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Volumn 19, Issue 9, 1999, Pages 2245-2250

Kininogens are antithrombotic proteins in vivo

Author keywords

Antithrombotic; Arterial thrombosis; Fibrinolysis; Kininogens; Rats

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 5; FIBRINOGEN; KININOGEN; THROMBIN;

EID: 0032877560     PISSN: 10795642     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.ATV.19.9.2245     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 84931128415 scopus 로고
    • Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin
    • 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;150:261-272.
    • (1949) Am J Physiol. , vol.150 , pp. 261-272
    • Roche E Silva, M.1    Beraldo, W.T.2    Rosenfeld, G.3
  • 2
    • 0016774847 scopus 로고
    • Williams trait: Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways
    • 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.
    • (1975) J Clin Invest. , vol.56 , pp. 1650-1662
    • Colman, R.W.1    Bagdasarian, A.2    Talamo, R.C.3    Scott, C.F.4    Seavey, M.5    Guimaraes, J.A.6    Pierce, J.V.7    Kaplan, A.P.8
  • 3
    • 0021800408 scopus 로고
    • Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens: Primary structures of two human prekininogens
    • 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;260:8601-8609.
    • (1985) J Biol Chem. , vol.260 , pp. 8601-8609
    • Takagaki, Y.1    Kitamura, N.2    Nakanishi, S.3
  • 5
    • 0029884794 scopus 로고    scopus 로고
    • Thrombin-induced platelet aggregation is inhibited by the heptapeptide Leu271-Ala277 domain 3 in the heavy chain of high molecular weight kininogen
    • Kunapuli SP, Bradford HN, Jameson BA, DeLa Cadena RA, Rick L, Wassell RP, Colman RW. Thrombin-induced platelet aggregation is inhibited by the heptapeptide Leu271-Ala277 domain 3 in the heavy chain of high molecular weight kininogen. J Biol Chem. 1996;271: 11228-11234.
    • (1996) J Biol Chem. , vol.271 , pp. 11228-11234
    • Kunapuli, S.P.1    Bradford, H.N.2    Jameson, B.A.3    DeLa Cadena, R.A.4    Rick, L.5    Wassell, R.P.6    Colman, R.W.7
  • 6
    • 0029949824 scopus 로고    scopus 로고
    • Neutrophil adhesion on surfaces preadsorbed with high molecular weight kininogen under well-defined flow conditions
    • Yung LL, Lim F, Khan MMH, Kunapuli SP, Rick L, Colman RW, Cooper SL. Neutrophil adhesion on surfaces preadsorbed with high molecular weight kininogen under well-defined flow conditions. Immunopharmacology. 1996;32:19-23.
    • (1996) Immunopharmacology , vol.32 , pp. 19-23
    • Yung, L.L.1    Lim, F.2    Khan, M.M.H.3    Kunapuli, S.P.4    Rick, L.5    Colman, R.W.6    Cooper, S.L.7
  • 7
    • 0030803026 scopus 로고    scopus 로고
    • High molecular weight kininogen peptides inhibit the formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation
    • Lin Y, Harris RB, Yan W, McCrae KR, Zhang H, Colman RW. High molecular weight kininogen peptides inhibit the formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation. Blood. 1997;90:690-697.
    • (1997) Blood , vol.90 , pp. 690-697
    • Lin, Y.1    Harris, R.B.2    Yan, W.3    McCrae, K.R.4    Zhang, H.5    Colman, R.W.6
  • 8
    • 0024333375 scopus 로고
    • Thrombin-induced platelet aggregation involves an indirect proteolytic cleavage of aggregin by calpain
    • Puri RN, Zhou FX, Bradford H, Hu CJ, Colman RF, Colman RW. Thrombin-induced platelet aggregation involves an indirect proteolytic cleavage of aggregin by calpain. Arch Biochem Biophys. 1989;271: 346-358.
    • (1989) Arch Biochem Biophys. , vol.271 , pp. 346-358
    • Puri, R.N.1    Zhou, F.X.2    Bradford, H.3    Hu, C.J.4    Colman, R.F.5    Colman, R.W.6
  • 9
    • 0026090569 scopus 로고
    • High molecular weight kininogen inhibits thrombin-induced platelet aggregation and cleavage of aggregin by inhibiting binding of thrombin to platelets
    • Puri RN, Zhou F, Hu CJ, Colman RF, Colman RW. High molecular weight kininogen inhibits thrombin-induced platelet aggregation and cleavage of aggregin by inhibiting binding of thrombin to platelets. Blood. 1991;77:500-507.
