Contact Activation: A Revision

• References

• 1 Roche e Silva M, Beraldo WT, Rosenfeld G. Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Am J Physiol 1949; 150: 261-273
• 2 Colman RW, Bagdasarian A, Talamo RC, Scott CF, Seavey M, Guimaraes JA, Pierce JV, Kaplan AP, 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: 1650-1662
• 3 Wuepper KD, Miller DR, Lacombe MJ, Flaujeac trait. Deficiency of human plasma kininogen. J Clin Invest 1975; 56: 1663-1672
• 4 Saito H, Ratnoff OD, Waldmann R, Abraham JP, 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: 1082-1089
• 5 Rapaport SI, Rao LVM. The tissue factor pathway: how it has become a “Prima Ballerina”. Thromb. Haemost 1995; 74: 07-17
• 6 Gailiani D, Broze Jr GJ. Factor XI activation in a revised model of blood coagulation. Science 1991; 253: 909-912
• 7 Ishiguro H, Higashiyama S, Ohkubo I, Sasaki M. Heavy chain of human high molecular weight and low molecular weight kininogen binds calcium ion. Biochemistry 1987; 26: 7450-7458
• 8 Croxatto HR, Boric MP, Roblero J, Albertini R, Silva R. Digestive process and regulation of renal excretory function. Pepsanurin and prokinins inhibitors of diuresis mediated by atrial natriuretic peptide. Rev Med Chile 1995; 122: 1162-1172
• 9 Salvesen G, Parkes C, Abrahamson M, Grubb A, Barrett AJ. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem J 1986; 234: 429-434
• 10 Schmaier AH, Bradford H, Silver LD, Farber A, Scott CF, Schutsky D, Colman RW. High molecular weight kininogen is an inhibitor of platelet calpain. J Clin Invest 1986; 77: 1565-1573
• 11 Bradford HN, Schmaier AH, Colman RW. Kinetics of inhibition of platelet calpain II by human kininogens. Biochem J 1990; 270: 83-90
• 12 Herwald H, Hasan AAK, Godovac-Zimmermann J, Schmaier AH, Muller-Esterl W. Identification of an endothelial cell binding site on kininogen domain D3. J Biol Chem 21995 70: 14634-14642
• 13 Meloni FJ, Schmaier AH. Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation. J Biol Chem 1991; 266: 6786-6794
• 14 Jiang YP, Muller Esterl W, Schmaier AH. Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets. J Biol Chem 1992; 267: 3712-3717
• 15 Hasan AAK, Amenta S, Schmaier AH. Bradykinin and its metabolite, Arg-Pro-Pro-Gly-Phe, are selective inhibitors of α-thrombin-induced platelet activation. Circulation 1996; 94: 517-528
• 16 Tayeh MA, Olson ST, Shore JD. Surface-induced alterations in the kinetic pathway for cleavage of human high molecular weight kininogen by plasma kallikrein. J Biol Chem 1994; 269: 16318-16325
• 17 Hasan AA, Zhang J, Samuel M, Schmaier AH. Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells. Thromb Haemost 1995; 74: 1088-1095
• 18 Crutchley DJ, Ryan JW, Ryan US, Fisher GH. Bradykinin-induced release of prostacyclin and thromboxanes from bovine pulmonary artery endothelial cells. Studies with lower homologs and calcium antagonists. Biochim Biophys Acta 1983; 751: 099-107
• 19 Hong SL. Effect of bradykinin and thrombin on prostacyclin synthesis in endothelial cells from calf and pig aorta and human umbilical cord vein. Thromb Res 1980; 18: 787-796
• 20 Holland JA, Pritchard KA, Pappolla MA, Wolin MS, Rogers NJ, Stemerman MB. Bradykinin induces superoxide anion release from human endothelial cells. J Cell Physiol 1990; 143: 21-25
• 21 Smith D, Gilbert M, Owen WG. Tissue plasminogen activator release in vivo in response to vasoactive agents. Blood 1983; 66: 835-839
• 22 Palmer RMJ, Ferrige AG, Moncada S. Nitric oxide release accounts for the biologic activity of endothelium-derived relaxing factor. Nature 1987; 327: 524-526
• 23 Nakashima M, Mombouli JV, Taylor AA, Vanhoutte PM. Endothelium-dependent hyperpolarization caused by bradykinin in human coronary arteries. J Clin Invest 1993; 92: 2867-2871
