Zusammenfassung
Fibrinogen, the central protein of blood coagulation, is a giant molecule (Henschen 1981). It has a molecular weight of 340,000. The molecule is composed of three pains of non-identical peptide chains, Aα, Bβ and γ)2, and the structure can therefore be described as (Aα, Bβ and γ)2. During coagulation thrombin cleaves two of the peptide chain pairs, i.e., Aα and Bβ, within the amino-terminal parts of these chains. Hereby the fibrinopeptides A and B are released and fibrin, with the structure (α, β, γ)2, is formed. The peptide chains are held together by 29 disulfide bridges. Two of the chain pairs, Bβ and γ, have carbohydrate side chains attached. A schematic representation of the molecule is shown in Fig. 1.
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References
Blombäck M, Blombäck B, Mammen EF, Prasad AS (1968) Nature 218: 134–137
Blombäck B, Gröndahl NJ, Hessel B, Iwanaga S, Wallén P (1973) J Biol Chem 248: 5806–5820
Edman P, Henschen A (1975) In: Needleman SB (ed) Protein sequence determination, 2nd edn. Springer, Berlin, pp 232–279
Gârdlund B, Hessel B, Marguerie G, Murano G, Blombäck B (1977) Eur J Biochem 77: 595–610
Henschen A (1978) Hoppe Seylers Z Physiol Chem 359: 1757–1770
Henschen A (1981) Hämostaseologie 1: 30–40
Henschen A, Edman P (1972) Biochim Biophys Acta 263: 351–367
Henschen A, Lottspeich F (1977a) Hoppe Seylers Z Physiol Chem 358: 1643–1646
Henschen A, Lottspeich F (1977b) Thromb Res 11: 869–880
Henschen A, Lottspeich F, Hessel B (1979) Hoppe Seylers Z Physiol Chem 360: 1951–1956
Henschen A, Lottspeich F, Kehl M, Southan C, Lucas J (1982) In: Henschen A, Graeff H, Lottspeich F (eds) Fibrinogen. de Gruyter, Berlin, pp 67–89
Kehl M, Lottspeich F, Henschen A (1981) Hoppe Seylers Z Physiol Chem 362: 1661–1664
Kehl M, Lottspeich F, Henschen A (1982) In: Henschen A, Graeff H, Lottspeich F (eds) Fibrinogen. de Gruyter, Berlin, pp 217–226
Lottspeich F, Henschen A (1977) Hoppe Seylers Z Physiol Chem 358: 935–938
Marx R, Schramm W (1982) In: Henschen A, Graeff H, Lottspeich F (eds) Fibrinogen. de Gruyter, Berlin, pp 123–128
Soria J, Soria C, Samama M, Henschen A, Southan C (1982) In: Henschen A, Graeff H, Lottspeich F (eds) Fibrinogen. de Gruyter, Berlin, pp 129–143
Töpfer-Petersen E, Lottspeich F, Henschen A (1976) Hoppe Seylers Z Physiol Chem 357: 1509–1513
Bennett JS, Vilaire G (1979) Exposure of platelet fibrinogen receptors by ADP and epinephrine. J Clin Invest 63: 1393–1401
Bennett JS, Vilaire G, Burch JW (1981) A role for prostaglandins and thromboxanes in the exposure of platelet fibrinogen receptors. J Clin Invest 68: 981–987
Castaldi PA, Caen J (1965) Platelet fibrinogen. J Clin Pathol 18: 579–585
Doolittle RF, Takagi T, Cottrell BA (1974) Platelet and plasma fibrinogen are identical gene products. Science 185: 368–370
Ganguly P (1972) Isolation and some properties of fibrinogen from human blood platelets. J Biol Chem 247: 1809–1815
Goldstein A, Aronow L, Kaltian SM (1974) In: Principles of drug action. The basis of pharmacology, 2nd ed. John Wiley and Sons, New York, p 80
Harfenist GJ, Packham MA, Mustard JF (1980) Reversibility of the association of fibrinogen with rabbit platelets exposed to ADP. Blood 56: 189–198
Hawiger J, Parkinson S, Timmons S (1980) Prostacyclin inhibits mobilization of fibrinogen binding sites on human ADP and thrombin treated platelets. Nature 293: 195–197
Kaplan KL, Brockman MS, Chernoff A, Lesznik GR, Drillings M (1979) Platelet and granules proteins: studies on release and subcellular localization. Blood 53: 604–618
Kaplan KL, Dauzier MS, Rose S (1981) ADP and epinephrine-induced release of platelet fibrinogen. Blood 55: 797–802
