czekay R.P., Aertgeerts K., Curriden S.A., et al. Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins. J. Cell Biol. 2003, 160(5):781-791.
66. Hekman C.M., Loskutoff D.J. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J. Biol. Chem. 1985, 260:11581-11587.
67. Dederck P.J., De Mal M., Alessi M.C., et al. Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J. Biol. Chem. 1988, 263:15454-15461.
68. Kruithof E.K., Gudinchet A., Bachmann E. Plasminogen activator inhibitor 1 and plasminogen activator inhibitor 2 in various disease states. Thromb. Haemost. 1988, 59:7-12.
69. Loskutoff D.J., Samad F. The adipocyte and hemostatic balance in obesity: studies of PAI-1. Arterioscler. Thromb. Vasc. Biol. 1998, 18:1-6.
70. Crandall D.L., Quinet E.M., Morgan G.A., et al. Synthesis and secretion of plasminogen activator inhibitor-1 by human preadipocytes. J. Clin. Endocrinol. Metab. 1999, 84:3222-3227.
71. 2-antiplasmin and plasminogen activator inhibitor-1 of clot lysis in vitro. Fibrinolysis 1990, 4:169-175.
72. Collen D., Wiman B. Fast-acting plasmin inhibitor in human plasma. Blood 1978, 51:563-569.
73. Bangert K., Johnsen A.H., Christensen U., et al. Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma. Biochem. J. 1993, 291:623-625.
74. Nesheim M. Fibrinolysis and the plasma carboxypeptidase. Curr. Opin. Hematol. 1998, 5:309-313.
75. Bajzar L., Morser J., Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombinthrombomodulin complex. J. Biol. Chem. 1996, 271:16603-16608.
76. Mao S.S., Cooper C.M., Wood T., et al. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans. J. Biol. Chem. 1999, 274:35046-35052.
77. Merskey C., Johnson A.J., Kleiner G.J., et al. The defibrination syndrome clinical features and laboratory diagnosis. Br. J. Haematol. 1967, 13:528-549.
78. M. Verstraete, J. Vermylen, M.B. Donant (Eds.), Fibrinogen degradation products, Scand. J. Haematol. (Suppl. 8) (1971) 3-392.
79. Donati M.B. Assays for fibrinogen-fibrin degradation products in biological fluids: some methodological aspects. Thromb. Diath. Haemorrh. 1975, 34:652-660.
80. Merskey C., Johnson A.J., Lalezari P. Increase in fibrinogen and fibrin-related antigen in human serum due to in vitro lysis of fibrin by thrombin. J. Clin. Invest. 1972, 51:903.
81. Arnesen H., Ly B., Odagard O.R. Improved quantization of serum FDP after coagulation at low pH. Thromb. Res. 1973, 3:643.
82. Gaffney P.J. Letters to the editor. Lancet 1972, 300:1422.
83. Gaffney P.J. Subunit relationships between fibrinogen and fibrin degradation products. Thromb. Res. 1973, 2:201-217.
84. Cambrosio A., Keating P. Between fact and technique: the beginnings of hybridoma technology. J. Hist. Biol. 1992, 25:175-230.
85. Gaffney P.J., Brasher M. Subunit structure of the plasmin-induced degradation products of crosslinked fibrin. Biochim. Biophys. Acta 1973, 295:308-313.
86. Elms M.J., Bunce I.H., Bundesen P.G., et al. Measurement of crosslinked fibrin degradation products-an immunoassay using monoclonal antibodies. Thromb. Haemost. 1983, 50:591-594.
87. Whitaker A.N., Elms M.J., Masci P.P., et al. Measurement of cross linked fibrin derivatives in plasma: an immunoassay using monoclonal antibodies. J. Clin. Pathol. 1984, 37:882-887.
88. Greenberg C.S., Devine D.V., McCrae K.M. Measurement of plasma fibrin D-dimer levels with the use of a monoclonal antibody coupled to latex beads. Am. J. Clin. Pathol. 1987, 87:94-100.
89. Mager J.J., Schutgens R.E., Haas F.J., et al. The early course of D-dimer concentration following pulmonary artery embolisation. Thromb. Haemost. 2001, 86:1578-1579.