• 24 Boulanger C, Schini VB, Moncada S, Vanhoutte PM. Stimulation of cyclic GMP production in cultured endothelial cells of the pig by bradykinin, adenosine diphosphate, calcium ionophore A23187 and nitric oxide. Br J Pharmacol 1990; 101: 152-156
• 25 Busse R, Mulsch A. Induction of nitric oxide synthase by cytokines in vascular smooth muscle cells. FEBS Lett 1990; 275: 87-90
• 26 Dixon BS, Breckon R, Fortune J, Vavrek RJ, Stewart JM, Marzec-Calvert R, Linas SL. Effects of kinins on cultured arterial smooth muscle. Am J Physiol 1990; 258: C299-C308
• 27 Hasan AAK, Cines DB, Zhang J, Schmaier AH. The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain. J Biol Chem 1994; 269: 31822-31830
• 28 Weisel JW, Nagaswami C, Woodhead JL, DeLa Cadena RA, Page JD, Colman RW. The shape of high molecular weight kininogen: Organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopy. J Biol Chem 1994; 269: 10100-10106
• 29 Hasan AAK, Cines DB, Ngaiza JR, Jaffe EA, Schmaier AH. High-molecular-weight kininogen is exclusively membrane bound on endothelial cells to influence activation of vascular endothelium. Blood 1995; 85: 3134-3143
• 30 Zini JM, Schmaier AH, Cines DB. Bradykinin regulates the expression of kininogen binding sites on endothelial cells. Blood 1993; 81: 2936-2946
• 31 Meloni FJ, Gustafson EJ, Schmaier AH. High molecular weight kininogen binds to platelets by its heavy and light chains and when bound has altered susceptibility to kallikrein cleavage. Blood 1992; 79: 1233-1244
• 32 Hasan AAK, Cines DB, Herwald H, Schmaier AH, Muller-Esterl W. Mapping the cell binding site on high molecular weight kininogen domain 5. J Biol Chem 1995; 270: 19256-19261
• 33 DeLa CadenaRA, Colman RW. The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface. Prot Sci 1992; 01: 151-160
• 34 Ben NasrAB, Herwald H, Muller-Esterl W, Bjorck L. Human kininogens interact with M protein, a bacterial surface protein and virulence determinant. Biochem J 1995; 305: 173-180
• 35 Tait JF, Fujikawa K. Identification of the binding site for plasma prekallikrein in human high molecular weight kininogen. A region from residues 185 to 224 of the kininogen light chain retains full binding activity. J Biol Chem 1986; 261: 15396-15401
• 36 Tait JF, Fujikawa K. Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. J Biol Chem 1987; 262: 11651-11656
• 37 Schmaier AH, Schutsky D, Farber A, Silver LD, Bradford HN, Colman RW. Determination of the bifunctional properties of high molecular weight kininogen by studies with monoclonal antibodies directed to each of its chains. J Biol Chem 1987; 262: 1405-1411
• 38 Greengard JS, Heeb MJ, Ersdal E, Walsh PN, Griffin JH. Binding of coagulation factor XI to washed human platelets. Biochemistry 1986; 25: 3884-3890
• 39 Lenich C, Pannell R, Gurewich V. Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture. Thromb Haemost 1995; 74: 698-703
• 40 Motta G, Hasan AAK, Cines DB, Schmaier AH. High molecular weight kininogen and prekallikrein assembly on endothelial cells produce plasminogen activation independent of Factor XII. Blood 1995; 86 S 374a (abstract)
• 41 Greengard JS, Griffin JH. Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry 1984; 23: 6863-6869
• 42 Wachtfogel YT, DeLa CadenaRA, Kunapuli SP, Rick L, Miller M, Schultze RL, Altieri DC, Edgington TS, Colman RW. High molecular weight kininogen binds to Mac-1 on neutrophils by its heavy chain (domain 3) and its light chain (domain 5). J Biol Chem 1994; 269: 19307-19312
• 43 Gustafson EJ, Lukasiewicz H, Wachtfogel YT, Norton KJ, Schmaier AH, Niewiarowski S, Colman RW. High molecular weight kininogen inhibits fibrinogen binding to cytoadhesins of neutrophils and platelets. J Cell Biol 1989; 109: 377-389
• 44 Herwald H, Dedio J, Kellner R, Loos M, Mueller-Esterl W. Isolation and characterization of the kininogen-binding protein p33 from endothelial cells: Identity with the gClq receptor. J Biol Chem 1996; 271: 13040-13047
