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PubMed1991

Fibrin degradation product D-dimer in the diagnosis of pulmonary embolism.

The study objective was to determine the specificity and sensitivity of plasma concentrations of D-dimer, a fibrin degradation product, as a marker for ongoing thrombotic and thrombolytic events in pulmonary embolism. A prospective study was performed in 74 patients with suspected pulmonary embolism who appeared in the emergency room with dyspnea and/or chest pain. The presence of pulmonary embolism was established by positive findings either in pulmonary angiography or lung scan. D-dimer concentrations were determined in all patients. In 11 patients with positive pulmonary angiography, D-dimer concentrations were monitored for 6-12 days. D-dimer concentrations were determined by a quantitative enzyme-linked immunoassay. Plasma probes of 26 patients (16 with/10 without positive pulmonary angiography) were re-assayed with a semiquantitative latex agglutination assay. D-dimer levels were significantly higher in patients with pulmonary embolism (greater than 1000 ng/mL in 41 out of 43) than in those without (less than 1000 ng/mL in all 21 patients) (p less than 0.01). The sensitivity and specificity for the ELISA were found to be 95% and 100%, respectively, for establishing the diagnosis of pulmonary embolism. In the latex assay the values were 81% and 60%, respectively. It is concluded that in patients with dyspnea and/or chest pain, determination of D-dimer in plasma by ELISA adds a valuable tool to the noninvasive diagnostic procedure for pulmonary embolism. From the time-course of D-dimer values we conclude that this assay might be valuable up to at least 6 days after symptom onset. The assay, however, is unreliable in malignancies or after surgery.

Adult↗
PubMed1976

Ventriculography with methylglucamine iocarmate (Dimer-X). Experimental and clinical study.

In an attempt to study the use and value in ventriculography of meglumine iocarmate (Dimer-X), previously accepted as a water soluble contrast medium safe for myelography, we have conducted animal experiments to compare Dimer-X with megulumine iothalamate (Conray 60) and meglumine diatrizoate (Angiografin). We also made clinical studies of Dimer-X. In the animal experiments, 1.5 ml and 2.0 ml of Dimer-X were injected into the ventricles of 7 dogs. We noted the apparent superiority of Dimer-X over Conray 60 and Angiografin as far as side effects were concerned, but there were no particular differences in the intensities of the ventriculograms obtained. Morphological studies of the ventricles and histological examinations of the ventricular walls 1 month after intraventricular injections of Dimer-X showed no abnormalities. In the clinical studies, ventriculography with 1-5 ml Dimer-X, performed on 17 cases, aged 8 months to 62 years, with diseases of the central nervous system, produced ventriculograms of good diagnostic value with no side effects, such as convulsions, apart from mild headache or vomiting in 4 instances.

Animals↗
PubMed2006

D-dimer testing: advantages and limitations in emergency medicine for managing acute venous thromboembolism.

D-dimer values can be rapidly determined and used for the management of acute venous thromboembolism (VTE). However, its role in the setting of emergency still remains unclear and inappropriate testing is a significant clinical problem. This review discusses the currently used assays, clinical indications, and limitations of D-dimer measurement. Studies in English language were identified by searching PubMed from December 1985 to December 2005. Available literature on D-dimer was identified from Medline, along with cross referencing from the reference lists of major articles and reviews on this subject. Among 56 articles collected, 14 papers, 4 overviews and 1 systemic review were selected accordingly to predefined criteria. Data synthesis shows that D-dimer testing has sufficient diagnostic accuracy for ruling out acute VTE if used in combination with standardised clinical judgement. D-dimer seems to be also a useful tool for managing suspected VTE patients in absence of immediate imaging. Attention should be paid to exclude conditions that may affect the accuracy of the test, such as concomitant disease, heparin administration and symptom duration >15 days. Although enzyme-linked immunosorbent assay determination has the highest accuracy, immunoturbidimetric assay seems the most suitable on an emergency basis because of its rapid performance. In conclusion, at present D-dimer testing can be safely used in the management of acute VTE in emergency medicine. However, because of its heterogeneity related to the method used and setting implemented, it is preferable to assess D-dimer accuracy before its implementation in management strategies for VTE.