90. Chandler W.L., Velan T. Plasmin generation and D-dimer formation during cardiopulmonary bypass. Blood Coagul. Fibrinolysis 2004, 15:583-591.
91. Dindo D., Breitenstein S., Hahnloser D., et al. Kinetics of D-dimer after general surgery. Blood Coagul. Fibrinolysis 2009, 20:347-352.
92. Caliezi C., Reber G., Lämmle B., et al. Agreement of D-dimer results measured by a rapid ELISA (VIDAS) before and after storage during 24h or transportation of the original whole blood samples. Thromb. Haemost. 2000, 83:177-178.
93. Woodhams B., Girardot O., Blanco M.J., Colesse G., Gourmelin Y. Stability of coagulation proteins in frozen plasma. Blood Coagul. Fibrinolysis 2001, 12:229-236.
94. CLSI D-dimer for the Exclusion of Venous Thromboembolic Disease; Approved Guideline. CLSI document H59-A 2011, Clinical and Laboratory Standards Institute, Wayne, PA.
95. CLSI Collection, Transport, and Processing of Blood Specimens for Testing Plasma-Based Coagulation Assays and Molecular Hemostasis Assays; Approved Guideline-Fifth Edition. CLSI Document H21-A5 2008, Clinical and Laboratory Standards Institute, Wayne, PA.
96. Engvall E., Perlmann P. Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry 1971, 8(9):871-874.
97. Olson J.D., Cunningham M.T., Higgins R.A., et al. D-dimer: simple test, tough problems. Arch. Pathol. Lab. Med. 2013, 137:1030-1038.
98. CGL-A Coagulation Limited Proficiency Testing Survey Participant Summary 2014, 44-46. College of American Pathologists, Northfield, IL, USA.
99. Bates S.M. D-dimer assays in diagnosis and management of thrombotic and bleeding disorders. Semin. Thromb. Hemost. 2012, 38:673-682.
100. Tripodi A. D-dimer testing in laboratory practice. Clin. Chem. 2011, 57:1256-1262.
101. Righini M., Perrier A., De Moerloose P., et al. D-dimer for venous thromboembolism diagnosis: 20 years later. J. Thromb. Haemost. 2008, 6:1059-1071.
102. Pittet J.L., de Moerloose P., Reber G., et al. VIDAS D-dimer: fast quantitative ELISA for measuring D-dimer in plasma. Clin. Chem. 1996, 42:410-415.
103. Scarvelis D., Palareti G., Toulon P., et al. HemosIL D-dimer HS assay in the diagnosis of deep vein thrombosis and pulmonary embolism. Results of a multicenter management study. J. Thromb. Haemost. 2008, 6:1973-1975.
104. Newman D.J., Henneberry H., Price C.P. Particle enhanced light scattering immunoassay. Ann. Clin. Biochem. 1992, 29:22-42.
105. Dempfle C.E., Hafner G., Lestin H.G., et al. Multicentre evaluation of Tina-quant® D-dimer. J. Lab. Med. 1996, 20:31-37.
106. Dempfle C.E. Validation, calibration, and specificity of quantitative D-dimer assays. Semin. Vasc. Med. 2005, 5:315-320.
107. Charles L.A., Edwards T., Macik B.G. Evaluation of sensitivity and specificity of six D-dimer latex assays. Arch. Pathol. Lab. Med. 1994, 118:1102-1105.
108. Kutinsky I., Blakley S., Roche V. Normal D-dimer levels in patients with pulmonary embolism. Arch. Intern. Med. 1999, 159:1569-1572.
109. Freyberger G., Trillaud H., Labrouche S., et al. D-dimer strategy in thrombosis exclusion-a gold standard study in 100 patients suspected of deep venous thrombosis or pulmonary embolism: 8 DD methods compared. Thromb. Haemost. 1998, 79:32-37.
110. Di Nisio M., Squizzato A., Rutjes A.W.S., et al. Diagnostic accuracy of D-dimer test for exclusion of venous thromboembolism: a systematic review. J. Thromb. Haemost. 2007, 5:296-304.
111. Lee-Lewandrowski E., Nichols J., Van Cott E., et al. Implementation of a rapid whole blood D-dimer test in the emergency department of an urban academic medical center: impact on ED length of stay and ancillary test utilization. Am. J. Clin. Pathol. 2009, 132:326-331.
