메뉴 건너뛰기




Volumn 80, Issue 1, 1998, Pages 74-81

Factor XII does not initiate prekallikrein activation on endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 12; BOVINE SERUM ALBUMIN; BUFFER; CHROMOGENIC SUBSTRATE; GELATIN; PREKALLIKREIN; SOYBEAN TRYPSIN INHIBITOR; ZINC ION;

EID: 0031878996     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1615142     Document Type: Article
Times cited : (88)

References (40)
  • 1
    • 0018632212 scopus 로고
    • The autoactivation of rabbit Hageman factor
    • Wiggins RC, Cochrane CG. The autoactivation of rabbit Hageman factor. J Exp Med 1979; 150: 1122-33.
    • (1979) J Exp Med , vol.150 , pp. 1122-1133
    • Wiggins, R.C.1    Cochrane, C.G.2
  • 3
    • 0019197848 scopus 로고
    • Autoactivation of human Hageman factor: Demonstration utilizing a synthetic substrate
    • Silverberg M, Dunn JT, Garen L, Kaplan AP. Autoactivation of human Hageman factor: demonstration utilizing a synthetic substrate. J Biol Chem 1980; 255: 7281-6.
    • (1980) J Biol Chem , vol.255 , pp. 7281-7286
    • Silverberg, M.1    Dunn, J.T.2    Garen, L.3    Kaplan, A.P.4
  • 4
    • 0023684099 scopus 로고
    • Structural changes of plasma high molecular weight kininogen after in vitro activation and in sepsis
    • Schmaier AH, Farber A, Schein R, Sprung C. Structural changes of plasma high molecular weight kininogen after in vitro activation and in sepsis. J Lab Clin Med 1988; 112: 182-92.
    • (1988) J Lab Clin Med , vol.112 , pp. 182-192
    • Schmaier, A.H.1    Farber, A.2    Schein, R.3    Sprung, C.4
  • 5
    • 0002172917 scopus 로고
    • The contact activation system of plasma: Biochemistry and pathophysiology
    • Gallin JI, Goldstein IM, Snyderman R, eds. New York: Raven Press, Ltd.
    • Kozin F, Cochrane CG. The contact activation system of plasma: Biochemistry and pathophysiology. In: Inflammation: Basic principles and clinical correlates. Gallin JI, Goldstein IM, Snyderman R, eds. New York: Raven Press, Ltd. 1988; pp 101-120.
    • (1988) Inflammation: Basic Principles and Clinical Correlates , pp. 101-120
    • Kozin, F.1    Cochrane, C.G.2
  • 6
    • 0027419518 scopus 로고
    • Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis
    • Gurewich V, Johnstone M, Loza J-P, 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: 317-21.
    • (1993) FEBS Lett , vol.318 , pp. 317-321
    • Gurewich, V.1    Johnstone, M.2    Loza, J.-P.3    Pannell, R.4
  • 7
    • 0028211344 scopus 로고
    • Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: A mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis
    • Loza J-P, 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: 347-52.
    • (1994) Thromb Haemost , vol.71 , pp. 347-352
    • Loza, J.-P.1    Gurewich, V.2    Johnstone, M.3    Pannell, R.4
  • 8
    • 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
  • 9
    • 2142725714 scopus 로고
    • Accelerating effect of zinc ions on the surface-mediated activation of factor XII and prekallikrein
    • Tokyo
    • Shimada T, Kato H, Iwanaga S. Accelerating effect of zinc ions on the surface-mediated activation of factor XII and prekallikrein. J Biochem (Tokyo) 1987; 102: 913-21.
    • (1987) J Biochem , vol.102 , pp. 913-921
    • Shimada, T.1    Kato, H.2    Iwanaga, S.3
  • 10
    • 0023255733 scopus 로고
    • Acceleration of surface dependent autocatalytic activation of blood coagulation factor XII by divalent metal ions
    • Shore JD, Day DE, Bock PE, Olson ST. Acceleration of surface dependent autocatalytic activation of blood coagulation factor XII by divalent metal ions. Biochemistry 1987; 26: 2250-8.
    • (1987) Biochemistry , vol.26 , pp. 2250-2258
    • Shore, J.D.1    Day, D.E.2    Bock, P.E.3    Olson, S.T.4
  • 11
    • 0024990508 scopus 로고
    • The inositol-phospholipid-accelerated activation of prekallikrein by activated factor XII at physiological ionic strength requires zinc ions and high-Mr kininogen
    • Schousboe I. The inositol-phospholipid-accelerated activation of prekallikrein by activated factor XII at physiological ionic strength requires zinc ions and high-Mr kininogen. Eur J Biochem 1990; 193: 495-9.
    • (1990) Eur J Biochem , vol.193 , pp. 495-499
    • Schousboe, I.1
  • 12
    • 0031027294 scopus 로고    scopus 로고
    • The surface dependent autoactivation mechanism of factor XII
    • Røjkjær R, Schousboe I. The surface dependent autoactivation mechanism of factor XII. Eur J Biochem 1997; 243: 160-6.
