The Leukocyte Digestion of Fibrinogen Degradation Products (FDP)

1971 ◽  
Vol 26 (03) ◽  
pp. 523-525
Author(s):  
K Gibiński ◽  
B Lipiński ◽  
M Trusz-Gluza
Keyword(s):  
Degradation Products ◽  
Fibrinogen Degradation Products

SummaryWhile the native fibrinogen is not digested by the leucocyte proteases both the early and late FDP are digestible without any denaturating reagent. Thus, this reaction may occur in vivo indicating an unknown role of granulocytes in paracoagulation.

Studies on the Role of Fibrinolysis and Fibrinogen Degradation Products (FDP) in Analgesic Action of Morphine

1972 ◽  
Vol 28 (03) ◽  
pp. 359-366 ◽  
Author(s):  
Włodzimierz Buczko ◽  
Konstanty Wiśniewski
Keyword(s):  
Molecular Weight ◽  
Brain Tissue ◽  
Clinical Effect ◽  
Degradation Products ◽  
Analgesic Action ◽  
Fibrinogen Degradation Products ◽  
The Brain

SummaryThe role of fibrinolysis and FDP in the analgesic action of morphine in mice and rats was studied. It was shown that during activation of blood fibrinolysis, both the accumulation of morphine in the brain tissue of rats and the clinical effect of this drug were increased. Similar results were observed after morphine given simultaneously with FDP obtained in vitro. The data from the analysis of FDP carried out on Sephadex G-25 Fine columns suggest that only FDP of molecular weight of about 10,000 potentiate the action of morphine; smaller peptides decreased the action of this drug.

Unreliability of Current Serum Fibrin Degradation Product (FDP) Assays

1985 ◽  
Vol 53 (03) ◽  
pp. 301-302 ◽  
Author(s):  
P J Gaffney ◽  
M J Perry
Keyword(s):  
Monoclonal Antibodies ◽  
Serum Level ◽  
Degradation Product ◽  
Degradation Products ◽  
Polyclonal Antibodies ◽  
Fibrin Degradation Product ◽  
Serum Samples ◽  
Fibrinogen Degradation Products ◽  
A Value

SummaryPreviously, assays of fibrin-fibrinogen degradation products (FDP) had to be performed on serum samples. However, monoclonal antibodies (Mabs) are now available which permit the measurement of FDP directly in plasma. We have employed two Mabs, one monospecific for FDP originating from crosslinked fibrin and another panspecific for the FDP fraction, to determine normal FDP levels in plasma and serum. The monospecific Mab gave a value of 40 ng FDP/ml in plasma and 10 ng/ml in serum, while the serum level of FDP recorded using the panspecific Mab was >1000 ng/ml, at all the concentrations of thrombin employed. Similarly, when a solution of purified fibrinogen was treated with thrombin, the concentration of FDP present in the clot supernatant was >1000 ng/ml when assayed using the panspecific Mab. Thus during serum preparation as much as 75% of the native FDP is incorporated into the clot while in excess of 1000 ng/ml of laboratory generated FDP, probably incompletely polymerized fibrin, is measured using panspecific antisera. These data indicate that current FDP assays using polyclonal antibodies are not a reliable reflection of the FDP level generated in vivo. The use of FDP-specific Mabs which do not react with fibrinogen is recommended for future FDP assays performed directly on plasma.

scholarly journals Thrombin-Antithrombin III and Plasm in-Antiplasmin Complexes as Indicators of in Vivo Activation of the Coagulation and/or Fibrinolytic Systems

1977 ◽  
Author(s):  
D. Collen ◽  
F.de Cock
Keyword(s):  
Human Blood ◽  
Half Life ◽  
Antithrombin Iii ◽  
Enzyme Inhibitor ◽  
Degradation Products ◽  
Clinical Value ◽  
Fibrinogen Degradation Products ◽  
Prethrombotic State ◽  
Immunochemical Methods

Both the thrombin-antithrombin III and plasmin-antiplasmin complexes contain neoantigenic structures, not present in the parent molecules, to which non cross-reacting precipitating antibodies can be produced (Thromb.Res. 5, 577, 1974). This phenomenon has been used to develop immunochemical methods for the quantitation of these complexes in human blood (Thromb. Res 7, 235, 1975). Patients with in vivo activation of the coagulation and/or fibrinolytic systems consistently showed increased levels of enzyme-inhibitor complexes (Eur.J.Clin.Invest, in press, 1977). The circulatory half-life of these complexes was estimated to be several hours (0.5 to 0.75 days).On several occasions, increased plasmin-antiplasmin titers were observed in the presence of a normal screening hemostasis analysis, suggesting that these assays may be more sensitive indicators of in vivo activation of the coagulation-fibrinolytic systems that assays for fibrinogen degradation products.Studies to determine the clinical value of the measurement of these enzyme-inhibitor complexes as indicators of a prethrombotic state are in progress and will be reported.