112. Dempfle C.E. Fibrin D-dimer testing for venous and arterial thrombotic disease. Semin. Vasc. Med. 2005, 5:315-320.
113. Dempfle C.E., Zips S., Ergul H., Heene D.L. The fibrin assay comparison trial (FACT): evaluation of 23 quantitative D-dimer assays as basis for the development of D-dimer calibrators. FACT study group. Thromb. Haemost. 2001, 85:671-678.
114. Dempfle C.E., Zips S., Ergul H., Heene D.L. The fibrin assay comparison trial (FACT): correlation of soluble fibrin assays with D-dimer. Thromb. Haemost. 2001, 86:1204-1209.
115. Edlund B., Nilsson T.K. A proposed stoichiometrical calibration procedure to achieve transferability of D-dimer measurements and to characterize the performance of different methods. Clin. Biochem. 2006, 39:137-142.
116. Adema E., Gebert U. Pooled patient samples as reference material for D-dimer. Thromb. Res. 1995, 80:85-88.
117. Meijer P., Haverkate F., Kluft C., et al. A model for the harmonization of test results of different quantitative D-dimer methods. Thromb. Haemost. 2006, 95:567-572.
118. Kitchen D.P., Munroe-Peart S., Kitchen S., et al. Introduction of a point of care D-dimer EQA program to include assessment of testing and postanalytical interpretation of results. J. Thromb. Haemost. 2014, 12(Suppl. 1):44. (abstract).
119. McKay D.G., Muller-Berghaus G. Therapeutic indications of disseminated intravascular coagulation. Am. J. Cardiol. 1967, 20:392-403.
120. Taylor F.B., Toh C.H., Hoots W.K., et al. Towards definition, clinical and laboratory criteria, and a scoring system for disseminated intravascular coagulation. Thromb. Haemost. 2001, 86:1327-1330.
121. Toh C.H., Hoots W.K. The scoring system of the Scientific and Standardisation Committee on Disseminated Intravascular Coagulation of the International Society on Thrombosis and Haemostasis: a 5-year overview. J. Thromb. Haemost. 2007, 5:604-606. on behalf of the SSC on Disseminated Intravascular Coagulation of the ISTH.
122. Blaisdell F.W. Causes, prevention, and treatment of intravascular coagulation and disseminated intravascular coagulation. J. Trauma Acute Care Surg. 2012, 72:1719-1722.
123. Angstwurm M.W., Dempfle C.E., Spannagl M. New disseminated intravascular coagulation score: a useful tool to predict mortality in comparison with Acute Physiology and Chronic Health Evaluation II and Logistic Organ Dysfunction scores. Crit. Care Med. 2006, 34:314-320.
124. Shah K., Quaas J., Rolston D., et al. Magnitude of D-dimer matters for diagnosing pulmonary embolus. Am. J. Emerg. Med. 2013, 31:942-945.
125. Rowbotham B.J., Carroll P., Whitaker A.N., et al. Measurement of crosslinked fibrin derivatives-use in the diagnosis of venous thrombosis. Thromb. Haemost. 1987, 57:59-61.
126. Bounameaux H., Schneider P.A., Reber G., et al. Measurement of plasma D-dimer for diagnosis of deep venous thrombosis. Am. J. Clin. Pathol. 1989, 91:82-85.
127. Bounameaux H., Slosman D., de Moerloose P., et al. Diagnostic value of plasma D-dimer in suspected pulmonary embolism. Lancet 1988, 2:628-629.
128. Bounameaux H., Cirafici P., de Moerloose P., et al. Measurement of D-dimer in plasma as diagnostic aid in suspected pulmonary embolism. Lancet 1991, 337:196-200.
129. Wells P.S. Integrated strategies for the diagnosis of venous thromboembolism. J. Thromb. Haemost. 2007, 5(Suppl. 1):41-50.
130. Wells P.S., Anderson D.R., Rodger M., et al. Derivation of a simple clinical model to categorize patients probability of pulmonary embolism: increasing the models utility with the SimpliRED D-dimer. Thromb. Haemost. 2000, 83:416-420.