Mac Farlane DE, Mills DCB (1981) Inhibition by ADP prostaglandin induced accumulation of cyclic AMP in intact human platelets. J Cyclic Nucleotide Res 7: 1–11
Marguerie G, Plow EF, Edgington TS (1979) Human platelets possess an inducible and saturable receptor specific for fibrinogen. J Biol Chem
-5363
Marguerie G, Edgington TS, Plow EF (1980) Interaction of fibrinogen with its platelet receptor as part of a multistep reaction in ADP induced platelet aggregation. J Biol Chem
-161
Marguerie G, Plow EF (1981) Interaction of fibrinogen with its platelet receptor: kinetics and effect of pH and temperature. Biochemistry 20: 1074–1080
Marguerie G, Thomas-Maison N, Larrieu MJ, Plow EF (1982) The interaction of fibrinogen with human platelets in a plasma milieu. Blood 59: 91–95
Mustard JF, Perry DW, Ardlie NG, Packman MA (1972) Preparation of suspensions of washed platelet from humans.Br J Haematol 22: 193–204
Mustard JF, Packham MA, Perry DW, Guccione MA, Kinlough-Rathbone RC (1975) In: Biochemistry and pharmacology of platelets, C. Ciba Found Symp (New Series) 35: 47
Mustard JF, Packham MA, Kinglough-Rathbone RL, Perri DW, Regoeczi I (1978) Fibrinogen and ADP-induced platelet aggregation. Blood 52: 193–204
Niewiarowski S, Budzinski AZ, Morinelli TA, Brudzinski TM, Stewart GJ (1981) Exposure of fibrinogen receptor on human platelets by proteolytic enzymes. J Biol Chem 256: 917–925
Peerschke EI, Zucker MB, Grant RA, Egan JJ, Johnson (1980) Correlation between fibrinogen binding to human platelets and platelet aggregability. Blood 55: 841–847
Plow EF, Edgington TS (1975) Unique immunochemical features and intracellular stability of platelet fibrinogen. Thromb Res 7: 729–735
Plow EF, Marguerie G (1980a) Participation of ADP in the binding of fibrinogen to thrombin stimulated platelets. Blood 56: 553–555
Plow EF, Marguerie G (1980b) Induction of the fibrinogen receptor on human platelets by epinephrine and the combination of epinephrine and ADP. J Biol Chem 255: 10971–10977
Plow EF, Marguerie G (1980c) A regulatory role for fibrinogen in platelet aggregation. Circulation [Suppl] 62: 111
Tollefsen DM, Majerus PW (1975) Inhibition of human platelet aggregation by monovalent anti fibrinogen antibody fragment. J Clin Invest 55: 1259–1268
Weiss HI, Rogers J (1971) Fibrinogen and platelets in the primary arrest of bleeding. N Engl J Med 285: 369–374
White JG, Krivit W, Vernier RL (1965) The platelet-fibrin relationship in human blood clots. An ultrastructural study utilizing ferritin conjugated anti-fibrinogen antibody. Blood 25: 241–252
Blomback B, Hessel B, Hogg D, Therkildsen L (1978) A two-step fibrinogen-fibrin transition in blood coagulation. Nature 275: 501–505
Laurent TC, Blomback B (1958) On the significance of the release of two different peptides from fibrinogen during clotting. Acta Chem Scand 12: 1875–1977
Blomback B, Okada M (1982) Fibrin gel structure and clotting time. Thromb Res 25: 51–70
Brosstad F (1978) Lower susceptibility of human des-AA versus des-AABB fibrin towards fibrin stabilizing factor. Thromb Res 13: 799–803
Nossel HL (1981) Relative proteolysis of the fibrinogen Bß chain by thrombin and plasmin as a determinant of thrombosis. Nature 291: 5811–165–167
Eckhardt T, Nossel HL, Hurlet-Jensen A, LaGamma KS, Owen J, Auerbach M (1981) Measurement of desarginine fibrinopeptide B in human blood. J Clin Invest 67: 809–816
Kudryk B, Robinson D, Netre C, Hessel B, Blomback M, Blomback B (1982) Measurement of human blood of fibrinogen/fibrin fragments containing Bß 15–42 sequence. Thromb Res 25: 277–291
Nossel HL, Yudelman I, Canfield RE, Butler VP Jr, Spanondis K, Wilner G, Qureshi GD (1974) Measurement of fibrinopeptide A in human blood. J Clin Invest 54: 43–53
