Zusammenfassung
Fibrin tritt in der Blutbahn bekanntlich in verschiedenen Formen auf, als lösliches zirkulierendes Fibrin (Fibrinmonomer, Fibrinmonomer-Fibrinogen-Komplex bzw. Fibrinoligomer) und als unlösliches, hochpolymeres, periodenkoinzident quervernetztes, „korpuskuläres“ und dadurch zunehmend zirkulationsunfähiges Derivat. Die Elimination dieser heterogenen Fibrinformen folgt entsprechend der unterschiedlichen Löslichkeit dieser Derivate wesensverschiedenen Prinzipien.
Herrn Prof. Dr. med. Volker Becker (Erlangen) zum 60. Geburtstag in Dankbarkeit und Verehrung
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Literatur
Allen C, Saga TM, Molnar J (1973) Isolation, purification and characterization of opsonic protein. J Reticuloendothel Soc 13: 410–423
Benzer H (1975) Oberflachenspannung in der Lunge and Schocklunge. Verh Dtsch Ges Inn Med 81: 455 - 462
Bergström J, Fürst P (1978) Uremic toxins. Kidney Intern 13: 5
Bleyl U (1971) Pathomorphologie und Pathogenese des Atemnotsyndroms. Verh Dtsch Ges Pathol 55: 39–72
Bleyl U (1978) Haemostase und Schocklunge. Verh Dtsch Ges Pathol 62: 39–54
Bleyl U, Kuhn W, Graeff H (1969) Reticuloendothelial Clearance intravasaler Fibrin- monomere in der Milz. Thromb Diath Haemorrh (Stuttg) 22: 87–100
Bleyl U, Nagel W (1968) Untersuchungen zur leukocytären Fibrinolyse. Klin Wochenschr 46: 413–415
Bleyl U, Rieger P, Rossner JA (1978) Indentification of soluble fibrinogen fibrin monomer complexes by non-enzymatic polymerisation in the tissue. Virchows Arch [Pathol Anat] 378: 67–74
Bleyl U, Rossner JA (1976) Globular hyaline microthrombi, their nature and morphogenesis. Virchows Arch [Pathol Anat] 370: 113–128
Blumenstock F, Saba TM, Weber P, Cho E (1976) Purification and biochemical char-acterization of a macrophage stimulating alpha-2-globulin opsonic protein. J Reticuloendothel Soc 19: 157–172
Busch G, Gerdin B (1977) Effect of low molecular weight fibrin degradation products on endothelial cells in culture. 1st Scandinavian Symposium on Atherosclerosis Research Stockholm
Camiolo SM, Thorsen S, Astrup S (1971) Fibrinogenolysis and fibrinolysis with tissue plasminogen activator, urokinase, streptokinase - activated human globulin, and plasmin. Proc Soc Exper Biol Med 138: 277 - 280
Cash JD (1978) Control mechanisms of activator release. In: Davidson JF, Rowan RM, Samama MM, Desnoyers PC (eds) Progress in chemical fibrinolysis and thrombolysis. Raven Press, New York, pp 65–75
Chang ML, Bang NU, Truex L, Boxer L, Mattler LE, Marks CA (1977) Degradation of soluble fibrin complexes, fibrinogen and fibrin by macrophage enzymes. Thromb. Haemost (Stuttg) 38: 102 (Abstract)
Cole ER, Bachmann FW (1977) Purification and properties of a plasminogen activator from pig heart. J Biol Chem 252: 3729–3737
Collen D (1980) On the regulation an control of fibrinolysis. Thromb Haemost (Stuttg) 43: 77–89
Emeis J J, Lindemann J (1976) Rat liver macrophages will not phagocytose fibrin during disseminated intravascular coagulation. Haemostasis 5: 193–210
Gans H, Lowman JT (1967) The uptake of fibrin and fibrin-degradation products by the isolated perfused rat liver. Blood 29: 526–539
Gerdin B, Belew M, Lindquist O, Saldeen T (1979) Effect of an fibrin derived peptide on pulmonary microvascular permeability. In: Saldeen T(ed) The microembolism syndrome
