Catabolism of Purified Rat Fibrin(ogen) Plasmin Degradation Products in Rats

1982 ◽  
Vol 48 (01) ◽  
pp. 059-061 ◽  
Author(s):  
W Nieuwenhuizen ◽  
J J Emeis ◽  
A Vermond
Keyword(s):  
Rate Constants ◽  
Degradation Products ◽  
Blood Clearance ◽  
Flux Rate ◽  
Fractional Catabolic Rate ◽  
Catabolic Rate ◽  
Main Fraction ◽  
Fibrinogen Molecule ◽  
Different Parts ◽  
D Dimer

SummaryThe blood clearance of purified plasmin degradation products (X, Y, D-dimer, Dcate, D EGTA, E-fibrin, Ecate and E EGTA) of rat fibrin(ogen) has been studied in a homologous system. Transcapillary flux rate constants, fractional catabolic rate constants and the ratios of intravascular and extravascular pools have been calculated. There are considerable differences in these constants between the two early fibrinogen degradation products X and Y. Also the differences between fibrinogen D and E fragments, derived from different parts of the fibrinogen molecule, are considerable. However, the differences between fibrin fragment D-dimer and fibrinogen fragment Dcate are relatively small. Also the differences between fragments E-fibrin, Ecate and EEGTA are small. The main fraction of all E-fragments is extravascular.

Estimation of the fractional catabolic rate constants for the elimination of cytosolic liver enzymes from plasma

Hepatology ◽  
1989 ◽  
Vol 10 (5) ◽  
pp. 833-839 ◽  
Author(s):  
Henny G. Peltenburg ◽  
Wim T. Hermens ◽  
George M. Willems ◽  
J. Guus Flendrig ◽  
Ellen Schmidt
Keyword(s):  
Rate Constants ◽  
Liver Enzymes ◽  
Fractional Catabolic Rate ◽  
Catabolic Rate

Some Factors Influencing Metabolism and Distribution of Fibrinogen in Man and Rabbits

1977 ◽  
Vol 37 (02) ◽  
pp. 243-252
Author(s):  
Yi-Hsiang Chen ◽  
E. B Reeve
Keyword(s):  
Plasma Fibrinogen ◽  
Synthesis Rate ◽  
Fibrinogen Concentration ◽  
Fractional Catabolic Rate ◽  
System Parameters ◽  
Catabolic Rate ◽  
Simultaneous Decrease ◽  
Normal Males ◽  
Healthy Females ◽  
Made In

SummaryTo shed some light on the homeostatic regulation of plasma fibrinogen, metabolic studies were made in healthy females, and in normal, thyroidectomized, and thyroxine-treated rabbits. In females, compared with normal males, plasma fibrinogen concentration, plasma and interstitial fibrinogen decreased consequent to an increased fractional catabolic rate and a normal fibrinogen synthesis rate. The interstitial/plasma fibrinogen ratio remained unchanged. In normal rabbits, with increasing body weight fractional catabolic rate and catabolic rate decreased, while fibrinogen concentration and plasma fibrinogen remained constant owing to a simultaneous decrease in fibrinogen synthesis. In addition, fractional transcapillary transfer rate and transcapillary flux also decreased resulting in a shrinkage of interstitial fibrinogen. Thyroidectomy and thyroxine-injection markedly altered fibrinogen metabolism: thyroid hormone accelerated fibrinogen catabolism but also stimulated synthesis. The net result was an increase in plasma fibrinogen and fibrinogen concentration. The interstitial/plasma fibrinogen ratio decreased in thyroxine-treated, and increased in thyroidectomized animals. This study defines the variations of the fibrinogen system parameters in these physiologic and pathologic conditions, and illustrates some patterns of alterations in fibrinogen metabolism.