Yudelman IM, Nossel HL, Kaplan KL, Hirsh J (1978) Plasma fibrinopeptide A levels in symptomatic venous thromboembolism. Blood 51: 1189–1195
Kockum C (1976) Radioimmunoassay of fibrinopeptide A
clinical applications. Thromb Res 8: 225–236
Peuscher FW, Von Aken WG, Flier OThN, Stoepman-van Dalen EA, Cremer-Groote TM, van Mourik JA (1980) Effect of anticoagulant treatment measured by fibrinopeptide A ( FPA) in patients with venous thrombo-embolism. Thromb Res 18: 33–43
Yudelman I, Greenberg J (1982) Factors affecting fibrinopeptide A levels in patients with venous thromboembolism during anticoagulant therapy. Blood (in press)
Thomas DP (1981) Pathogenesis of venous thrombosis. In: Bloom AL, Thomas DP (eds) Haemostasis and thrombosis. Churchill Livingston, Edinburgh London Melbourne New York, p 637
Nichols AB, Owen J, Fleischer L, Marcella J, Kaplan KL, Weiss MB, Camion P, Nossel HL (1982) Comparison of the thrombogenicity of woven dacron and heparin bonded coronary sinus catheters. Clin Res 30: 209A
Nossel HL, Ti M, Kaplan KL, Spanondis K, Soland T, Butler VP Jr (1976) The generation of fibrinopeptide A in clinical blood samples. J Clin Invest 58: 1136–1144
Wessler S (1962) Thrombosis in the presence of vascular stasis. Am J Med 33: 648–666
Cronlund M, Hardin J, Burton J, Lee L, Haber E, Block ICI (1976) Fibrinopeptide A in plasma of normal subjects and patients with disseminated intravascular coagulation and systemic lupus erythematosus. J Clin Invest 58: 142–151
Peuscher FW, van Aken WG, Armstrong AL, Stoepman-van Dalen EA, van Mourik JA (1980) Significance of plasma fibrinopeptide A ( FPA) in patients with malignancy. J Lab Clin Med 96: 5–14
Nossel HL, Wasser J, Kaplan KL, LaGamma KS, Yudelman I, Canfield RE (1979) Sequence of fibrinogen proteolysis and platelet release after intrauterine infusion of hypertonic saline. J Clin Invest 64: 1371–1378
Kaplan KL, Nossel HL, Drillings M, Lesznik GR (1978) Radioimmunoassay of platelet factor 4 and beta-thromboglobulin: Development and application to studies of platelet release in relation to fibrinopeptide A generation. Br J Haematol 39: 129–146
Owen J, Kvam D, Kaplan KL, Nossel HL (1980) Sequence of platelet release and fibrinogen proteolysis associated with post-operative venous thrombosis. Clin Res 28: 2 (Abstract 495A)
deBoer AC, Han P, Turpie AGG, Butt R, Zielinsky A, Genton E (1981) Plasma and urine beta-thromboglobulin concentration in patients with deep vein thrombosis. Blood 58: 693–698
Ackerman SK, Douglas SD (1978) Purification of human monocytes on microexudate-coated surfaces. J Immunol 120: 1372
Bevilacqua MP, Amrani DL, Mosesson MW, Bianco C (1981) Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes. J Exp Med 153: 42
Bianco C, Griffin FM Jr, Silverstein SC (1975) Studies on the macrophage complement receptor. Alteration of receptor function upon macrophage activation. J Exp Med 141: 1278
Bianco C (1977) Plasma membrane receptors for complement. In: Day NK, Good RA (eds) Biological amplification systems in immunology. Plenum Publ. Corp., New York, p 69
Bianco C, Götze O, Cohn ZA (1979) Regulation of macrophage migration by products of the complement system. Proc Natl Acad Sci USA 76: 888
Bianco CO, Götze O, Cohn ZA (1980) Complement, coagualtion and mononuclear phagocytes. In: Furth R van (ed) Mononuclear phagocytes. Martinus Nijhoff Publ., The Hague, p 1443
Blumenstock FA, Saba TM, Weber P, Cho E (1976) Purification and biochemical characterization of a macrophage stimulating alpha-2-globulin opsonic protein. J Reticuloendothel Soc 19: 157