Fibrinogen Fragments X, Y, D and E Increase Levels of Plasma Fibrinogen and Liver mRNAs Coding for Fibrinogen Polypeptides in Rats

1985 ◽  
Vol 53 (02) ◽  
pp. 212-215 ◽  
Author(s):  
H M G Princen ◽  
H J Moshage ◽  
J J Emeis ◽  
H J W de Haard ◽  
W Nieuwenhuizen ◽  
...  
Keyword(s):  
Regulatory Mechanism ◽  
Degradation Products ◽  
Mrna Level ◽  
Plasma Fibrinogen ◽  
Fibrin Degradation Product ◽  
Fibrinogen Degradation Products ◽  
Fibrin Degradation Products ◽  
First Time ◽  
D Dimer

SummaryPreviously, we demonstrated that in vivo regulation of liver fibrinogen synthesis occurs via the fibrinogen mRNA level. However, the molecular regulatory mechanism of fibrinogen synthesis is still not well understood. Fibrinogen or fibrin degradation products might play an important role in regulating fibrinogen synthesis. In our present study, we have injected rats intraperitoneally with purified homologous fragments and measured the liver content of mRNA specific coding for fibrinogen. Increased levels of fibrinogen mRNA and elevated plasma fibrinogen concentrations were observed in rats after administration of fibrinogen degradation products X, Y, DEGTA Dcate or E. Fragment E or E’ has a less stimulatory effect than X, Y or Dcate, whereas cross-linked fibrin degradation product D dimer does not increase fibrinogen synthesis. This article reports for the first time a stimulatory effect of the high molecular weight fibrinogen degradation products on fibrinogen synthesis.

Role of D Dimer in Patients with Elevated Fibrinogen Degradation Products in Serum: Further Study in Chronic Myelogenous Leukemia

1990 ◽  
Vol 84 (3) ◽  
pp. 149-155 ◽  
Author(s):  
Masanori Saito ◽  
Hidesaku Asakura ◽  
Hiroshi Jokaji ◽  
Chika Uotanzi ◽  
Ichiro Kumabashiri ◽  
...  
Keyword(s):  
Chronic Myelogenous Leukemia ◽  
Degradation Products ◽  
Myelogenous Leukemia ◽  
Fibrinogen Degradation Products ◽  
D Dimer

Studies on the Molecular Pathology and Pathogenesis of Bleeding in Severe Fibrinolytic States in Dogs

1964 ◽  
Vol 12 (01) ◽  
pp. 069-086 ◽  
Author(s):  
E Kowalski ◽  
A. Z Budzynski ◽  
Maria Kopec ◽  
Z. S Latallo ◽  
B Lipinski ◽  
...  
Keyword(s):  
Molecular Pathology ◽  
Bleeding Time ◽  
Degradation Products ◽  
Close Similarity ◽  
Platelet Adhesiveness ◽  
Plasma Medium ◽  
Fibrinogen Degradation Products ◽  
Fibrin Monomer

Summary1. In the course of fibrinogen digestion by plasmin in a plasma medium in vitro “early” and “late” fibrinogen degradation products (FDP) are formed.2. The formation of the early FDP is correlated with the appearance of the “peak”, e.g. the highest plasma anticlotting activity. This activity after further FDP digestion with plasmin and formation of late FDP attains lower “plateau” values.3. A similar effect is observed after SKP1 infusion into dogs.4. The close similarity between the course of in vitro and in vivo digestion of fibrinogen allows to conclude that, as has been shown in purified systems, early FDP act predominantly as inhibitors of thrombin-fibrinogen reaction, whereas late FDP are responsible for the inhibition of fibrin monomer polymerization.5. Methods for identification and differentation of circulating FDP are described.6. The appearance of early FDP circulating in blood is correlated with the most pronounced prolongation of the bleeding time and with prof used bleeding.7. It has been shown that circulating FDP interference with platelet adhesiveness, aggregation and viscous metamorphosis, the effect of early FDP being more pronounced than that of late FDP.8. A concept is put forward according to which bleeding in plasma proteolytic states is due to the impairment of hemostatic function of platelets by FDP.

scholarly journals Autophagy and Autophagy-Related Diseases: A Review

2020 ◽  
Vol 21 (23) ◽  
pp. 8974
Author(s):  
Tadashi Ichimiya ◽  
Tsukasa Yamakawa ◽  
Takehiro Hirano ◽  
Yoshihiro Yokoyama ◽  
Yuki Hayashi ◽  
...  
Keyword(s):  
Quality Control ◽  
Cell Differentiation ◽  
Physiological Function ◽  
Degradation Products ◽  
Starvation Response ◽  
Comprehensive Review ◽  
Selective Autophagy ◽  
Related Disease

Autophagy refers to the process involving the decomposition of intracellular components via lysosomes. Autophagy plays an important role in maintaining and regulating cell homeostasis by degrading intracellular components and providing degradation products to cells. In vivo, autophagy has been shown to be involved in the starvation response, intracellular quality control, early development, and cell differentiation. Recent studies have revealed that autophagy dysfunction is implicated in neurodegenerative diseases and tumorigenesis. In addition to the discovery of certain disease-causing autophagy-related mutations and elucidation of the pathogenesis of conditions resulting from the abnormal degradation of selective autophagy substrates, the activation of autophagy is essential for prolonging life and suppressing aging. This article provides a comprehensive review of the role of autophagy in health, physiological function, and autophagy-related disease.

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