Hamostaseologie 1987; 07(05): 128-138
DOI: 10.1055/s-0038-1660542
Originalarbeit
Schattauer GmbH

Hochmolekulares Kininogen : Biochemie und Funktion

Ch. Mannhalter
1   I. Medizinischen Universitätsklinik Wien (Vorstand: Prof. Dr. Dr. h. c. E. Deutsch)
› Author Affiliations
Further Information

Publication History

Publication Date:
25 June 2018 (online)

 

 
  • LITERATUR

  • 1 Abe K, Watanabe N, Kumagai N, Mouri T, Seki T, Yoshinaga K. Circulating plasma kinin in patients with bronchial asthma. Experientia 1967; 23: 626-7.
  • 2 Adam A, Albert A, Boulanger J, Genot D, Demoulin A, Damas J. Influence of oral contraceptives and pregnancy on constituents of the kallikrein - kininogen system in plasma. Clin Chem 1985; 31: 1533-6.
  • 3 Anderson K P, Heath E C. The relationship between the major acute phase protein and the kininogens. J Biol Chem 1985; 260: 12065-71.
  • 4 Arlaud G J, Reboul A, Sim R B, Colomb M G. Interaction of Cl-inhibitor with the Clr and Cls subcomponents of human Cl. Biochem Biophys Acta 1979; 576: 151-62.
  • 5 Barias A, Okamoto H, Greenbaum L M. T-kininogen - the major plasma kininogen in rat adjuvant arthritis. Biochem Biophys Res Comm 1985; 129: 280-6.
  • 6 Bauer J, Kurdowska A, Tran-Thi T A, Budek W, Koj A, Decker K, Heinrich P C. Biosynthesis and secretion of alpha-acute phase globulin in primary cultures of rat hepatocytes. Eur J Biochem 1985; 146: 347-52.
  • 7 Beraldo W T. Formation of bradykinin in anaphylactic and peptone shock. Am J Physiol 1950; 163: 283-9.
  • 8 Bock D E, Shore J O, Tans G, Griffin J H. Protein-protein interactions in contact activation of blood coagulation. Binding of high molecular weight kininogen and the 5-(iodoacetamido) fluorescein-labelled kininogen light chain to prekallikrein, kallikrein, and the separated kallikrein heavy and light chains. J Biol Chem 1985; 260: 12434-43.
  • 9 Bouma B N, Griffin J H. Human blood coagulation factor XI. Purification, properties and mechanism of activation by activated factor XII. J Biol Chem 1977; 252: 6432-7.
  • 10 Bouma B N, Kerbiriou D M, Vlooswijk R A A, Griffin J H. Immunological studies of prekallikrein, kallikrein and high molecular weight kininogen in normal and deficient plasmas and in normal plasma after cold-dependent activation. J Lab Clin Med 1980; 96: 693-709.
  • 11 Bouma B N, Miles L A, Beretta G, Griffin J H. Human plasma prekallikrein. Studies of its activation by activated factor XII and of its inactivation by diisopropyl phosphofluoridate. Biochemistry 1980; 19: 1151-60.
  • 12 Bouma B N, Vlooswijk R A, Griffin J H. Immunologic studies of human coagulation factor XI and its complex with high molecular weight kininogen. Blood 1983; 62: 1123-31.
  • 13 Breckenridge R T, Kellermeyer R W R T. The inflammatory process in acute gouty arthritis. II. The presence of Hageman factor and plasma thromboplastin antecedent in synovial fluid. J Lab Clin Med 1966; 67: 455-60.
  • 14 Briseid K, Qvigstaid E K, Engelstadt M, Kageriov P, Lange-Nielsen F. Assay of factors of the kinin system in plasma from patients with specific exogeneous allergies. Acta Allergol 1976; 31: 297-311.
  • 15 Briseid K, Johansen H T. Activation of factor XII in human plasma: protection by benzamidine of the cofactor function of high molecular weight kininogen. Acta Pharmacol Toxicol (Copenh) 1983; 53: 344-52.
  • 16 Brocklehurst W E, Lahiri S C. Formation and destruction of bradykinin during anaphylaxis. J Physiol (Paris) 1962; 165: 39-40.
  • 17 Chang J J, Scott C F, Colman R W. Role of arginine residues in the coagulant activity of high molecular weight kininogen. Blood 1986; 67: 805-10.