Blumenstock FA, Saba TM, Weber P, Laffin R (1978) Biochemical and immunological characterization of human opsonic a2-SB-glycoprotein: its identity with cold-insoluble globulin. J Biol Chem 253: 4287
Blumenstock FA, Saba TM, Roccario E, Cho E, DeLaughter M (1980) Stimulation of peritoneal macrophage phagocytosis by gelatinized fixed sheep erythrocytes by human and rat plasma fibronectin (opsonic a2-surface binding glycoprotein). Fed Proc 29: 4035 (Abstract)
Chen AB, Mosesson MW (1977) An improved method for purification of the cold-insoluble globulin of human plasma ( CIg ). Anal Biochem 79: 144
Chen AB, Amrani DL, Mosesson MW (1977) Heterogeneity of the cold-insoluble globulin of human plasma ( CIg ). Biochim Biophys Acta 493: 310
Cuatrecasas P (1974) Membrane receptors. Annu Rev Biochem 43: 169
Doran JE, Mansberger AR, Reese AC (1980) Cold insoluble globulin-enhanced phagocytosis of gelatinized targets by macrophage monolayers: a model system. J
Reticuloendothel Soc 27: 471
Doran JE, Mansberger AR, Edmondson HT, Reese AC (1981) Cold insoluble globulin and heparin interactions in phagocytosis by macrophage monolayers: mechanism of heparin enhancement. J Reticuloendothel Soc 285: 1981
Engvall E, Ruoslahti E (1977) Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer 20: 1
Engvall E, Ruoslahti E, Miller EJ (1978) Affinity of fibronectin to collagens of different genetic types and to fibrinogen. J Exp Med 147: 1584
Grinnell F (1980) Fibroblast receptor for cell-substratum adhesion: studies on the interaction of baby hamster kidney cells with latex beads coated by cold-insoluble globulin. J Cell Biol 86: 104
Hubbard AL, Cohn ZA (1976) Specific labels for cell surfaces. In: Maddy AH (ed) Biochemical analysis of membranes. Chapman and Hall Ltd., London, p 427
Jilek F, Hörmann H (1978) Cold-insoluble globulin (fibronectin) IV Affinity to soluble collagen of various types. Hoppe Seylers Z Physiol Chem 359: 247
Molnar J, Gelder FB, Lai MB, Siefring GE, Credo RB, Lorand L (1979) Purification of opsonically active human and rat cold-insoluble globulin (plasma fibronectin). Biochemistry 18: 3909
Mosesson MW, Umfleet RA (1970) The cold-insoluble globulin of plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. J Biol Chem 245: 5728
Mosesson MW, Chen AB, Huseby RM (1975) The cold-insoluble globulin of human plasma: studies of its essential structural features. Biochim Biophys Acta 386: 509
Mosesson MW, Amrani D (1980) The structure and biologic activities of plasma fibronectin. Blood 56: 145
Mosher DF (1980) In: Spaet TH (ed) Fibronectin. Prog Hemostasis Thromb 5: 111
Rabinovitch M (1967) The dissociation of the attachment and ingestion phase of phagocytosis by macrophages. Exp Cell Res 46: 19
Rabinovitch M (1970) Phagocytic recognition. In: Furth R van (ed) Mononuclear phagocytes. Blackwell Scientific Publ Ltd., Oxford, p 299
Ruoslahti E, Vaheri A (1975) Interaction of soluble fibroblast surface antigen with fibrinogen and fibrin. Identity with cold insoluble globulin of human plasma. J Exp Med 141: 497
Saba TM, Blumenstock FA, Weber P, Kaplan JE (1978) Physiologic role of cold-insoluble globulin in systemic host defence: implications of its characterization as the opsonic a2-surface binding glycoprotein. Ann NY Acad Sci 312: 43
Snyderman R, Mergenhagen SE (1976) Chemotaxis of macrophages. In: Nelson DS (ed) Immunobiology of the macrophage. Academic Press, New York, p 323
Stathakis NE, Mosesson MW (1977) Interactions among heparin, cold-insoluble globulin and fibrinogen in formation of the heparin precipitable fraction of plasma. J Clin Invest 60: 855
Stathakis NE, Mosesson MW, Chen AB, Galanakis DK (1978) Cryoprecipitation of fibrin-fibrinogen complexes induced by cold-insoluble globulin of plasma. Blood 51: 1211