Gordon S, Cohn ZA (1978) Bacille Calmette-Guerin infection in the mouse. Regulation on macrophage plasminogen activator by T-lymphocytes and specific antigen. J Exp Med 147: 1175–1188
Granelli-Piperno A, Vassali JD, Reich E (1977) Secretion of plasminogen activator by human polymorphnuclear leucocytes. J Exp Med 146: 1693–1706
Griffin JH (1978) Role of surface in surface-dependent activation of Hageman factor (blood coagulation factor XII). Proc Natl Acad Sci 75: 1998–2002
Hamilton J, Vassali JD, Reich R (1976) Macrophage plasminogen activator: induction by asbestos is blocked by antiinflammatory steroids. J Exp Med 144: 1689 - 1694
Henry RL (1965) Leukocytes and thrombosis. Thromb Diath Haemorrh (Stuttg) 13: 35–46
Hisano S, Sueishi K, Ishij Y, Tanaka K (1979) Immunhistochemical and histochemical investigations on in vivo thrombosis with urokinase in rabbits. Thromb Haemost (Stuttg) 41: 796–803
Kaplan AP, Castellino FJ, Collen D, Wiman B, Taylor FB (1978) Molecular mechanisms of fibrinolysis in man. Thromb Haemost (Stuttg) 39: 263–283
Kaplan JE, Saba TM (1976) Humoral deficiency and reticuloendothelial depression after traumatic shock. Am J Physiol 230: 7–14
Lewis JH, Szeto IL (1965) Clearance of infused fibrin. Fed Proc 24: 840–845
Lopaciuk S, Bykowska K, Kaczanowska J, Stachurska J, Jelenska M, Kopec M (1979) Effects of neutral proteases of human granulocytes on factor XIII and fibrinogen. Thromb Haemost (Stuttg) 42: 228
Mosesson MW, Umfleet RA (1970) The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and human relationship to fibrinogen and other cold-insoluble fraction components. J Biol Chem 245: 5728–5736
Mullertz S (1953) Plasminogen activator in spontaneously active human blood. Proc Soc Exper Biol Med 82: 291–295
Mullertz S (1956) Mechanism of activation and effect of plasmin in blood. Ph.D. Thesis. Munksgaard, Copenhagen
Niewiarowski S, Prou-Wartelle O (1959) Role of the contact factor (Hageman factor) in fibrinolysis. Thromb Diath Haemorrh 3: 593–603
Ogston D, Ogston CM, Ratnoff OD, Forbes CD (1969) Studies on a complex mechanism for the activation of plasminogen by kaolin and by chloroform: the participation of Hageman factor and additional cofactors. J Clin Invest 48: 1786–1801
Okamoto U, Nagamatsu Y, Anemiya T (1981) Human spleen insoluble fibrinolytic proteinase acting at neutral pH: its partial purification and characterization. Thromb Haemost (Stuttg) 45: 180–185
Plow EF, Edington TS (1975) The cleavage of fibrinogen by leukocyte proteases at physiological pH. J Clin Invest 56: 30–38
Prose PH, Lee L, Balk SD (1965) Electron microscopic study of the phagocytic fibrin- clearing mechanism. Am J Pathol 47: 403–417
Rakoczi I, Wiman B, Colleen D (1978) On the biological significance of the specific interaction between fibrin, plasminogen and antiplasmin. Biochim Biophys Acta 540: 295–300
Ratliff NB, Wilson JW, Mikat E, Hackel DB (1970) Altered leukozytes in pulmonary vessels of dogs in hemorrhagic shock. Microvasc Res 2: 241–256
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
Risberg B, Heideman M (1980) The cascade systems in posttraumatic pulmonary insuf-ficiency. Acta Chir Scand [Suppl] 499: 107
Riifer R (1971) Surfactant inhibition in vitro. X XV. Internat. Congr. of Physiol. Sciences. Proceedings of the International Union of Physiol. Sciences IX.