• 45 Joseph K, Ghebrehiwet B, Peerschke EIB, Reid KBM, Kaplan AP. Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: Identity with the receptor that binds to the globular “heads” of Clq (gC1q-R). Proc Natl Acad Sci USA 1996; 93: 8552-8557
• 46 Colman RW, Pixley RA, Najamunnisa S, Yan WY, Wang J, Mazar A, McCrae KR. High molecular weight kininogen binds to the vitronectin binding domain(s) on the endothelial cell receptor. Circulation 1996; 94: 01-42 (abstract)
• 47 Wei Y, Lukashev M, Simon DI, Bodary SC, Rosenberg S, Doyle MV. Chapman HA: Regulation of integrin function by the urokinase receptor. Science 1996; 273: 1551-1555
• 48 Hembrough TA, Vasudevan J, Allietta MM, Glass WF II, Gonias SL. A cytokeratin 8-like protein with plasminogen-binding activity is present on the external surface of hepatocytes, HepG2 cells, and breast carcinoma cell line. J Cell Sci 1995; 108: 1071-1082
• 49 Hembrough TA, Li L, Gonias SL. Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell-associated plasminogen by tissue-type plasminogen activator. J Biol Chem 1996; 271: 25684-25691
• 50 Ratnoff OD, Busce FJ, Sheon RP. The demise of John Hageman. N Engl J Med 1968; 279: 760-761
• 51 Colman RW. Contributions of Mayme Williams to the elucidation of the multiple functions of the plasma kininogens. Thromb Haemost 1992; 68: 099-101
• 52 Goodnough LT, Saito H, Ratnoff OD. Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: a report of 21 patients and a review of 50 previously reported cases. [Review]. Medicine (Baltimore) 1983; 62: 248-255
• 53 Jespersen J, Munkvad S, Pedersen OD, Gram J, Kluft C. Evidence for a role of factor XH-dependent fibrinolysis in cardiovascular diseases. Ann N Y Acad Sci 1992; 667: 454-456
• 54 Munkvad S, Jespersen J, Gram J, Kluft C. Long-lasting depression of the factor XII-dependent fibrinolytic system in patients with myocardial infarction undergoing thrombolytic therapy with recombinant tissue-type plasminogen activator: a randomized placebo-controlled study. J Am Coll Cardiol 1991; 17: 957-962
• 55 Schmaier AH, Bradford HN, Lundberg D, Farber A, Colman RW. Membrane expression of platelet calpain. Blood 1990; 75: 1273-1281
• 56 Saido T, Suzuki H, Yamazaki H, Tanoue K, Suzuki K. In situ capture of m-calpain activation of platelets. J Biol Chem 1993; 268: 7422-7426
• 57 Coller BS. Effects of tertiary amine local anesthetics on von Willebrand factor-dependent platelet function: alteration of membrane reactivity and degradation of GPIb by a calcium-dependent protease(s). Blood 1982; 60: 731-743
• 58 Puri RN, Gustafson EJ, Zhou FX, Bradford H, Colman RF, Colman RW. Inhibition of thrombin-induced platelet aggregation by high molecular weight kininogen. Trans Assoc Am Physicians 1987; 100: 232-240
• 59 Schmaier AH, Meloni FJ, Nawarawong W, Jiang YP. PPACK-thrombin is a noncompetitive inhibitor of alpha-thrombin binding to human platelets. Thromb Res 1992; 67: 479-489
• 60 Majima M, Sunahara N, Harada Y, Katori M. Detection of the degradation products of bradykinin by enzyme immunoassays as markers for the release of kinin in vivo. Biochem Pharmacol 1993; 45: 559-567
• 61 Shima C, Majima M, Katori M. A stable metabolite, Arg-Pro-Pro-Gly-Phe, of bradykinin in the degradation pathway in human plasma. Jpn J Pharmacol 1992; 60: 111-119
• 62 Niewiarowski S, Prou-Wartelle O. Role of the contact factor (Hageman factor) in fibrinolysis. Thromb Diath Haemorrh 1959; 03: 593-598
• 63 Ichinose A, Fujikawa K, Suyama T. The activation of prourokinase by plasma kallikrein and its inactivation by thrombin. J Biol Chem 1986; 261: 3486-3489
• 64 Loza JP, Gurewich V, Johnstone M, Pannell R. Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: a mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis. Thromb Haemost 1994; 71: 347-352
• 65 Gurewich V, Johnstone M, Loza JP, Pannell R. Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis. FEBS Lett 1993; 318: 317-321