    • (1991) Blood , vol.77 , pp. 500-507
    • Puri, R.N.1    Zhou, F.2    Hu, C.J.3    Colman, R.F.4    Colman, R.W.5
  • 12
    • 0027182033 scopus 로고
    • A point mutation of alanine 163 to threonine is responsible for the defective secretion of high molecular weight kininogen by the liver of brown Norway Katholiek rats
    • Hayashi I, Hoshiko S, Makabe O, Oh-ishi S. A point mutation of alanine 163 to threonine is responsible for the defective secretion of high molecular weight kininogen by the liver of brown Norway Katholiek rats. J Biol Chem. 1993;268:17219-17224.
    • (1993) J Biol Chem. , vol.268 , pp. 17219-17224
    • Hayashi, I.1    Hoshiko, S.2    Makabe, O.3    Oh-Ishi, S.4
  • 13
    • 0022870220 scopus 로고
    • Determination of antithrombin III (AT-III) using the coatest antithrombin kit and a microplate system
    • Scott CF. Determination of antithrombin III (AT-III) using the Coatest Antithrombin Kit and a microplate system. Ann N Y Acad Sci. 1986;485: 443-444.
    • (1986) Ann N Y Acad Sci. , vol.485 , pp. 443-444
    • Scott, C.F.1
  • 14
    • 33745551242 scopus 로고
    • Gerinnungsphysiologische schnellmethode zur bestimung des fibrinogens
    • Clauss A. Gerinnungsphysiologische Schnellmethode zur Bestimung des Fibrinogens. Acta Hematol. 1957;17:237-246.
    • (1957) Acta Hematol. , vol.17 , pp. 237-246
    • Clauss, A.1
  • 15
    • 0009716652 scopus 로고
    • The assay and properties of labile factor (factor V)
    • Quick RJ. The assay and properties of labile factor (factor V). J Clin Pathol. (London) 1960;13:457.
    • (1960) J Clin Pathol. (London) , vol.13 , pp. 457
    • Quick, R.J.1
  • 16
    • 72949143661 scopus 로고
    • The partial thromboplastin time with kaolin: A simple screening test for first stage plasma clotting factor deficiencies
    • Proctor RR, Rapaport SI. The partial thromboplastin time with kaolin: a simple screening test for first stage plasma clotting factor deficiencies. Am J Clin Pathol. 1961;36:212-219.
    • (1961) Am J Clin Pathol. , vol.36 , pp. 212-219
    • Proctor, R.R.1    Rapaport, S.I.2
  • 17
    • 0014708242 scopus 로고
    • Measurement of fibrinogen and fibrin degradation products in serum by staphylococcal clumping test
    • Hawiger J, Niewiarowski S, Gurewich V, Thomas DP. Measurement of fibrinogen and fibrin degradation products in serum by staphylococcal clumping test. J Lab Clin Med. 1970;75:93-108.
    • (1970) J Lab Clin Med. , vol.75 , pp. 93-108
    • Hawiger, J.1    Niewiarowski, S.2    Gurewich, V.3    Thomas, D.P.4
  • 18
    • 0029875007 scopus 로고    scopus 로고
    • Failure of thrombin inhibition to prevent intracoronary thrombosis in the dog
    • Belcher PR, Drake-Holland AJ, Hynd JW, Noble MI. Failure of thrombin inhibition to prevent intracoronary thrombosis in the dog. Clin Sci. 1996; 90:363-368.
    • (1996) Clin Sci. , vol.90 , pp. 363-368
    • Belcher, P.R.1    Drake-Holland, A.J.2    Hynd, J.W.3    Noble, M.I.4
  • 19
    • 0028873121 scopus 로고
    • Dose-related cardioprotection by ifetroban in relation to inhibition of thrombosis and ex vivo platelet function
    • Gomoll AW, Schumacher WA, Ogletree ML. Dose-related cardioprotection by ifetroban in relation to inhibition of thrombosis and ex vivo platelet function. Pharmacology. 1995;50:92-110.
    • (1995) Pharmacology , vol.50 , pp. 92-110
    • Gomoll, A.W.1    Schumacher, W.A.2    Ogletree, M.L.3
  • 21
    • 0025122795 scopus 로고
    • Kinetics of inhibition of platelet calpain II by human kininogens
    • Bradford HN, Schmaier AH, Colman RW. Kinetics of inhibition of platelet calpain II by human kininogens. Biochem J. 1990;270:83-90.