Acute Disease↗
PubMed2005

Usefulness of a latex agglutination assay for FDP D-dimer to demonstrate the presence of postmortem blood.

D-dimer, a specific fragment resulting from degradation of cross-linked fibrin, is an essential marker for the diagnosis of disseminated intravascular coagulation (DIC). Rapid assay for D-dimer using monoclonal antibody coated-latex particles might be useful for discriminating between postmortem and antemortem blood in bloodstains. We tried to detect D-dimer in nine postmortem blood samples by the rapid latex agglutination assay and to quantify them automatically using the latex photometric immunoassay system. The results showed that all samples were positive and that their amounts of D-dimer were 335-2,800 microg/ml (the normal blood level, <1 microg/ml; the pathogenic blood level with DIC, 1-100 microg/ml). Next, nine stains made of postmortem blood were examined by the rapid latex agglutination assay. The result showed that only one case (D-dimer 335 microg/ml blood) showed weak positive while the others (D-dimer 600-2,800 microg/ml blood) were positive. The present study indicates that the latex agglutination assay for D-dimer can be useful to demonstrate the presence of postmortem blood.

Adolescent↗
PubMed1984

Captopril disulfide conjugates may act as prodrugs: disposition of the disulfide dimer of captopril in the rat.

The absorption and metabolism of the disulfide dimer conjugate of captopril has been studied in the rat following both oral and intravenous dosing and compared with that of the active monomer, captopril. Metabolism of the dimer to captopril has been shown after both oral and intravenous administration of the dimer (10 mg/kg) with peak plasma levels of captopril (154 ng/ml) occurring at 1 hr post dose. By contrast the peak plasma level of captopril after oral administration of captopril (10 mg/kg) at the same dose was much higher at 678 ng/ml and also occurred at 1 hr post dose. Plasma captopril disulfide species were much higher than the plasma levels of captopril after the administration of either dimer or captopril and tended to persist for much longer than for monomeric captopril particularly after administration of the dimer. Both the dimer and its pharmacologically active product captopril were found in relatively large amounts in lung, kidney and liver following the oral administration of the dimer.

Administration, Oral↗
PubMed1985

Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum.

The three-dimensional structure of scallop sarcoplasmic reticulum membranes has been determined from electron micrographs of two classes of stain-filled tubules by helical reconstruction methods. These structures are characterized by dimer ribbons of Ca2+-ATPase molecules running diagonally around the tube wall. Deep right-handed grooves separate the ribbons. The elongated, curved units of the dimer (approximately 95 A long in the radial direction; 60 to 70 A axially, and about 30 A wide) are displaced axially by approximately 34 A and are connected at their outer ends by a bridge running nearly parallel to the tube axis. The monomers make a second contact at their inner ends. Adjacent units with the same orientation form a strong contact that is responsible for the ribbon appearance. Comparison of tubules of different diameter shows that one set of connections between the dimer ribbons is conserved: the inner ends of axially displaced dimers appear to make contact along a left-handed path almost perpendicular to the major grooves. The lipid bilayer cannot be clearly identified. The two-dimensional map obtained from flattened tubules is consistent with the three-dimensional reconstruction in showing dimer ribbons connected by a weak contact across the grooves, strongly resembling the inter-dimer bond observed in three dimensions. The two-dimensional map shows a 2-fold axis relating units of the dimer, but the three-dimensional tubes show a slight axial polarity that may arise from the presence of proteins other than the Ca2+-ATPase.

Animals↗
PubMed1986

MgATPase activity of myosin subfragment 1. The dimer is more active than the monomer.