Catabolism of Human Fibrinogen Fragment D in Normal Subjects and Patients with Liver Cirrhosis

1980 ◽  
Vol 44 (03) ◽  
pp. 146-149 ◽  
Author(s):  
Nicole Ardaillou ◽  
Jeannine Yvart ◽  
Philippe Le Bras ◽  
Marie-José Larrieu
Keyword(s):  
Liver Cirrhosis ◽  
Clearance Rate ◽  
Plasma Clearance ◽  
Normal Subjects ◽  
Fractional Catabolic Rate ◽  
Human Fibrinogen ◽  
Plasma Pool ◽  
Catabolic Rate ◽  
Chloramine T

SummaryThe catabolism of human fragment D, (FgD), obtained by plasmin digestion of fibrinogen has been investigated in normal subjects and patients with liver cirrhosis and the results compared with those obtained for fibrinogen (Fg). Fg was labelled with I-125 and Fg D with I-131 using the chloramine T method. The plasma disappearance curves of both labelled proteins fitted a two exponential curve. In controls the plasma clearance rate of Fg D was greater than that of Fg as shown by the marked difference between the half-lives of these two tracers: 8,9 and 83,5 hours for Fg D and Fg respectively. The fractional catabolic rate of Fg D was 3.38 times the plasma pool per day. In nine patients with liver cirrhosis, catabolism of Fg was not modified. In contrast, catabolism of Fg D was significantly reduced with a half life of 13.0 hours and a low fractional catabolic rate. These results suggest the role of the liver in the catabolism of Fg D in man.

A Novel Method for the Rapid Purification of Human and Rat Fibrin(OGEN) Degradation Products in High Yields

1979 ◽  
Author(s):  
W. Nieuwenhuizen ◽  
I. A. M. van Ruijven-Vermeer ◽  
F. Haverkate ◽  
G. Timan
Keyword(s):  
Degradation Products ◽  
Complete Separation ◽  
Purification Method ◽  
Amino Terminal ◽  
Novel Method ◽  
Rapid Purification ◽  
The One ◽  
High Yields ◽  
Size Heterogeneity ◽  
D Dimer

A novel method will be described for the preparation and purification of fibrin(ogen) degradation products in high yields. The high yields are due to two factors. on the one hand an improved preparation method in which the size heterogeneity of the degradation products D is strongly reduced by plasmin digestion at well-controlled calcium concentrations. At calcium concentrations of 2mM exclusively D fragments, M.W.= 93-000 (Dcate) were formed; in the presence of 1OmM EGTA only fragments M.W.= 80.000 (D EGTA) were formed as described. on the other hand a new purification method, which includes Sephadex G-200 filtration to purify the D:E complexes and separation of the D and E fragments by a 16 hrs. preparative isoelectric focussing. The latter step gives a complete separation of D (fragments) (pH = 6.5) and E fragments (at pH = 4.5) without any overlap, thus allowing a nearly 100% recovery in this step. The overall recoveries are around 75% of the theoretical values. These recoveries are superior to those of existing procedures. Moreover the conditions of this purification procedure are very mild and probably do not affect the native configuration of the products. Amino-terminal amino acids of human Dcate, D EGTA and D-dimer are identical i.e. val, asx and ser. in the ratgly, asx and ser were found. E 1% for rat Dcate=17-8 for rat D EGTA=16.2 and for rat D- dimer=l8.3. for the corresponding human fragments, these values were all 20.0 ± 0.2.

MONOCLONAL ANTIBODIES OF THE IgM AND IgG CLASS SPECIFIC FOR CROSSLINKED FIBRIN DEGRADATION PRODUCTS

1987 ◽  
Author(s):  
P J Gaffney ◽  
L J Creighton ◽  
A Curry ◽  
B MacMahon ◽  
R Thorpe
Keyword(s):  
Monoclonal Antibodies ◽  
Thrombolytic Therapy ◽  
Epitope Mapping ◽  
Degradation Products ◽  
Subcutaneous Route ◽  
Fibrin Degradation Products ◽  
Conformational Epitopes ◽  
Immunoglobulin Class Switching ◽  
Unique Specificity ◽  
D Dimer