Vaheri A, Mosher DF (1978) High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochim Biophys Acta 516: 1
Wright AE, Douglas SR (1904) Role of the blood fluids in phagocytosis. Proc R Soc Lond [Biol] 72: 357
Yamada KM, Olden K (1978) Fibronectins
adhesive glycoproteins of cell surface and blood. Nature 275: 179
Yamada KM, Kennedy DW (1979) Fibroblast cellular and plasma fibronectins are similar but not identical. J Cell Biol 80: 492
Cash JD (1978) Control mechanism of activator release. In: Davidson JF, Rowan RM, Samama MM, Desnoyers PC (eds) Progress in chemical fibrinolysis and thrombolysis, vol 3. Raven Press, New York, pp 65–75
Collen D (1976) Identification and some properties of a new fast-reacting plasmin inhibitor in human plasma. Eur J Biochem 69: 209–216
Collen D (1980) On the regulation and control of fibrinolysis. Thromb Haemostas 43: 77–89
Davidson JF, Lochhead M, McDonald GA, McNicol GP (1972) Fibrinolytic enhancement by stanozolol: a double blind trial. Br J Haematol 22: 543–559
Hoylaerts M, Rijken DC, Lijnen HR, Collen D (1981) Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. Thromb Haemostas 46: 162 (Abstract 494)
Korninger C, Collen D (1981) Studies on the specific fibrinolytic effect of human extrinsic (tissue-type) plasminogen activator in human blood and in various animal species in vitro. Thromb Haemostas 46: 561–565
Korninger C, Collen D (1981) Neutralization of human extrinsic (tissue-type) plasminogen activator in human plasma: no evidence for a specific inhibitor. Thromb Haemostas 46: 662–665
Korninger C, Stassen JM, Collen D (1981) Turnover of human extrinsic (tissue-type) plasminogen activator in rabbits. Thromb Haemostas 46: 658–661
Korninger C, Matsuo O, Suy R, Stassen JM, Collen D (1982) Thrombolysis with human extrinsic (tissue-type) plasminogen activator in dogs with femoral vein thrombosis. J Clin Invest 69: 573–580
Matsuo O,Rijken DC, Collen D (1981) Comparison of the relative fibrinogenolytic, fibrinolytic and thrombolytic properties of tissue plasminogen activator and urokinase in vitro. Thromb Haemostas 45: 115–229
Matsuo O, Rijken DC, Collen D (1981) Thrombolytic properties of human tissue plasminogen activator, as compared to urokinase in rabbits with a experimental pulmonary embolus. Nature 291: 590–591
Nilsson IM (1978) Effect of drugs on activator synthesis and release. In: Davidson JF, Rowan RM, Samama MM, Desnoyers PC (eds) Progress in chemical fibrinolysis and thrombolysis, vol 3. Raven Press, New York, pp 77–89
Rijken DC, Wijngaards G, Zaal-de Jong M, Welbergen J (1979) Purification and partial characterization of plasminogen activator from human uterine tissue. Biochim Biophys Acta 580: 140–153
Rijken DC, Collen D (1981) Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J Biol Chem 256: 7035–7041
Verstraete M (1980) A far reaching program: rapid, safe, and predictable thrombolysis in man. In: Kline DL, Reddy KNN (eds) Fibrinolysis. CRC Press, Boca Raton, Florida, pp 185–200
Weimar W, Stibbe J, Van Seyen AJ, Billiau A, De Somer P, Collen D (1981) Specific lysis of an iliofemoral thrombus by administration of extrinsic (tissue-type) plasminogen activator. Lancet 2: 1018–1020
Wiman B, Collen D (1978) Molecular mechanism of physiological fibrinolysis. Nature 272: 549–550
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Henschen, A. et al. (1982). Symposium Fibrinogen. In: Schlegel, B. (eds) Verhandlungen der Deutschen Gesellschaft für innere Medizin. Verhandlungen der Deutschen Gesellschaft für innere Medizin, vol 88. J.F. Bergmann-Verlag, Munich. https://doi.org/10.1007/978-3-642-47093-6_28
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