    • (1997) Eur J Biochem , vol.243 , pp. 160-166
    • Røjkjær, R.1    Schousboe, I.2
  • 13
    • 0027233729 scopus 로고
    • Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement
    • Bernardo MM, Day DE, Olson ST, Shore JD. Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement. J Biol Chem 1993; 268: 12468-76.
    • (1993) J Biol Chem , vol.268 , pp. 12468-12476
    • Bernardo, M.M.1    Day, D.E.2    Olson, S.T.3    Shore, J.D.4
  • 14
    • 0027281416 scopus 로고
    • Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies
    • Bernardo MM, Day DE, Halvorson HR, Olson ST, Shore JD. Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies. J Biol Chem 1993; 268: 12477-83.
    • (1993) J Biol Chem , vol.268 , pp. 12477-12483
    • Bernardo, M.M.1    Day, D.E.2    Halvorson, H.R.3    Olson, S.T.4    Shore, J.D.5
  • 15
    • 0030788208 scopus 로고    scopus 로고
    • 2+-binding sites in factor XII and its derivatives
    • 2+-binding sites in factor XII and its derivatives. Eur J Biochem 1997; 247: 491-6.
    • (1997) Eur J Biochem , vol.247 , pp. 491-496
    • Røjkjær, R.1    Schousboe, I.2
  • 16
    • 0023797442 scopus 로고
    • Expression of high molecular weight kininogen on human umbilical vein endothelial cells
    • Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB. Expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 1988; 263: 16327-33.
    • (1988) J Biol Chem , vol.263 , pp. 16327-16333
    • Schmaier, A.H.1    Kuo, A.2    Lundberg, D.3    Murray, S.4    Cines, D.B.5
  • 17
    • 0025834590 scopus 로고
    • Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation
    • Meloni FJ, Schmaier AH. Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation. J Biol Chem 1991; 266: 6786-94.
    • (1991) J Biol Chem , vol.266 , pp. 6786-6794
    • Meloni, F.J.1    Schmaier, A.H.2
  • 19
    • 0027212538 scopus 로고
    • Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells
    • Reddigari SR, Shibayama T, Brunnee T, Kaplan AP. Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells. J Biol Chem 1993; 268: 11982-7.
    • (1993) J Biol Chem , vol.268 , pp. 11982-11987
    • Reddigari, S.R.1    Shibayama, T.2    Brunnee, T.3    Kaplan, A.P.4
  • 20
    • 0031973492 scopus 로고    scopus 로고
    • High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation
    • Motta G, Røjkjær R, Hasan AAK, Cines DB, Schmaier AH. High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation . Blood 1998; 91: 516-28.
    • (1998) Blood , vol.91 , pp. 516-528
    • Motta, G.1    Røjkjær, R.2    Hasan, A.A.K.3    Cines, D.B.4    Schmaier, A.H.5
  • 21
    • 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: 690-7.
    • (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
  • 22
    • 0020055028 scopus 로고
    • Assay of plasma prekallikrein: Comparison of amidolytic, esterolytic, coagulation and immunochemical assays
    • Fisher CA, Schmaier AH, Addonizio VP, Colman RW. Assay of plasma prekallikrein: comparison of amidolytic, esterolytic, coagulation and immunochemical assays. Blood 1982; 59: 963-70.
    • (1982) Blood , vol.59 , pp. 963-970
    • Fisher, C.A.1    Schmaier, A.H.2    Addonizio, V.P.3    Colman, R.W.4
  • 24
    • 0027418773 scopus 로고
    • Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties
    • Kaufman J, Haaseman M, Modrow S, Muller-Esterl W. Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties. J Biol Chem 1993; 268: 9079-91.
    • (1993) J Biol Chem , vol.268 , pp. 9079-9091
    • Kaufman, J.1    Haaseman, M.2    Modrow, S.3    Muller-Esterl, W.4
  • 26
    • 0021610573 scopus 로고
    • Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocellulose
    • Johnson DA, Gautsch JW, Sportsman JR, Elder JH. Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocellulose. Gene Anal Tech 1984; 1: 3-8.
    • (1984) Gene Anal Tech , vol.1 , pp. 3-8
    • Johnson, D.A.1    Gautsch, J.W.2    Sportsman, J.R.3    Elder, J.H.4
  • 27
    • 0027093242 scopus 로고
    • Direct determination of zinc in serum by zeeman atomic absorption spectrometry with a graphite furnace
    • D'Haese PC, Lamberts LV, Vanheule AO, De Broe ME. Direct determination of zinc in serum by zeeman atomic absorption spectrometry with a graphite furnace. Clin Chem 1992; 38: 2439-43.
    • (1992) Clin Chem , vol.38 , pp. 2439-2443
    • D'Haese, P.C.1    Lamberts, L.V.2    Vanheule, A.O.3    De Broe, M.E.4
  • 28
    • 0014847438 scopus 로고
    • Binding of zinc to amino acids and serum proteins in vitro
    • Prasad AS, Oberleas D. Binding of zinc to amino acids and serum proteins in vitro. J Lab Clin Med 1970; 36: 416-25.