Monoclonal antibodies (mabs) to crosslinked fibrin degradation products (XL-FDP) having the general formula D/Y[X]nY/D (known as X-oligomer) and D-D (known as D dimer) have been raised in balb/C mice by both a novel mtrasplenic and a conventional subcutaneous route of immunisation and by combinations of both these procedures. Mabs to X-oligomers (NIBn 52 and NIBn 123) obtained by an intrasplenic procedure have been demonstrated to crossreact only with X-oligomer in a 2-site ELISA procedure and not with D dimer or whole fibrinogen and have been shown to be of value m the examination of clinical material obtained from patients with various types of thrombosis and have also been useful in monitoring the efficacy of thrombolytic therapy. The X-oligomer mabs are immunoglobulins of the M class. It was demonstrated that their unique specificity for conformational epitopes on the large X-oligomer fragments does not reside in the IgM structure since alterative immunisation procedures have been used to generate mabs of the IgG class which have the same specificity. Using immunoglobulin class switching in culture rather than during immunisation was suggested by certain cell lines which produced both IgM and IgG specific for X-oligomer. This latter point needs rigorous validation.Immunoglobulin G type mabs to highly purified D dimer were raised by conventional subcutaneous immunisation of balb/C mice. One of these, NIBn-11, was found to crossreact with PVC-immobilised X-oligomer and D dimer but not with fibrinogen. However NIBn-11 did not bind to D dimer in a 2-site ELISA procedure while crossreactmg quite avidly with X-oligomer. This suggests that the D dimer epitope to which NIBn-11 is directed is expressed in some conformations and not m others and that these conformations are always expressed in the complex X-oligomer group of fragments. These mabs, whilst of value in measuring certain unique fibrin fragments m plasma, are useful in the epitope mapping of fibrinogen/fibrin and their plasmm-mediated

scholarly journals Increased Apolipoprotein AI Production Rate and Redistribution of High-Density Lipoprotein Size Induced by Estrogen plus Progestin as Oral Contraceptive

2009 ◽  
Vol 94 (12) ◽  
pp. 4891-4897 ◽  
Author(s):  
Laurence Duvillard ◽  
Guillaume Dautin ◽  
Emmanuel Florentin ◽  
Aline Jeannin ◽  
Jean-Paul Pais de Barros ◽  
...  
Keyword(s):  
Oral Contraceptive ◽  
High Density Lipoprotein ◽  
Production Rate ◽  
Density Lipoprotein ◽  
High Density ◽  
Pool Size ◽  
Fractional Catabolic Rate ◽  
Fed State ◽  
Catabolic Rate ◽  
Estrogen Plus Progestin

Context: The impact of estrogen plus progestin as an oral contraceptive on high density lipoprotein (HDL) apolipoprotein (apo) AI metabolism in humans is poorly understood. Objectives: This study was designed to measure the in vivo effect of Moneva (30 μg ethinylestradiol, 75 μg gestodene) on HDL apoAI production rate and fractional catabolic rate. Design: Using 13C-leucine, we performed two kinetic studies in the fed state in 10 normolipidemic young women, before and 3 months after beginning Moneva. Results: On Moneva, serum triglycerides increased by 12% (P = 0.03) in the fed state, whereas low-density lipoprotein and HDL cholesterol remained unchanged. HDL apoAI pool size and production rate were increased by 9.2% (67.3 ± 7.1 vs. 61.6 ± 6.7 mg · kg−1; P = 0.05) and 26.5% (14.3 ± 2.7 vs. 11.3 ± 2.2 mg · kg−1 · d−1; P = 0.02), respectively. HDL apoAI fractional catabolic rate was not significantly modified. Three-month treatment by Moneva induced a shift of HDL size distribution from HDL2 toward HDL3 (HDL3 = 51.5 ± 8.1 vs. 46.5 ± 9.2% of total HDL; P = 0.02) and an increase in the proportion of apoAI among HDL components (38.8 ± 4.3 vs. 34.4 ± 2.8%; P = 0.01). Conclusion: Oral contraception by estrogen plus progestin induces changes in HDL apoAI metabolism characterized by an increase in production rate and pool size, with a higher proportion of HDL3 particles. Whether or not these changes are beneficial to prevent atherosclerosis has to be explored further.

