Fibrinogen turnover: demonstration of multiple pathways of catabolism.

Abstract Studies have been conducted to identify early in vivo products of normal fibrinogen catabolism, focusing on 2 normal variants: (1) the high solubility, low molecular weight (269,000) fibrinogen (LMWF) of Mosesson and co-workers 3 and (2) the cryofibrinogen/fibrin complex (cryoprofibrin) characterized by Shainoff and Page. 5 In normal rabbits, LMWF has been demonstrated to be derived in vivo from the low solubility, high molecular weight fibrinogen (HMWF) which is the bulk of the plasma pool. 1 In the present study, 125 I-HMWF was injected into normal rabbits and the gradual appearance of radioactivity noted not only in the LMWF, but also in cryoprofibrin. By day 2 the specific activity of cryoprofibrin equaled that of HMWF, and by day 3 the specific activity of LMWF equaled that of HMWF. Thereafter, the specific activities of cryoprofibrin and LMWF slightly exceeded that of HMWF. The HMWF t12 was 47 hours, and total fibrinogen t12 was 6312 hours. In separate experiments, the t12 of 125 I-LMWF and 125 I-cryoprofibrin were 2612 and 13 hours, respectively. These studies support a concept of several normal catabolic pathways for fibrinogen (1) by low grade proteolysis to LMWF and (2) limited, partial, soluble, fibrin formation (cryoprofibrin). There is indirect evidence to suggest these processes also occur in man.

[1]  U. Abildgaard,et al.  Gelation of soluble fibrin in plasma by ethanol. , 2009, Scandinavian journal of haematology.

[2]  M. Mosesson,et al.  The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. , 1970, The Journal of biological chemistry.

[3]  R. Colman,et al.  A comparative study of four methods for detecting fibrinogen degradation products in patients with various diseases. , 1970, The New England journal of medicine.

[4]  E. Israels,et al.  Fibrinogen breakdown products: identification and assay in serum and urine. , 1969, The Journal of laboratory and clinical medicine.

[5]  L. Sherman,et al.  In vivo transformation between fibrinogens of varying ethanol solubilities: a pathway of fibrinogen catabolism. , 1969, The Journal of laboratory and clinical medicine.

[6]  R. Colman,et al.  Chronic intravascular coagulation syndrome. , 1968, The New England journal of medicine.

[7]  D. Woodfield,et al.  Fibrin degradation products in sera of normal subjects. , 1967, British medical journal.

[8]  S. Sherry,et al.  Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility. , 1967, Biochemistry.

[9]  C. Merskey,et al.  The Defibrination Syndrome: Clinical Features and Laboratory Diagnosis , 1967, British journal of haematology.

[10]  Z. Wegrzynowicz,et al.  Soluble Unclottable Complexes Formed in the Presence of Fibrinogen Degradation Products (FDP) during the Fibrinogen-Fibrin Conversion and Their Potential Significance in Pathology , 1967, Thrombosis and Haemostasis.

[11]  S. Sherry,et al.  The preparation and properties of human fibrinogen of relatively high solubility. , 1966, Biochemistry.

[12]  F. Rodríguez-Erdmann Bleeding due to increased intravascular blood coagulation. Hemorrhagic syndromes caused by consumption of blood-clotting factors (consumption-coagulopathies). , 1965, The New England journal of medicine.

[13]  C. J. Amris,et al.  Turnover and Distribution of 131Iodine-Labelled Human Fibrinogen , 1964, Thrombosis and Haemostasis.

[14]  J. Lewis Effects of Epsilon Amino Caproic Acid (EACA) on Survival of Fibrinogen I131 and on Fibrinolytic and Coagulation Factors in Dogs.∗ , 1963, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.

[15]  B. Alexander,et al.  Effect of Epsilonaminocaproic Acid on the Turnover of Labelled Fibrinogen in Rabbits , 1963, Circulation research.

[16]  A. Mcfarlane,et al.  IN VIVO BEHAVIOR OF I131-FIBRINOGEN , 1963 .

[17]  W. Crosby,et al.  Platelet and fibrinogen survival in normal and abnormal states of coagulation. , 1961, Blood.

[18]  I. Page,et al.  Cofibrins and Fibrin‐Intermediates as Indicators of Thrombin Activity in Vivo , 1960 .

[19]  E. Rosenblum,et al.  Mixtures of coagulase-positive staphylococci and strain variation in specimens from clinical sources. , 1959, The Journal of laboratory and clinical medicine.

[20]  R. T. Smith A heparin-precipitable fraction of human plasma. II. Occurrence and significance of the fraction in normal individuals and in various disease states. , 1957, The Journal of clinical investigation.

[21]  T. Astrup,et al.  The biological significance of fibrinolysis. , 1956, Lancet.

[22]  D. Korst,et al.  Cryofibrinogen in a case of lung neoplasm associated with thrombophlebitis migrans. , 1955, Blood.

[23]  D. Jenden,et al.  Micro-Kjeldahl Distillation Apparatus , 1953 .

[24]  Oliver H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[25]  E. Regoeczi 30 – ABNORMAL FIBRINOGEN METABOLISM , 1970 .

[26]  H. Bostrom,et al.  On the [35S]sulphate incorporation in fibrinopeptide B from rabbit fibrinogen. , 1960, Biochimica et biophysica acta.

[27]  J. Scheidegger Une micro-méthode de l’immuno-électrophorèse , 1955 .

[28]  H. Scheraga,et al.  The Non-clotting Component of the Human Plasma Fraction I-1 (“Cold Insoluble Globulin”)1 , 1955 .