131. Ten Cate-Hoek A.J., Prins M.H. Management studies using a combination of D-dimer test result and clinical probability to rule out venous thromboembolism: a systematic review. J. Thromb. Haemost. 2005, 3:2465-2470.
132. Wells P.S., Anderson D.R., Rodger M.A., et al. Excluding pulmonary embolism at the bedside without diagnostic imaging: management of patients with suspected pulmonary embolism presenting to the emergency department by using a simple clinical model and D-dimer. Ann. Intern. Med. 2001, 135:98-107.
133. Freyburger G., Trillaud H., Labrouche S., et al. Rapid ELISA D-dimer testing in the exclusion of venous thromboembolism in hospitalized patients. Clin. Appl. Thromb. Hemost. 2000, 6:77-81.
134. Keeling D.M., Mackie I.J., Moody A., Watson H.G. The diagnosis of deep vein thrombosis in symptomatic outpatients and the potential for clinical assessment and D-dimer assays to reduce the need for diagnostic imaging. Br. J. Haematol. 2004, 124:15-25. on behalf of the Haemostasis and Thrombosis Task Force of the British Committee for Standards in Haematology.
135. Akman M.N., Cetin N., Bayramoglu M., et al. Value of the D-dimer test in diagnosing deep vein thrombosis in rehabilitation inpatients. Arch. Phys. Med. Rehabil. 2004, 85:1091-1094.
136. Zhi M., Ding E.L., Theisen-Toupal J., et al. The landscape of inappropriate laboratory testing: a 15-year meta-analysis. PLoS One 2013, 8:e78962.
137. Rathbun S.W., Whitsett T.L., Raskob G.E. Negative D-dimer result to exclude recurrent deep venous thrombosis: a management trial. Ann. Intern. Med. 2004, 141:839-845.
138. Le Gal G., Righini M., Roy P.M., et al. Value of D-dimer testing for the exclusion of pulmonary embolism in patients with previous venous thromboembolism. Arch. Intern. Med. 2006, 166:176-180.
139. Prandoni P., Noventa F., Ghirarduzzi A., et al. The risk of recurrent venous thromboembolism after discontinuing anticoagulation in patients with acute proximal deep vein thrombosis or pulmonary embolism. A prospective cohort study in 1,626 patients. Haematologica 2007, 92:199-205.
140. Palareti G., Cosmi B., Legnani C., et al. D-dimer testing to determine the duration of anticoagulation therapy. N. Engl. J. Med. 2006, 355:1780-1789. PROLONG Investigators.
141. Tosetto A., Iorio A., Marcucci M., et al. Predicting disease recurrence in patients with previous unprovoked venous thromboembolism: a proposed prediction score (DASH). J. Thromb. Haemost. 2012, 10:1019-1025.
142. Ginsberg J.S., Brill-Edwards P., Burrows R.F., et al. Venous thrombosis during pregnancy: leg and trimester of presentation. Thromb. Haemost. 1992, 80:132-137.
143. Morse M. Establishing a normal range for D-dimer levels through pregnancy to aid in the diagnosis of pulmonary embolism and deep vein thrombosis. J. Thromb. Haemost. 2004, 2:1202-1204.
144. Chan W.S.C.S., Bates S., Naguit I., et al. The prevalence of positive soluble fibrin and D-dimer results in healthy asymptomatic pregnant women. Blood 1999, 94:20a.
145. Nolan T.E., Smith R.P., Devoe L.D. Maternal plasma D-dimer levels in normal and complicated pregnancies. Obstet. Gynecol. 1993, 81:235-238.
146. Chan W.S., Chunilal S., Lee A., et al. A red blood cell agglutination D-dimer test to exclude deep venous thrombosis in pregnancy. Ann. Intern. Med. 2007, 147:165-170.
147. Kline J.A., Williams G.W., Hernandes-Nino J. D-dimer concentrations in normal pregnancy: new diagnostic thresholds are needed. Clin. Chem. 2005, 51:825-829.
148. Kovac M., Mikovic Z., Rakicevic L., et al. The use of D-dimer with new cut-off can be useful in diagnosis of venous thromboembolism in pregnancy. Eur. J. Obstet. Gynecol. Reprod. Biol. 2010, 148:27-30.