    • (1970) J Lab Clin Med , vol.36 , pp. 416-425
    • Prasad, A.S.1    Oberleas, D.2
  • 30
    • 0027459092 scopus 로고
    • Endothelial cells produce a substance that inhibits contact activation of coagulation by blocking the activation of Hageman factor
    • Kleniewski J, Donaldson, VH. Endothelial cells produce a substance that inhibits contact activation of coagulation by blocking the activation of Hageman factor. Proc Natl Acad Sci 1993; 90: 198-202.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 198-202
    • Kleniewski, J.1    Donaldson, V.H.2
  • 31
    • 0023583161 scopus 로고
    • Inhibition of the activation of Hageman factor (factor XII) by peripheral blood cells
    • Ratnoff OD, Emanuelson MM, Ziats NP. Inhibition of the activation of Hageman factor (factor XII) by peripheral blood cells. J Clin Invest 1987; 80: 1180-9
    • (1987) J Clin Invest , vol.80 , pp. 1180-1189
    • Ratnoff, O.D.1    Emanuelson, M.M.2    Ziats, N.P.3
  • 32
    • 0027399846 scopus 로고
    • Inhibition of the activation of hageman factor (Factor XII) by eosinophils and eosinophilic constituents
    • Ratnoff OD, Gleich GJ, Shurin SB, Kazura J, Everson B, Embury P. Inhibition of the activation of hageman factor (Factor XII) by eosinophils and eosinophilic constituents. Am L Hematol1993; 42: 138-45.
    • (1993) Am L Hematol , vol.42 , pp. 138-145
    • Ratnoff, O.D.1    Gleich, G.J.2    Shurin, S.B.3    Kazura, J.4    Everson, B.5    Embury, P.6
  • 34
    • 0020035474 scopus 로고
    • Zinc in plasma, neutrophils, lymphocytes and erythrocytes as determined by flameless atomic absorbtion spectrophotometry
    • Whitehouse RC, Prasad AS, Rabbani PI, Cossack ZT. Zinc in plasma, neutrophils, lymphocytes and erythrocytes as determined by flameless atomic absorbtion spectrophotometry. Clin Chem 1982; 28: 475-80.
    • (1982) Clin Chem , vol.28 , pp. 475-480
    • Whitehouse, R.C.1    Prasad, A.S.2    Rabbani, P.I.3    Cossack, Z.T.4
  • 35
    • 0020593779 scopus 로고
    • Determination of ultrafiltrable zinc in plasma by flameless atomic absorption spectrophotometry
    • Whitehouse RC, Prasad AS, Cossack ZT. Determination of ultrafiltrable zinc in plasma by flameless atomic absorption spectrophotometry. Clin Chem 1983; 29: 1971-7.
    • (1983) Clin Chem , vol.29 , pp. 1971-1977
    • Whitehouse, R.C.1    Prasad, A.S.2    Cossack, Z.T.3
  • 36
    • 0025615418 scopus 로고
    • Zinc mediation of the binding of human growth hormone to the human prolactin receptor
    • Cunningham BC, Bass S, Fuh G, Wells JA. Zinc mediation of the binding of human growth hormone to the human prolactin receptor. Science 1990; 250: 1709-12.
    • (1990) Science , vol.250 , pp. 1709-1712
    • Cunningham, B.C.1    Bass, S.2    Fuh, G.3    Wells, J.A.4
  • 38
    • 0018150855 scopus 로고
    • Platelet metal levels in normal subjects determined by atomic absorption spectrophotometry
    • Baker RJ, McNeil JJ, Lander H. Platelet metal levels in normal subjects determined by atomic absorption spectrophotometry. Thromb Haemost 1978; 39: 360-5.
    • (1978) Thromb Haemost , vol.39 , pp. 360-365
    • Baker, R.J.1    McNeil, J.J.2    Lander, H.3
  • 39
    • 0018749573 scopus 로고
    • Elemental composition of platelets. Part II: Water content of normal human platelets and measurements of their concentration of Cu, Fe, K, and Zn by neutron activation analysis
    • Kiem J, Borberg H, Iyengar GV, Kasperek K, Siegers M, Feinendegen LE, Gross R. Elemental composition of platelets. Part II: Water content of normal human platelets and measurements of their concentration of Cu, Fe, K, and Zn by neutron activation analysis. Clin Chem 1979; 25: 705-10.
    • (1979) Clin Chem , vol.25 , pp. 705-710
    • Kiem, J.1    Borberg, H.2    Iyengar, G.V.3    Kasperek, K.4    Siegers, M.5    Feinendegen, L.E.6    Gross, R.7
  • 40
    • 2642699455 scopus 로고
    • Normal human platelet zinc content and its release
    • Ulutin ON, ed. Amsterdam, Excerpta Medica
    • Aktulga A, Ulutin ON. Normal human platelet zinc content and its release. In: Monograph: Platelets. Ulutin ON, ed. Amsterdam, Excerpta Medica; 1975.
    • (1975) Monograph: Platelets
    • Aktulga, A.1    Ulutin, O.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.