The MgATPase activity of the rabbit skeletal myosin subfragment 1 (S1), in the steady state, was measured by means of the intrinsic fluorescence of tryptophan. This technique gave results similar to those obtained by other methods (linked or radioactive assays). The activity was measured under conditions that effect the monomer/dimer ratio. It is shown that there is a close correlation between MgATPase activity and the proportion of dimer. At 20 degrees C, for pH 6.9 to 8.1 and for [KCl] less than or equal to 1 M, the observed activity (kobs) can be linearly related to the proportion of dimer (Ed/Eo) by: kobs(s-1) = 0.016-7 X 10(-3)[KCl] + 0.031(Ed/Eo), where [KCl] is expressed in M. We deduce that, at 20 degrees C and for [KCl] = 0 M, the activity of the monomer is kmobs = 0.016 s-1 (Ed/Eo = 0) and that of the dimer kdobs = 0.047 s-1 (Ed/Eo = 1), i.e. a ratio kdobs/kmobs approximately equal to 3. Beyond pH approximately equal to 8.3, the activities of both the monomer and the dimer increased steeply with increasing pH value. In the standard conditions (pH 8.0, [KCl] = 0 to 100 mM), S1 is mainly in the form of a dimer, and such conditions are not appropriate for study of the S1 monomer. For studying the pure monomer, the conditions required at 20 degrees C and in bis-Tris-propane are: S1 concentration approximately equal to 0.2 mg/ml, pH 6.9 to 7.8, [KCl] approximately equal to 300 mM. For studying the pure dimer, the conditions required are: S1 concentration greater than or equal to 0.2 mg/ml, pH 7.8 to 8.1 and [KCl] approximately equal to 0. In both cases the MgATP concentration is about 50 microM. Finally, if great care is taken concerning the age of the S1 solutions and the evaluation of the proportion of dimer, the values of kobs are extremely precise: the uncertainty regarding the values of kobs, as determined by means of intrinsic fluorescence, does not exceed +/- 0.001 s-1. Beyond this error bar conditions are uncontrolled.

Adenosine Triphosphate↗
PubMed1987

Spectroscopic studies on histone-DNA interactions. I. The interaction of histone (H2A, H2B) dimer with DNA: DNA sequence dependence.

Binding of the histone (H2A, H2B) dimer with chicken erythrocyte DNA has been studied by salt-titration spectroscopy in equilibrium conditions. The circular dichroism of DNA near 275 nm is depressed by the interaction with (H2A, H2B) at low concentrations of salt. The depression increases with increasing amounts of (H2A, H2B), and reaches a plateau at an (H2A, H2B) to DNA ratio of 1.5 (w/w), at which one (H2A, H2B) dimer occupies 28 base-pairs of DNA. The fluorescence emission intensity of the tyrosine residues in (H2A, H2B) is depressed by the H2A, H2B)-DNA interaction. When the DNA-(H2A, H2B) complex is titrated with NaCl, these two signals show transitions with increasing ionic strength of the buffer, whose normalized transition curves agree well. The midpoint of the transition is about 0.42 M-NaCl for a sample with a DNA concentration of 0.05 mg/ml and an (H2A, H2B) to DNA ratio of 0.4 (w/w). The fluorescence titration curves have been analyzed to obtain the binding constant for the (H2A, H2B) dimer with DNA. The sample concentration dependence of the titration profiles is consistent with the model of non-cooperative binding of (H2A, H2B) dimer to DNA. The titration profiles are reversible. The obtained binding constant for the (H2A, H2B) dimer with chicken erythrocyte DNA at 20 degrees C (pH 7.6), as a function of the ionic strength, I, is as follows: log10K = -14.9 log10(I)-1.2. The change of enthalpy delta H accompanied by the binding of the (H2A, H2B) dimer is nearly equal to zero, within an error of +/- 1.4 kcal/mol (1 cal = 4.184 J). DNA sequence dependence of the stability of DNA-(H2A, H2B) interactions is observed using reconstituted materials of synthetic DNAs. A decreasing stability of the interaction is observed following the order: the duplex of poly[(dA)-(dT)] greater than chicken erythrocyte DNA or the copolymer duplex of poly(dA).poly(dT) greater than the duplex of poly[(dG)-(dC)]. The difference in free energy of the association of the (H2A,H2B) dimer between the two copolymers is 0.8 kcal/mol.