  • 18 Cochrane C G, Revak S D, Wuepper K D. Activation of Hageman factor in solid and fluid phases. A critical role of kallikrein. J Exp Med 1973; 138: 1564-83.
  • 19 Chochrane C G, Griffin J H. The biochemistry and pathophysiology of the contact system of plasma. Adv Immunol 1982; 33: 241-306.
  • 20 Cole T, Inglis A S, Roxburgh C M, Howlett G J, Schreiber G. Major acute phase alpha-protein of the rat is homologous to bovine kininogen and contains the sequence for bradykinin: its synthesis is regulated at the mRNA level. FEBS Lett 1985; 182: 57-61.
  • 21 Colman R W. Activation of plasminogen by human plasma kallikrein. Biochem Biophys Res Commun 1969; 351: 273-9.
  • 22 Colman R W, Bagdasarian A, Talamo R C, Scott C F, Seavay M, Guimares J A, Pierce J V, Kaplan A P. Williams trait: human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways. J Clin Invest 1975; 56: 16050-62.
  • 23 Colman R W, Wong P Y. Participation of Hageman factor dependent pathways in human disease states. Thromb Haemost 1977; 38: 751-75.
  • 24 Colman R W, Wong P Y. Kallikrein-kinirisystem in pathologic conditions. In: Bradykinin, Kallidin and Kallikrein. Erdös E G. (ed) Berlin - Heidelberg - New York: Springer; 1979: 569-608.
  • 25 Cooper N R, Miles L A, Griffin J A. Activation of purified Cl, the first component of complement, by purified plasma kallikrein and plasmin. Thromb Haemost 1979; 42: 251-8.
  • 26 Cordova C, Violi F, Alessandri C, Ferro D, Saliola M, Balsano F. Hageman factor, high molecular weight kininogen, and prekallikrein in chronic liver disease. J Clin Pathol 1986; 39: 1003-5.
  • 27 Damas J, Remade-Volon G, Adam A. Inflammation in the rat paw due to urate crystals. Involvement of the kininsystem. Naunyn Schmiedebergs Arch Pharmacol 1984; 325: 76-9.
  • 28 de Agostini A, Schapira M, Wachtfogel Y T, Colman R W, Carrel S. Human plasma kallikrein and Cl-inhibitor form a complex possessing an epitope that is not detectable on the parent molecules. Demonstration using a monoclonal antibody. Proc Natl Acad Sci USA 1985; 82: 5190-3.
  • 29 Derkx F H, Bouma B N, Schalekamp M A. Prorenin-renin conversion by the contact activation system in human plasma: role of plasma protease inhibitors. J Lab Clin Med 1984; 103: 560-73.
  • 30 Deutsch E, Dragosics B, Kopsa H, Mannhalter C, Rainer H. Prekallikrein, HMW-kininogen and factor XII in various disease states. Thromb Res 1983; 31: 351-64.
  • 31 Di Scipio R G. The activation of the alternative pathway of C3 convertase by human plasma kallikrein. Immunology 1982; 45: 587-95.
  • 32 Dittman B, Steger A, Wimmer R, Fritz H. A convenient large-scale preparation of high molecular weight kininogen from human plasma. Hoppe-Seyler’s Z Physiol Chem 1981; 362: 919-27.
  • 33 Esnard F, Gauthier F. Rat alpha-cysteine proteinase inhibitor. An acute phase reactant identical with alpha-acute phase globulin. J Biol Chem 1983; 258: 12443-7.
  • 34 Gallimore M J, Aasen A O, Lyngaas K H N, Larsbraaten M, Amundsen E. Falls in plasma levels of prekallikrein, high molecular weight kininogen and kallikrein inhibitors during lethal endotoxin shock in dogs. Thromb Res 1978; 12: 307-18.
  • 35 Ginsberg M H, Jaques B, Cochrane C G, Griffin J H. Urate crystal dependent cleavage of Hageman factor in human plasma and synovial fluid. J Lab Clin Med 1980; 95: 497-506.
  • 36 Gounaris A D, Brown M A, Barrett A J. Human plasma a-cysteine proteinase inhibitor. Purification by affinity chromatography, characterization, and isolation of an active fragment. Biochem J 1984; 221: 445-52.