False-Positive D-Dimer Result in a Patient With Castleman Disease

2004 ◽  
Vol 128 (3) ◽  
pp. 328-331
Author(s):  
Kimberly Mugler ◽  
Jerry B. Lefkowitz
Keyword(s):  
Western Blot ◽  
Disseminated Intravascular Coagulation ◽  
False Positive ◽  
Degradation Products ◽  
False Negative ◽  
Castleman Disease ◽  
Laboratory Findings ◽  
Intravascular Coagulation ◽  
Immunodeficiency Virus ◽  
D Dimer

Abstract In suspected cases of disseminated intravascular coagulation, concurrent elevation of both fibrin(ogen) degradation products (FDPs) and D-dimer levels aids in confirming the diagnosis. This pattern of results reflects the action of plasmin proteolysis of cross-linked fibrin polymers as well as fibrinogen. We report the case of a patient with human immunodeficiency virus (HIV) and Castleman disease who presented with a high-positive D-dimer level and a negative FDP level in the course of a workup for disseminated intravascular coagulation. This finding suggested the possibility of either a false-positive D-dimer or a false-negative FDP level. To investigate the former, a Western blot was performed on the patient's serum to determine the presence of the D-dimer. No D-dimer band was visualized on the Western blot, confirming the false-positive nature of the D-dimer result. Insufficient quantity of patient serum, however, prevented further investigation into the etiology of this result. The false-positive D-dimer result is likely attributable to interference caused by the patient's Castleman disease–associated monoclonal gammopathy, a phenomenon that has been reported in other immunoassays. As the development of lymphoproliferative disorders is especially common within the HIV population, and hypergammaglobulinemia in Castleman disease is particularly common, clinicians should be aware of this phenomenon when the laboratory findings do not fit the clinical picture. Although it is rare, recognition of potential paraprotein interference in immunoassays will help avoid undertreatment or overtreatment of patients based on erroneous laboratory results.

scholarly journals Overestimation of the lipoprotein fractional catabolic rate(FCR) measured in short duration experiments.

1992 ◽  
Vol 15 (9) ◽  
pp. 541-546 ◽  
Author(s):  
Gerard CHAMPARNAUD ◽  
Khadija OUGUERRAM ◽  
Thierry MAGOT ◽  
Claude LUTTON
Keyword(s):  
Short Duration ◽  
Fractional Catabolic Rate ◽  
Catabolic Rate

scholarly journals In vivo behavior of human radioiodinated antithrombin III: distribution among three physiologic pools

Blood ◽  
1985 ◽  
Vol 66 (1) ◽  
pp. 13-19 ◽  
Author(s):  
TH Carlson ◽  
TL Simon ◽  
AC Atencio
Keyword(s):  
Endothelial Cell ◽  
Antithrombin Iii ◽  
Young Men ◽  
Fractional Catabolic Rate ◽  
Kinetic Behavior ◽  
Exponential Curve ◽  
Catabolic Rate ◽  
Total Body ◽  
Endothelial Receptor

Abstract It has recently been shown that antithrombin III (AT) distributes between plasma, a noncirculating vascular-associated pool and an extravascular pool in rabbit. Study of the in vivo behavior of autologous human 131I-AT demonstrates that in humans AT also distributes among three pools that are analogous to those found in rabbit. From the in vivo kinetic behavior of the 131I-labeled AT, the fractions of total-body AT in the plasma, noncirculating vascular- associated, and extravascular pools were calculated to be 0.393 +/- 0.015, 0.109 +/- 0.016, and 0.496 +/- 0.014, respectively. From three- exponential plasma radioactivity disappearance curves, an average plasma fractional catabolic rate, j3, of 0.576 +/- 0.034 day-1 was obtained for five healthy young men. This is almost identical to the result obtained if plasma 131I-AT disappearance is assumed to fit a two- exponential curve (0.546 +/- 0.038), where the constant C2 from *Ap(t) = C1e-a1t + C2e-a2t is assumed to be equal to 1 - C1. The fraction of the total vascular AT catabolized daily, j3.5, was calculated to be 0.457 +/- 0.034, and the fractional catabolic rate of total-body AT, jT, averaged 0.2271 +/- 0.0176. The results give further support to a model of in vivo behavior in which the vascular AT distributes between plasma and an endothelial receptor. Thus, the latter may serve to mediate activation of AT for its reaction with coagulation proteases and to mediate its entrance into the endothelial cell, where it is either transported to the extravascular fluids or is catabolized.

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