Animals↗
PubMed1991

DNA-induced dimerization of the Escherichia coli Rep helicase.

The Escherichia coli Rep protein is a DNA helicase that is involved in DNA replication. We have examined the effects of DNA binding on the assembly state of the Rep protein using small-zone gel permeation chromatography and chemical crosslinking of the protein. Complexes of Rep protein were formed with short single-stranded and duplex hairpin oligodeoxynucleotides with lengths such that only a single Rep monomer could bind per oligodeoxynucleotide (i.e. 2 Rep monomers could not bind contiguously on the oligodeoxynucleotides). In the absence of DNA, Rep protein is monomeric (Mr 72,800) up to concentrations of at least 8 microM (monomer), even in the presence of its nucleotide cofactors (ATP, ADP, ATP-gamma-S). However, the binding of Rep monomers to single-stranded (ss) oligodeoxynucleotides, d(pN)n (12 less than or equal to n less than or equal to 20), induces the Rep monomers to oligomerize. Upon treatment of the Rep-ss oligodeoxynucleotide complexes with the protein crosslinking reagent dimethyl-suberimidate (DMS) and subsequent removal of the DNA, crosslinked Rep dimers are observed, independent of oligodeoxynucleotide length (n less than or equal to 20). Furthermore, short duplex oligodeoxynucleotides also induce the Rep monomers to dimerize. Formation of the Rep dimers results from an actual DNA-induced dimerization, rather than the adventitious crosslinking of Rep monomers bound contiguously to a single oligodeoxynucleotide. The purified DMS-crosslinked Rep dimer shows increased affinity for DNA and retains DNA-dependent ATPase and DNA helicase activities, as shown by its ability to unwind M13 RF DNA in the presence of the bacteriophage f1 gene II protein. On the basis of these observations and since the dimer is the major species when Rep is bound to DNA, we suggest that a DNA-induced Rep dimer is the functionally active form of the Rep helicase.

Adenosine Triphosphatases↗
PubMed1992

Effect of dimerization on the conformation of the encapsidation Psi domain of Moloney murine leukemia virus RNA.

In Moloney murine leukemia virus, the encapsidation Psi element was shown to be necessary and sufficient to promote packaging of viral RNA, and to be required for dimerization. The conformation of the Psi domain (nucleotides 215 to 565) was investigated in solution by chemical probing. The four bases were monitored at one of their Watson-Crick positions with dimethylsulfate at cytosine N3 and adenosine N1, and with a carbodiimide derivative at guanosine N1 and uridine N3. Position N7 of adenine residues was probed with diethylpyrocarbonate. The analyses were conducted on in vitro transcribed fragments corresponding either to the isolated Psi domain or to the 5'-terminal 725 nucleotides. The RNA fragments were analyzed in their monomeric and dimeric forms. A secondary structure model was derived from probing data, computer prediction and sequence analysis of related murine retroviruses. One major result is that Psi forms an independent and highly structured domain. Dimerization induces an extensive reduction of reactivity in region 278 to 309 that can be interpreted as the result of intermolecular interactions and/or intramolecular conformational rearrangements. A second region (around position 215) was shown to display discrete reactivity changes upon dimerization. These two regions represent likely elements of dimerization. More unexpectedly, reactivity changes (essentially enhancement of reactivity) were also detected in another part of Psi (around position 480) not believed to contain elements of dimerization. These reactivity changes could be interpreted as dimerization-induced allosteric transitions.

Base Sequence↗
PubMed1990

Structure-activity relationships of monomeric and dimeric synthetic ACTH fragments in perifused frog adrenal slices.