  • 37 Greengard J S, Griffin J H. Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry 1984; 23: 6863-9.
  • 38 Griffin J H, Cochrane C G. Mechanism for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor. Proc Natl Acad Sci USA 1976; 73: 2554-8.
  • 39 Griffin J H. Role of surface in surface-dependent activation of Hageman factor (Blood coagulation factor XII). Proc Natl Acad Sci USA 1978; 75: 1998-2002.
  • 40 Gustafsen E J, Schutsky D, Knight L C, Schmaier A H. High molecular weight kininogen binds to unstimulated platelets. J Clin Invest 1986; 78: 310-8.
  • 41 Han Y N, Komiya M, Iwanaga S, Suzuki T. Studies on the primary structure of bovine high molecular weight kininogen. Amino acid sequence of a fragment (“histidine rich peptide”) released by kallikrein. J Biochem 1975; 77: 55-68.
  • 42 Han Y N, Kato H, Iwanaga S, Komiya K. Actions of urinary kallikrein on plasma kininogens. J Biochem 1978; 83: 223-35.
  • 43 Hayashi I, Oh-Ishi S, Kato H, Enjyoji K, Iwanaga S, Nakano T. Identification of T-kininogen in high and low molecular weight kininogen deficient rat (Brown Norway Katholiek strain). Thromb Res 1985; 39: 313-8.
  • 44 Higashiyama S, Ohkubo I, Ishiguro H, Kunimatsu M, Sawaki K, Sasaki M. Human high molecular weight kininogen as thiol proteinase inhibitor: presence of the entire inhibitor capacity in the native form of heavy chain. Biochemistry 1986; 25: 1669-75.
  • 45 Hirsch E F, Nagajima T, Oshima G, Erdös E G, Herman C M. Kininsystem responses in sepsis after trauma in man. J Surg Res 1974; 17: 147-53.
  • 46 Hruby M A, Honig G R, Shapira E. Immunoquantitation of Hageman factor in urine and plasma of children with nephrotic syndrome. J Lab Clin Med 1980; 96: 501-10.
  • 47 Iwanga S, Kato H, Sugo T, Ikari N, Hashimoto N, Fuji S. The kallikrein-kinin-system: a functional role of plasma kallikrein and kininogen in blood coagulation. In: Biological Functions of Proteinase. Holzer H, Tschesche H. (eds) Berlin: Springer; 1979: 243-59.
  • 48 Jacobs A, Mannhalter C, Margalit R, Schiffman S. Contact activation of factor XI. Br J Haematol 1981; 49: 77-86.
  • 49 Johansen H T, Briseid K. Reduced cofactor function of human high molecular weight kininogen induced by human plasma kallikrein. Acta Pharmacol Toxicol 1984; 55: 25-32.
  • 50 Kageyama R, Kitamura N, Ohkubo H, Nakanishi S. Differential expression of the multiple forms of rat prekininogen mRNAs after acute inflammation. J Biol Chem 1985; 260: 12060-4.
  • 51 Kallen R J, Lee S-K. A study of the plasma kinin-generating system in children with the minimal lesion, idiopathic nephrotic syndrome. Pediatr Res 1975; 09: 705-9.
  • 52 Kalter E S, Daha M R, ten Cate J W, Verhoef J, Bouma B N. Activation and inhibition of Hageman factor-dependent pathways and the complement system in uncomplicated bacteremia or bacterial shock. J Infect Dis 1985; 151: 1019-27.
  • 53 Kamitani T, Little M H, Ellis E F. Evidence for a possible role of the brain kallikreinkinin system in the modulation of the cerebral circulation. Circ Res 1985; 545-52.
  • 54 Karges H E, Egbring R, Merte D. Störungen des Gerinnungs-, Fibrinolyse-und Komplementsystems beim septischen Schock. Behring Inst Mitt 1986; 79: 154-63.
  • 55 Kato H, Han Y N, Iwanaga S, Hashimoto N, Sugo T, Fujii S, Suzuki R. Mammalian plasma kininogens, their structures and functions. In: Kininogenases 4. Haberland G, Rohen J W, Suzuki T. (eds) Stuttgart: Schattauer; 1977: 63-72.