    • (1990) Biochem J. , vol.270 , pp. 83-90
    • Bradford, H.N.1    Schmaier, A.H.2    Colman, R.W.3
  • 24
    • 0024325179 scopus 로고
    • Modulation of thrombin-induced platelet aggregation by inhibition of calpain by a synthetic peptide derived from the thiol-protease inhibitory sequence of kininogens and S-(3-nitro-2-pyridinesulfenyl)-cysteine
    • Puri RN, Matsueda R, Umeyama H, Bradford HN, Colman RW. Modulation of thrombin-induced platelet aggregation by inhibition of calpain by a synthetic peptide derived from the thiol-protease inhibitory sequence of kininogens and S-(3-nitro-2-pyridinesulfenyl)-cysteine. Biochem Biophys Res Commun. 1989;162:1017-1024.
    • (1989) Biochem Biophys Res Commun. , vol.162 , pp. 1017-1024
    • Puri, R.N.1    Matsueda, R.2    Umeyama, H.3    Bradford, H.N.4    Colman, R.W.5
  • 25
    • 0030823246 scopus 로고    scopus 로고
    • Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2+3 of the urokinase receptor
    • Colman RW, Pixley RA, Najamunnisa S, Yan W, Wang J, Mazar A, McCrae KR. Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2+3 of the urokinase receptor. J Clin Invest. 1997;100:1481-1487.
    • (1997) J Clin Invest. , vol.100 , pp. 1481-1487
    • Colman, R.W.1    Pixley, R.A.2    Najamunnisa, S.3    Yan, W.4    Wang, J.5    Mazar, A.6    McCrae, K.R.7
  • 26
    • 0017149563 scopus 로고
    • Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma
    • Mandle R Jr, Colman RW, Kaplan AP. Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma. Proc Natl Acad Sci U S A. 1976;73:4179-4183.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 4179-4183
    • Mandle R., Jr.1    Colman, R.W.2    Kaplan, A.P.3
  • 27
    • 0029028074 scopus 로고
    • Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture
    • 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.
    • (1995) Thromb Haemost. , vol.74 , pp. 698-703
    • Lenich, C.1    Pannell, R.2    Gurewich, V.3
  • 28
    • 0021930258 scopus 로고
    • Tissue plasminogen activator release in vivo in response to vasoactive agents
    • Smith D, Gilbert M, Owen WG. Tissue plasminogen activator release in vivo in response to vasoactive agents. Blood. 1983;66:835-839.
    • (1983) Blood , vol.66 , pp. 835-839
    • Smith, D.1    Gilbert, M.2    Owen, W.G.3
  • 29
    • 0022535288 scopus 로고
    • Studies of the digestion of bradykinin. Lys-bradykinin, and des-Arg9-bradykinin by angiotensin converting enzyme
    • Sheikh IA, Kaplan AP. Studies of the digestion of bradykinin. Lys-bradykinin, and des-Arg9-bradykinin by angiotensin converting enzyme. Biochem Pharmacol. 1986;35:1951-1956.
    • (1986) Biochem Pharmacol. , vol.35 , pp. 1951-1956
    • Sheikh, I.A.1    Kaplan, A.P.2
  • 30
    • 0029814343 scopus 로고    scopus 로고
    • Bradykinin and its metabolite, Arg-Pro-Pro-Gly-Phe, are selective inhibitors of a-thrombin-induced platelet activation
    • Hasan AAK, Amenta S, Schmaier AH. Bradykinin and its metabolite, Arg-Pro-Pro-Gly-Phe, are selective inhibitors of a-thrombin-induced platelet activation. Circulation. 1996;94:517-528.
    • (1996) Circulation , vol.94 , pp. 517-528
    • Hasan, A.A.K.1    Amenta, S.2    Schmaier, A.H.3
  • 32
    • 0001610584 scopus 로고    scopus 로고
    • Evidence that the zinc-dependent platelet binding protein of factor XII and high molecular weight kininogen is glycoprotein Ib
    • Abstract
    • Joseph K, Bahou W, Kaplan AP. Evidence that the zinc-dependent platelet binding protein of factor XII and high molecular weight kininogen is glycoprotein Ib. J Invest Med. 1997;45:267A. Abstract.