The effect of synthetic monomeric and dimeric ACTH fragments on spontaneous and ACTH(1-39)-evoked steroidogenesis in frog interrenal tissue was studied in vitro. Infusion of ACTH fragment 11-24 (10(-6) M) or its dimeric conjugates, attached either by their N-terminal, Glu(11-24)2, or their C-terminal amino acid, (11-24)2Lys, had no effect on the spontaneous release of corticosteroids. The monomer ACTH(11-24) and the dimer Glu(11-24)2 were also totally devoid of effect on the steroidogenic response to ACTH(1-39) (10(-9)M). In contrast, the (11-24)2Lys conjugate (10(-6)M) significantly decreased ACTH-induced stimulation of corticosterone and aldosterone (-63 and -62%, respectively). The dimeric conjugate of the fragment ACTH(7-24), linked through the C-terminal ends, (7-24)2Lys (10(-6)M), was also completely devoid of effect on basal steroidogenesis but caused a marked decrease of ACTH-evoked corticosterone and aldosterone release (-72 and -80%, respectively). Conversely, infusion of the dimer (1-24)2Lys gave rise to a dose-related stimulation of corticosterone and aldosterone release. The time-course of the steroidogenic response to the dimer was similar to that of ACTH(1-24). The 1-24 conjugate was 70 times less potent than the monomers ACTH(1-24) and ACTH(1-39). These results suggest that amphibian adrenocortical cells contain only one class of ACTH receptor which recognizes the 11-24 domain of ACTH with an affinity which depends on the presence of a strong potentiator segment, located at the N-terminus end of ACTH(1-39). Since the ACTH-dimers are thought to induce cross-linking of the receptors, our results suggest that aggregation of ACTH receptors causes a down-regulation of the receptors.

Adrenal Glands↗
PubMed1993

Relationships between lipoprotein(a), lipids, apolipoproteins, basal and stimulated fibrinolytic regulators, and D-dimer.

In 191 newly referred hyperlipidemic patients, our specific aim was to assess relationships between levels of lipoprotein(a) [Lp(a)], lipids, apolipoproteins, regulators of basal and stimulated fibrinolytic activity, and D-dimer, a measure of in vivo fibrinolysis. Lp(a) levels correlated with none of the measures of basal fibrinolytic regulators or D-dimer. In 25 patients, levels of stimulated regulators of fibrinolytic activity and D-dimer were measured after 10-minute cuff venous occlusion. Lp(a) levels again correlated with none of the stimulated regulators of fibrinolytic activity or D-dimer. However, both basal and stimulated levels of fibrinolytic regulators and D-dimer were closely related to other major risk factors for coronary heart disease (CHD) including triglyceride, apolipoprotein (apo) A1, apo B, Quetelet index (QI), and sex. By stepwise regression in 191 patients, the following standardized partial regression coefficients were significant (P < or = .05), and model R2 and P values were as follows: basal tissue plasminogen activator (tPA) with apo B-.18, with time .17, with QI -.28, R2 = 17%, P < or = .0001; basal plasminogen activator inhibitor (PAI) with apo B..25, with time -.15, with QI .17, R2 = 14%, P < or = .0001; basal alpha 2-antiplasmin with apo A1.14, with apo B.24, with QI.17, with sex .30, R2 = 25%, P < .0001; basal plasminogen with A1.15, with apo B.21, with QI.17, with sex.17, R2 = 15%, P < or = .0001; basal fibrinogen with Lp(a).17, with QI.21, with sex.26, R2 = 14%, P < or = .0001; D-dimer with sex.15, R2 = 21%, P < or = .048. Given the absence of any relationship between Lp(a) levels and inhibition or stimulation of fibrinolysis regulators or D-dimer either in the basal or stimulated state, we postulate that Lp(a)'s major atherogenic effects are mediated by mechanisms other than reduction of fibrinolysis stimulation or in vivo fibrinolysis.

Apolipoproteins↗
PubMed1986

Novel dimeric configurations from bacteriophage G4 replicative form DNA.