Ruoslahti E, Vaheri A (1976) Immunological interspecies cross reaction of fibroblast surface antigen (Fibronectin). Immunochemistry 13: 639–642
Saba TM (1975) Reticuloendothelial systemic host defense after surgery and traumatic shock. Circulat Shock 2: 91–107
Saba TM, Blumenstock FA, Scovill WA, Bernhard H (1978) Cryoprecipitate reversal of opsonic-2-surface binding glycoprotein deficiency in septic surgical and trauma patients. Science 201: 622–624
Saldeen T (1980) Fibrin derived peptides as mediators of increased vascular permeability. Acta Chir Scand [Suppl] 499: 67
Schneider J, Baggiolini M (1978) Role of phagocytosis in the activation of macrophages. J Exp Med 148: 1449–1457
Schreiner GE (1975) The search for the uremic toxin. Kidney Int 1: 5
Schreiner GE, Winchester JF (1979) Uremia - 1978 perspective. Chir Nephrol 2: 52
Sherman LA, Harwig S, Lee J (1975) In vitro formation and in vivo clearance of fibrinogen fibrin complexes. J Laborat Clin Med 86: 100–111
Sherman LA, Lee J (1977) Specific binding of soluble fibrin to macrophages. J Exp Med 145: 76 - 85
Sherman LA, Lee J, Jacobson A (1977) Quantitation of the reticuloendothelial system clearance of soluble fibrin. Br J Haematol 37: 231–238
Shermann LA, Lee J, Stewart CC (1977) Release of fibrinolytic enzymes by macrophages in response to soluble fibrin. Thromb Haemost (Stuttg) 38: 46
Starkey PM, Barrett AJ (1976) Neutral proteinases of human spleen. Purification and criteria for homogenicity of elastase and cathepsin G. Biochem J 155: 225–263
Stemberger A, Hormann H (1976) Affinity chromatography on immobilized fibrinogen and fibrin monomer. II. The behavior of cold-insoluble globulin. Hoppe-Seyler’s Z Physiol Chem 357: 1003–1005
Sueishi K, Nanno S, Tanaka K (1981) Permeability enhancing and chemotactic activities of lower molecular weight degradation products of human fibrinogen. Thromb Haemost (Stuttg) 45: 90–94
Thorsen S (1975) Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-amino-carboxylic acids. Biochim Biophys Acta 393: 55–65
Thorsen S (1977) Human urokinase and porcine tissue plasminogen activator. Thesis, University of Copenhagen
Unkeless JC, Gordon S, Reich E (1974) Secretion of plasminogen activator by stimulated macrophages. J Exp Med 139: 834–850
Vassalli JD, Hamilton J, Reich E (1976) Macrophage plasminogen activator: Modulation of enzyme production by antiinflammatory steroids, mitotic inhibitors, and cyclic nucleotides. Cell 8: 271–281
Wallen P (1977) Activation of plasminogen with urokinase and tissue activator. In: Paoletti R, Sherry S (eds) Thrombosis and urokinase. Academic Press, London, pp 91–102
Werb Z, Foley R, Munck A (1978) Glucocorticoid receptors and glucocorticoid-sensitive secretion of neutral proteinases in a macrophage cell line. J Immunol 121: 115–121
Werb Z, Foley R, Munck A (1978) Interaction of glucocorticoids with macrophages. Identification of glucocorticoid receptors in monocytes and macrophages. J Exp Med 147: 1684–1694
Wichert P von (1978) Alveolarwandphysiologie und Surfactant. Verh Dtsch Ges Pathol 62: 29–36
Wilson JW (1972) Pulmonary factors produced by septic shock: Cause or consequence of shock lung? J Reprod Med 8: 307
Wiman B, Wallen P (1977) The specific interaction between plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen. Thromb Res 10: 213–222
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Bleyl, U. (1984). Elimination des Fibrins. In: Scheele, J. (eds) Fibrinklebung. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-69655-8_5
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