    • (1997) J Invest Med. , vol.45
    • Joseph, K.1    Bahou, W.2    Kaplan, A.P.3
  • 33
    • 0020565895 scopus 로고
    • 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
    • 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. Medicine (Baltimore). 1983;62:248-255.
    • (1983) Medicine (Baltimore) , vol.62 , pp. 248-255
    • Goodnough, L.T.1    Saito, H.2    Ratnoff, O.D.3
  • 34
    • 0003371207 scopus 로고
    • Factor XII activity and antigen concentrations in patients suffering from recurrent thrombosis
    • Mannhalter C, Fisher M, Hopmeier P, Deutch E. Factor XII activity and antigen concentrations in patients suffering from recurrent thrombosis. Fibrinolysis. 1987;1:259-263.
    • (1987) Fibrinolysis , vol.1 , pp. 259-263
    • Mannhalter, C.1    Fisher, M.2    Hopmeier, P.3    Deutch, E.4
  • 35
    • 0026065260 scopus 로고
    • Thromboembolism and bleeding tendency in congenital factor XII deficiency: A study on 74 subjects from 14 Swiss families
    • Lammle B, Wuillemin WA, Huber I, Krauskopf M, Zurcher C, Pflugshaupt R, Furlan M. Thromboembolism and bleeding tendency in congenital factor XII deficiency: a study on 74 subjects from 14 Swiss families. Thromb Haemost. 1991;65:117-121.
    • (1991) Thromb Haemost. , vol.65 , pp. 117-121
    • Lammle, B.1    Wuillemin, W.A.2    Huber, I.3    Krauskopf, M.4    Zurcher, C.5    Pflugshaupt, R.6    Furlan, M.7
  • 36
    • 0026803207 scopus 로고
    • The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism
    • Halbmayer WM, Mannhalter C, Feichtinger C, Rubi K, Fischer M. The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism. Thromb Haemost. 1992;68:285-290.
    • (1992) Thromb Haemost. , vol.68 , pp. 285-290
    • Halbmayer, W.M.1    Mannhalter, C.2    Feichtinger, C.3    Rubi, K.4    Fischer, M.5
  • 37
    • 0026458603 scopus 로고
    • Factor XII clotting activity and antigen levels in patients with thromboembolic disease
    • von Kanel R, Wuillemin WA, Furlan M, Lammle B. Factor XII clotting activity and antigen levels in patients with thromboembolic disease. Blood Coagul Fibrinolysis, 1992;3:555-561.
    • (1992) Blood Coagul Fibrinolysis , vol.3 , pp. 555-561
    • Von Kanel, R.1    Wuillemin, W.A.2    Furlan, M.3    Lammle, B.4
  • 38
    • 0027057953 scopus 로고
    • Evidence for a role of factor XII-dependent fibrinolysis in cardiovascular diseases
    • Jespersen J, Munkvad S, Pedersen OD, Gram J, Kluft C. Evidence for a role of factor XII-dependent fibrinolysis in cardiovascular diseases. Ann N Y Acad Sci. 1992;667:454-456.
    • (1992) Ann N Y Acad Sci. , vol.667 , pp. 454-456
    • Jespersen, J.1    Munkvad, S.2    Pedersen, O.D.3    Gram, J.4    Kluft, C.5
  • 39
    • 44949281924 scopus 로고
    • 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
    • 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.
    • (1991) J Am Coll Cardiol. , vol.17 , pp. 957-962
    • Munkvad, S.1    Jespersen, J.2    Gram, J.3    Kluft, C.4
  • 40
    • 0030913006 scopus 로고    scopus 로고
    • The etiology, diagnosis and treatment of thrombocic disorders in newborn infants: A call for international and multi-institutional studies
    • Schmidt B. The etiology, diagnosis and treatment of thrombocic disorders in newborn infants: a call for international and multi-institutional studies. Semin Perinatol. 1997;21:86-89.
    • (1997) Semin Perinatol. , vol.21 , pp. 86-89
    • Schmidt, B.1
  • 41
    • 0028862304 scopus 로고
    • Neonatal thrombosis: Are we doing the right studies?
    • Roy M, Schmidt B. Neonatal thrombosis: are we doing the right studies? Semin Thromb Hemost. 1995;21:313-316.
    • (1995) Semin Thromb Hemost. , vol.21 , pp. 313-316
    • Roy, M.1    Schmidt, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.