  • 56 Kato H, Sugo T, Ikari N, Hashimoto N, Fujii S. Role of bovine HMW kininogen in contact mediated activation of factor XII: demonstration of a nicked form “active kininogen”, with maximal cofactor activity by limited proteolysis. Thromb Haemost 1979; 42: 262 (Abstr)
  • 57 Kato H, Nagasawa S, Iwanaga S. HMW and LMW kininogens. Methods Enzymol 1981; 80: 172-98.
  • 58 Kellermann J, Lottspeich F, Henschen A, Mueller-Esterl W. Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heave chain and evidence for its evolution by gene triplication. Eur J Biochem 1986; 154: 471-8.
  • 59 Kellermeyer R W, Breckenridge R T. Inflammatory process in acute gouty arthritis. I. Activation of Hageman factor by sodium urate crystals. J Lab Clin Med 1965; 65: 307-15.
  • 60 Kellermeyer R W. Inflammatory process in acute gouty arthrits. III. Vascular permeability-enhancing activity in normal human synovial fluid; induction by Hageman factor activators and inhibition by Hageman factor antiserum. J Lab Clin Med 1967; 70: 372-83.
  • 61 Kerbiriou D M, Griffin J. Human high molecular weight kininogen. Studies of structure-function relationships and of proteolysis of the molecule occurring during contact activation of plasma. J Biol Chem 1979; 254: 12020-7.
  • 62 Kerbiriou D M, Bouma B N, Griffin J H. Immunochemical studies of human high molecular weight kininogen and of its complexes with plasma prekallikrein or kallikrein. J Biol Chem 1980; 255: 3952-8.
  • 63 Kerbiriou D M, Garcio F O, Larrieu M J. Radioimmunoassay of human HMW and LMW kininogens in plasma and platelets. Brit J Haematol 1984; 56: 273-86.
  • 64 Kitamura N, Takagaki Y, Furuto S, Tanaka T, Nawa H, Nakanishi S. A single gene for bovine high molecular weight and low molecular weight kininogens. Nature 1983; 305: 545-9.
  • 65 Kitamura N, Kitagawa H, Fukushima D, Takagaki Y, Miyata T, Nakanishi S. Structural organisation of the human kininogen gene and a model for its evolution. J Biol Chem 1985; 260: 8610-7.
  • 66 Kodama J, Uchida K, Yoshimura S, Katayama Y, Kushiro H, Yutani C, Funahashi S, Takamiya O, Matsumoto Y, Ando Y. et al. Studies of four Japanese families with hereditary angioneurotic edema: simultaneous activation of plasma protease systems and exogenous triggering stimuli. Blut 1984; 49: 405-18.
  • 67 Koide T, Foster D, Yoshitake S, Davie E W. Amino acid sequence of human histidine-rich glycoprotein derived from the nucleotide sequence of its cDNA. Biochemistry 1986; 25: 2220-5.
  • 68 Kurachi K, Davie E W. Activation of human factor XI (plasma thromboplastin antecedent) by factor Xlla (activated Hageman factor). Biochemistry 1977; 16: 5831-9.
  • 69 Lacombe M J, Varet B, Levy J-R. A hitherto undescribed plasma factor activity at the contact phase of blood coagulation (Flaujeac factor): case report and coagulation studies. Blood 1975; 46: 761-8.
  • 70 Lange L G, Carvalho A, Bagdasarian A, Lahiri B, Colman R W. Activation of Hageman factor in the nephrotic syndrome. Am J Med 1974; 56: 565-9.
  • 71 Lasson A. Acute pancreatitis in man. A clinical and biochemical study of pathophysiology and treatment. Scand J Gastroenterol 1984; (Suppl) 99: 1-57.
  • 72 Lasson A, Ohlsson K. On the potential role of trypsin and trypsin inhibitors in acute pancreatitis. Adv Exp Med Biol 1984; 167: 477-87.
  • 73 Lasson A, Ohlsson K. Changes in the kallikrein kininsystem during acute pancreatitis in man. Thromb Res 1984; 35: 27-41.
  • 74 Lottspeich F, Kellermann J, Henschen A, Rauth G, Mueller-Esterl W. Human low-molecular mass kininogen. Amino-acid sequence of the light chain; homology with other protein sequences. Eur J Biochem 1984; 142: 227-32.
  • 75 Lukjan H. The kinin system in allergic state. Allerg Immunol (Leipz) 1972; 18: 25-30.