149. Francalanci I., Comeglio P., Liotta A.A., et al. D-dimer concentrations during normal pregnancy, as measured by ELISA. Thromb. Res. 1995, 78:399-405.
150. Ballegeer V., Mombaerts P., Declerck P.J., et al. Fibrinolytic response to venous occlusion and fibrin fragment D-dimer levels in normal and complicated pregnancy. Thromb. Haemost. 1987, 58:1030-1032.
151. Harper P.L., Theakston E., Ahmed J., et al. D-dimer concentration increases with age reducing the clinical value of the D-dimer assay in the elderly. Intern. Med. J. 2007, 37:607-613.
152. Righini M., Goehring C., Bounameaux H., et al. Effects of age on the performance of common diagnostic tests for pulmonary embolism. Am. J. Med. 2000, 109:357-361.
153. Carrier M., Le Gal G., Bates S.M., et al. D-dimer testing is useful to exclude deep vein thrombosis in elderly outpatients. J. Thromb. Haemost. 2008, 6:1072-1076.
154. Douma R.A., le Gal G., Söhne M., et al. Potential of an age adjusted D-dimer cut-off value to improve the exclusion of pulmonary embolism in older patients: a retrospective analysis of three large cohorts. BMJ 2010, 340:c1475.
155. Khorana A.A., Connolly G.C. Assessing risk of venous thromboembolism in the patient with cancer. J. Clin. Oncol. 2009, 27:4839-4847.
156. ten Wolde M., Kraaijenhagen R.A., Prins M.H., et al. The clinical usefulness of D-dimer testing in cancer patients with suspected deep venous thrombosis. Arch. Intern. Med. 2002, 162:1880-1884.
157. Carrier M., Lee A.Y.Y., Bates S.M., Anderson D.R., Wells P.S. Accuracy and usefulness of a clinical prediction rule and D-dimer testing in excluding deep vein thrombosis in cancer patients. Thromb. Res. 2008, 123(1):177-183.
158. King V., Vaze A.A., Moskowitz C.S., et al. D-dimer assay to exclude pulmonary embolism in high-risk oncologic population: correlation with CT pulmonary angiography in an urgent care setting. Radiology 2008, 247:854-861.
159. Di Nisio M., Rutjes A.W.S., Buller H.R. Combined use of clinical pretest probability and D-dimer test in cancer patients with clinically suspected deep vein thrombosis. J. Thromb. Haemost. 2006, 4:52-57.
160. DiNisio M., Sohne M., Kamphuisen P.W., et al. D-dimer test in cancer patients with suspected acute pulmonary embolism. J. Thromb. Haemost. 2005, 3:1239-1242.
161. Righini M., Le Gal G., De Lucia S., et al. Clinical usefulness of D-dimer testing in cancer patients with suspected pulmonary embolism. Thromb. Haemost. 2006, 95:715-719.
162. Cosmi B., Legnani C., Cini M., et al. The role of D-dimer and residual venous obstruction in recurrence of venous thromboembolism after anticoagulation withdrawal in cancer patients. Haematologica 2005, 90:713-715.
163. Knowlson L., Bacchu S., Paneesha S., et al. Elevated D-dimers are also a marker of underlying malignancy and increased mortality in the absence of venous thromboembolism. J. Clin. Pathol. 2010, 63:818-822.
164. Lee A.Y., Julian J.A., Levine M.N., et al. Clinical utility of a rapid whole-blood D-dimer assay in patients with cancer who present with suspected acute deep venous thrombosis. Ann. Intern. Med. 1999, 131:417-423.
165. Ay C., Vormittag R., Dunkler D., et al. D-dimer and prothrombin fragment 1.2 predict venous thromboembolism in patients with cancer: results from the Vienna Cancer and Thrombosis Study. J. Clin. Oncol. 2009, 27:4124-4129.
166. Ay C., Dunkler D., Marosi C., et al. Prediction of venous thromboembolism in cancer patients. Blood 2010, 116:5377-5382.
167. Gordge M.D., Faint R.W., Rylance P.B., et al. Plasma D-dimer: a useful marker of fibrin breakdown in renal failure. Thromb. Haemost. 1989, 61:522-525.