The oligomeric fraction of the replicative form of phage G4 was prepared by sedimentation on three successive CsCl velocity gradients followed by resolution on CsCl-propidium diiodide equilibrium gradients and subfractions through the equilibrium gradients were examined by electron microscopy. The most frequent dimer species were the circular dimer, the singly linked catenane and the figure 8; these occurred in a ratio of 10:3:1. The high enrichment for dimers and other oligomers made possible the observation and the determination of the frequency of occurrence of a number of minor species, some of them of novel configuration. These are (a) dimers similar to figure 8s except containing long, apparently four-stranded junctions common to the two halves (theta forms); (2) dimers similar to those in (1) except that the long junctions separate the two halves (dumbbell forms); (3) multiply catenated dimers with apparent right-handed intertwines; and (4) dimers containing a knot. Theta forms cleaved by EcoRI were shown to be stable under conditions in which EcoRI-treated figure 8s were resolved by branch migration.

Coliphages↗
PubMed1987

Reducing agent-sensitive dimerization of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus correlates with the presence of cysteine at residue 123.

Viruses within the Newcastle disease virus (NDV) serotype induce a wide array of disease manifestations ranging from an almost apathogenic pattern to the high mortality caused by avirulent or virulent isolates, respectively. A disulfide-linked dimer form of the NDV hemagglutinin-neuraminidase (HN) glycoprotein can be demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions for only some of these isolates. For others, indeed the majority of those we have studied, no such reducing agent-sensitive dimeric form of HN is demonstrable. Apparently, there is no causal relationship between disulfide-linked dimeric HN and virulence. Using the deduced amino acid sequence of the dimeric HN of isolate AV as a basis for selection of oligonucleotide primers, we sequenced three additional reducing agent-sensitive dimeric HN glycoproteins and eight for which a disulfide-linked dimer has not been identified, using primer extension and dideoxy sequencing. The deduced amino acid sequences reveal a strict correlation between the presence of cysteine at residue 123 and reducing agent-sensitive dimerization of HN.

Amino Acid Sequence↗
PubMed1992

Evaluation of plasma D-dimer in the diagnosis and in the course of fibrinolytic therapy of deep vein thrombosis and pulmonary embolism.

Blood samples were obtained from patients with deep venous thrombosis (DVT) or pulmonary embolism (PE) after angiographic confirmation as well as during fibrinolytic therapy with streptokinase. Plasma cross-linked fibrin degradation products were measured by a quantitative enzyme-linked immunoassay that recognizes the D-Dimer epitope. 24 patients with PE showed elevated D-Dimer levels (median; 25%-, 75%-quartile) (3,250 ng/ml; 1,270 ng/ml, 6,940 ng/ml) as well as 38 patients presenting with DVT (2,330 ng/ml; 1,760 ng/ml, 3,980 ng/ml). The sensitivity for the diagnosis of PE was 92%, for diagnosis of DVT 89% resp. 100%, depending on the cut-off limit. The D-Dimer level showed a correlation (r = 0.64) to the angiographically documented severity of PE quantified by the Miller's score, in contrast to DVT, where no such correlation could be found. During fibrinolytic therapy median levels rose from 3,020 ng/ml to 63,000 ng/ml within 8 hours and then fell within 6 days to 2,930 ng/ml. 10 patients with PE showed a good correlation (r = 0.72) between the reduction of Miller's score within 72 hours and D-Dimer 24 hours after the onset of therapy. In 17 patients with fibrinolytic treatment of DVT no correlation between D-Dimer and clot lysis could be found. These findings indicate that D-Dimer can provide additional information in the diagnostic procedure of suspected PE. During fibrinolytic therapy of PE with streptokinase, D-Dimer could serve as an early prognostic parameter of successful thrombolysis.

Biomarkers↗
PubMed1994

Global fibrinolytic capacity assessed by the serum D-dimer test. Correlation between basal and stimulated values.