  • 76 Lutcher C L. Reid trait: A new expression of high molecular weight kininogen (HMW-Kininogen) deficiency. Clin Res 1976; 34: 47.
  • 77 Machleidt W, Borchart U, Fritz H, Brzin J, Ritonja A, Turk V. Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler’s Z Physiol Chem 1983; 364: 1481-6.
  • 78 Maier M, Spragg J, Schwartz L B. Inactivation of human high molecular weight kininogen by human mast cell tryptase. J Immunol 1983; 130: 2352-6.
  • 79 Maier-Hauff K, Baethman A J, Lange M, Schuerer L, Unterberg A. The kallikreinkininsystem as a mediator in vasogenic brain edema. Part 2: Studies on kinin formation in focal and perifocal brain tissue. J Neurosurg 1984; 61: 97-106.
  • 80 Maki M, Soga K, Gotoh K. The kininforming enzyme system in pregnancy and obstetrical DIC. Bibl Haematol 1983; 49: 239-46.
  • 81 Mandle R J, Colman R W, Kaplan A P. Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma. Proc Natl Acad Sci USA 1976; 73: 4179-83.
  • 82 Mandle R J, Kaplan A P. Hageman factor substrates. Human plasma prekallikrein: mechanism of activation by Hageman factor and participation in Hageman factor dependent fibrinolysis. J Biol Chem 1977; 252: 6097-104.
  • 83 Mannhalter C, Schifman S, Jacobs A. Trypsin activation of human factor XI. J Biol Chem 1980; 255: 2667-9.
  • 84 Mannhalter C, Deutsch E, Kopsa H. Clotting activities and antigen concentrations of contact factors in kidney disease. Thromb Res 1985; 39: 475-84.
  • 85 Meier H K, Webster M E, Mandle R, Colman R W, Kaplan A P. Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein. J Clin Invest 1977; 60: 18-31.
  • 86 Melmon K L, Webster M E, Goldfinger S E, Seegmiller J E. Presence of kinin in inflammatory synovial effusion from arthritides of varying etiologies. Arthritis Rheum 1967; 10: 13-20.
  • 87 Morrison D C, Cochrane C G. Direct evidence for Hageman factor (factor XII) activation by bacterial lipopolysaccharides (endotoxins). J Exp Med 1974; 140: 797-811.
  • 88 Müller-Esterl W, Vohle-Timmermann M, Boos B, Dittmann B. Purification and properties of human low molecular weight kininogen. Biochim Biophys Acta 1982; 706: 145-52.
  • 89 Müller-Esterl W, Rauth G, Fritz H, Lottspeich F, Henschen A. Human kininogens. In: Kininogenase/Kallikrein VI. Haberland G L, Rohen J W, Fritz H, Huber P. (eds) Stuttgart: Schattauer; 1983: 3-28.
  • 90 Müller-Esterl W, Fritz H, Machleidt W, Ritonja A, Brzin J, Kotnik M, Turk V, Kellermann J, Lottspeich F. Human plasma kininogens are identical with a2-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data. FEBS Lett 1985; 182: 310-4.
  • 91 Müller-Esterl W, Iwanaga S, Nakanishi S. Kininogens revisited. Trends Biochem Sci 1986; 11: 336-9.
  • 92 Oh-Ishi S, Ueno A, Uchida Y, Katori M, Hayashi H, Koya H, Kitamjima K, Kimura J. Fujiwara trait: the first case of kininogen deficiency in Japan. Adv Exp Med Biol 1978; 120B: 93-9.
  • 93 Oh-Ishi S, Ueno A, Uchida Y, Katori M, Hayashi H, Koya H, Kitamjima K, Kimura J. Abnormalities in the contact activation through factor XII in Fujiwara trait: a deficiency in both high and low molecular weight kininogens with low level of prekallikrein. Tohoku J Exp Med 1981; 133: 67-80.
  • 94 Ohkubo I, Kurachi K, Takasawa T, Shiokawa H, Sasaki M. Isolation of a human cDNA for a2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 1984; 23: 5691-7.
  • 95 Okamoto H, Greenbaum L M. Isolation and structure of T-kinin. Biochem Biophys Res Commun 1983; 112: 701-8.
  • 96 Okamoto H, Greenbaum L M. Kininogen substrates for trypsin and cathepsin D in human, rabbit and rat plasma. Life Sci 1983; 32: 2007-13.
  • 97 Proud D, Pierce J V, Pisano J J. Radioimmunoassay of human HMW kininogen in normal and deficient patients. J Lab Clin Med 1980; 95: 563-74.
  • 98 Ratnoff O D, Saito H. Interactions among Hageman factor, plasma prekallikrein, high molecular weight kininogen, and plasma thromboplastin antecedent. Proc Natl Acad Sci USA 1979; 76: 958-61.
  • 99 Ratnoff O D, Saito H. Surface-mediated reactions. Curr Top Hematol 1979; 02: 1-57.
  • 100 Saito H, Ratnoff O D, Waldmann R, Abraham J P. Fitzgerald trait. Deficiency of a hitherto unrecognized agent, Fitzgerald factor, participating in surface-mediated reactions of clotting, fibrinolysis, generation of kinins, and the property of diluted plasma enhancing vascular permeability (PF/dil). J Clin Invest 1975; 55: 1082-9.
  • 101 Saito H, Goldsmith G H, Waldmann R. Fitzgerald factor (high molecular weight kininogen) clotting activity in human plasma in health and disease; and in various animal plasmas. Blood 1976; 48: 941-7.
  • 102 Saito H, Poon M-C, Vicic W, Goldsmith G H, Menitove J E. Human plasma prekallikrein (Fletcher factor) clotting activity and antigen in health and disease. J Lab Clin Med 1978; 92: 84-95.
  • 103 Saugstad O D. Pathogenetic aspects of respiratory distress syndrome in adults and newborns. Experimental and clinical data. Eur Surg Res 1984; 16 Suppl 2 113-9.
  • 104 Schapira M, Silver L D, Scott C F, Schmaier A H, Prograis L J, Curd J G, Colman R W. Prekallikrein activation and high molecular weight kininogen consumption in hereditary angioedema. N Engl J Med 1983; 308: 1050-3.
  • 105 Schapira M, Gardaz J P, Py P, Lew P D, Perrin L H, Suter P M. Prekallikrein activation in the adult respiratory distress syndrome. Bull Eur Physiopathol Respir 1985; 21: 237-41.
  • 106 Schiffman S, Lee P. Partial purification and characterization of contact activation cofactor. J Clin Invest 1975; 56: 1082-92.
  • 107 Schiffman S, Mannhalter C, Tyner K D. Human high molecular weight kininogen. Effects of cleavage by kallikrein on protein structure and procoagulant activity. J Biol Chem 1980; 255: 6433-8.
  • 108 Schmaier A H, Smith P M, Purdon A D, White J G, Colman R W. High molecular weight kininogen: localization in unstimulated and activated platelets, and activation by platelet calpain(s). Blood 1986; 67: 119-30.
  • 109 Scott C F, Silver L D, Schapira M, Colman R W. Cleavage of human high molecular weight kininogen markedly enhances its coagulant activity. Evidence that this molecule exists as a procofactor. J Clin Invest 1984; 73: 954-62.
  • 110 Scott C F, Silver L D, Purdon A D, Colman R W. Cleavage of human high molecular weight kininogen by Factor XIa in vitro. Effect on structure and function. J Biol Chem 1985; 260: 10856-63.
  • 111 Silva R O, Cunha S P, Peracoli J C, Duarte G, Martinez A R. Kininogen, esterase and kininase activities in human peripheral venous plasma and in plasma from the intervillous space of human placenta, before and during labor. Braz J Med Biol Res 1984; 17: 27-34.
  • 112 Smith O, Gilbert M, Owen W G. Tissue plasminogen activator release in vivo in response to vasoactive agents. Blood 1985; 66: 835-9.
  • 113 Smith P L, Kagey-Sobotka A, Bleecker E R, Traystman R, Kaplan A P, Gralnick H, Valentine M D, Permutt S, Lichtenstein L M. Physiologic manifestations of human anaphylaxis. J Clin Invest 1980; 66: 1072-80.
  • 114 Sueyoshi T, Enjyoji K, Shimada T, Kato H, Iwanaga S, Band Y, Kominami E, Katunuma N. A new function of kininogens as thiol-proteinase inhibitors: inhibition of papain and cathepsin B, H and L by bovine, rat and human plasma kininogens. FEBS Lett 1985; 182: 193-5.