Evaluation of fibrinolytic capacity is mostly done after stimulation by venous occlusion (VO) or 1-desamino-8-d-arginine vasopressin (DDAVP), either with global tests or with measurements of the specific fibrinolytic components. The serum D-dimer test has recently been described as a global fibrinolytic test in unstimulated individuals, and related to different levels of fibrinolytic activity. In the present study, we have compared the levels of serum D-dimer and t-PA before and after VO in order to see if the unstimulated values reflect the fibrinolytic capacity after stimulation. Twenty-eight healthy individuals and 126 patients with different metabolic disorders and/or coronary heart disease were included. Blood was drawn in a fasting state between 8 and 10 a.m. before and after VO for determinations of serum D-dimer after standardized coagulation, and of t-PA activity and antigen. There was a 7-fold increase in the median levels obtained after VO both for serum D-dimer and t-PA activity, whereas the increase in t-PA antigen was about 2.5 fold. The correlation coefficients between the levels of serum D-dimer, t-PA activity and t-PA antigen before and after VO were 0.63 (p < 0.001), 0.72 (p < 0.001) and 0.23 (p < 0.05), respectively. We conclude that the basal levels of t-PA and serum D-dimer to a certain degree reflect the fibrinolytic capacity after stimulation. Thus, the unstimulated serum D-dimer test, which reflects both t-PA and PAI-1, could be recommended as a global screening method for evaluation of the fibrinolytic potential.

Adult↗
PubMed1995

D-dimer concentrations during normal pregnancy, as measured by ELISA.

In pregnant women a number of changes in blood clotting and fibrinolysis proteins have been reported so indicating the existence of a state of hypercoagulability. In addition to fibrinogen and antithrombin III (AT), D-dimer is frequently checked during pregnancy, in particular during at risk pregnancy, but the exact pattern of D-dimer modifications during uncomplicated pregnancy is not definitively described. The aim of this study was to establish the range values in three different periods of uncomplicated pregnancy (A: 1-20 wks; B: 21-30 wks; C: 31-40 wks). We measured plasma levels of D-dimer, clottable fibrinogen and AT in 108 consecutive normal pregnant women aged 16 to 42 years. In period A, the range of D-dimer values was 43-211 ng/mL, not different from controls, while fibrinogen levels were significantly higher (p < 0.05) than in matched non pregnant women. Mean D-dimer levels were higher in periods B (p < 0.05) and C (p < 0.05) vs period A. Similarly, mean fibrinogen levels were found more elevated in periods B and C vs period A (p < 0.05). A significant correlation was found between fibrinogen and D-dimer levels (p < 0.001). No differences in AT levels were found among the three periods of pregnancy. The results of this study indicate that levels of D-dimer up to 685 micrograms/L may be reached at the end of physiological pregnancy. This fact should be taken into account in the evaluation of hemostatic studies performed in uncomplicated and complicated pregnant women.

Adolescent↗
PubMed1996

D-dimers are degraded by human neutrophil elastase.

To see if D-dimers were degraded by human neutrophil elastase (HNE), cross-linked fibrin was obtained by adding thrombin to purified fibrinogen in the presence of calcium ions and factor XIII, and the fibrin clot subsequently degraded by plasmin. Thereafter, the supernatant containing fibrin degradation products was removed and incubated with HNE. D-dimer levels were measured by two rapid semiquantitative tests, a latex agglutination test and the Nycocard immunofiltration test, and a quantitative ELISA-method. With increasing incubation time, D-dimer levels as measured by the latex and Nycocard tests rapidly decreased and subsequently became undetectable, while the ELISA D-dimer values remained essentially unchanged. By using SDS-electrophoresis and immunoblotting, the degradation of plasmic derivatives of cross-linked fibrin by fiNE was visualised. We conclude that in a purified system, D-dimers formed during plasmin mediated lysis of cross linked fibrin are further degraded by HNE. Such HNE degradation reduces the D-dimer concentration as measured by rapid semiquantitive tests, and may be partly responsible for discrepant results when using different D-dimer assays.

Antifibrinolytic Agents↗