  • 115 Sugo T, Ikari N, Kato H, Iwanaga S, Fujii S. Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin mediated activation of factor XII (Hageman factor). Biochemistry 1980; 19: 3215-20.
  • 116 Sugo T, Kato H, Iwanaga S, Takada K, Sakakibara S. Kinetic studies on surface-mediated activation of bovine factor XII and prekallikrein. Effects of kaolin and high-Mr kininogen on the activation reactions. Eur J Biochem 1985; 146: 43-50.
  • 117 Takagaki Y, Kitamura N, Nakanishi S. Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens. J Biol Chem 1985; 260: 8601-9.
  • 118 Thompson R E, Mandle Jr. R, Kaplan A P. Association of factor XI and high molecular weight kininogen in human plasma. J Clin Invest 1977; 60: 1376-80.
  • 119 Thompson R E, Mandle Jr. R, Kaplan A P. Studies of binding of prekallikrein and factor XI to high molecular weight kininogen and its light chain. Proc Natl Acad Sci USA 1979; 76: 4862-6.
  • 120 Travis J, Salvessen G S. Human plasma proteinase inhibitors. Ann Rev Biochem 1983; 62: 655-709.
  • 121 van der Graaf F, Tans G, Bouma B N, Griffin J H. Isolation and functional properties of the heavy and light chains of human plasma kallikrein. J Biol Chem 1982; 257: 14300-5.
  • 122 van der Graaf F, Koedam J A, Griffin J H, Bouma B N. Interaction of human plasma kallikrein and its light chain with Cl inhibitor. Biochemistry 1983; 22: 4860-6.
  • 123 van Iwaarden F, Bouma B N. Immunocytochemical localization of contact activation factors and inhibitors in human blood platelets. Thromb Haemost 1985; 54: 1493 (Abstr)
  • 124 van Iwaarden F, de Groot P G, Bouma B N. Immunocytochemical localization of contact factors and their inhibitors in cultured human endothelial cells. Thromb Haemost 1985; 54: 315 (Abstr).
  • 125 Vaziri N D, Toohey J, Powers D, Keegan K, Gupta A, Alikhani S, Mashood M, Barbari A. Activation of intrinsic coagulation pathway in pre-eclampsia. Am J Med 1986; 80: 103-7.
  • 126 Velasco F, Torres A, Guerrero A, Andres P, Guerrero R, Aljama P, Alvarez F. Behaviour of the contact phase of blood coagulation in the adult respiratory distress syndrome (ARDS). Thromb Haemost 1986; 55: 357-60.
  • 127 Waldman R, Abraham J P, Rebuck J W, Caldwell J, Saito H, Ratnoff O D. Fitzgerald factor: a hitherto unrecognized coagulation factor. Lancet 1975; I: 949-52.
  • 128 Walsh P N, Tuszynski G P, Greengard J S, Griffin J H. The possible role of platelets in bypassing the contact phase of blood coagulation. Haematologia (Budap) 1984; 17: 169-78.
  • 129 Warn-Cramer B J, Bajaj S P. Stoichiometry of binding of high molecular weight kininogen to factor XI/XIa. Biochem Biophys Res Commun 1985; 133: 417-22.
  • 130 Wiggins R C, Bouma B N, Cochrane C G, Griffin J H. Role of high molecular weight kininogen in surface-binding and activation of coagulation factor XI and prekallikrein. Proc Natl Acad Sci USA 1977; 74: 4636-40.
  • 131 Wiggins R C, Loskutoff D, Cochrane C G, Griffin J H, Edgington T E. Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells. J Clin Invest 1980; 65: 197-206.
  • 132 Wiggins R G, Giclas P C, Henson P M. Chemotactic activity generated from the fifth component of complement by plasma kallikrein of the rabbit. J Exp Med 1981; 153: 1391-404.
  • 133 Werle E, Götze W, Keppler A. Über die Wirkung des Kallikreins auf den isolierten Darm und über eine neue darmkontrahierende Substanz. Biochem Z 1937; 289: 217-33.
  • 134 Wuepper K D, Miller P R, Lacombe M J. Flaujeac trait: deficiency of human plasma kininogen. J Clin Invest 1975; 56: 1663-72.