The role of β2-glycoprotein I (β2GPI) in the activation of plasminogen
作者： Francisco López-Lira , Luis Rosales-León , Verónica Monroy Martínez , Blanca H. Ruiz Ordaz
DOI: 10.1016/J.BBAPAP.2005.12.020
关键词: Antibody 、 Antiphospholipid syndrome 、 Fibrin 、 Thrombomodulin 、 Cell biology 、 Glycoprotein 、 Fibrinolysis 、 Plasmin 、 Chemistry 、 Biochemistry 、 Function (biology) 、 Biophysics 、 Analytical chemistry 、 Molecular biology
摘要: Abstract β2-glycoprotein I (β 2 GPI) is a glycoprotein of unknown physiological function. It the main target antigen for antiphospholipid antibodies in patients with syndrome (APS). β GPI binds high affinity to atherogenic lipoprotein Lp(a) which shares structural homology plasminogen, key molecule fibrinolytic system. Impaired fibrinolysis has been described APS. The present work reports interaction between and Glu-Plasminogen may explain recently proteolytic effect plasmin on GPI. In process activation, we found an increase generation both at fibrin cellular surface level as function concentration added, suggesting important role cofactor trimolecular complex GPI-Plasminogen-tPA. This phenomenon represents novel regulatory step positive feedback mechanism extrinsic antithrombotic regulation. IgG anti-β recognized endothelial inducing its activation ICAM-I decrease expression thrombomodulin favoring pro-thrombotic state vascular endothelium. interference conversion by could generate thrombosis observed
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sci-hub.se 参考文章(33)
Charles S. COCKELL, Julian M. MARSHALL, Keith M. DAWSON, Stewart A. CEDERHOLM-WILLIAMS, Chris P. PONTING, Evidence that the conformation of unliganded human plasminogen is maintained via an intramolecular interaction between the lysine-binding site of kringle 5 and the N-terminal peptide Biochemical Journal. ,vol. 333, pp. 99- 105 ,(1998) , 10.1042/BJ3330099
Silvano Köchl, Friedrich Fresser, Eva Lobentanz, Gottfried Baier, Gerd Utermann, Novel Interaction of Apolipoprotein(a) With β-2 Glycoprotein I Mediated by the Kringle IV Domain Blood. ,vol. 90, pp. 1482- 1489 ,(1997) , 10.1182/BLOOD.V90.4.1482
David A. Kandiah, Andrej Sali, Yonghua Sheng, Edward J. Victoria, David M. Marquis, Stephen M. Coutts, Steven A. Krilis, Current Insights into the “Antiphospholipid” Syndrome: Clinical, Immunological, and Molecular Aspects Advances in Immunology. ,vol. 70, pp. 507- 563 ,(1998) , 10.1016/S0065-2776(08)60393-4
Erika Polz, Gerhard M. Kostner, The binding of β2
-glycoprotein-I to human serum lipoproteins FEBS Letters. ,vol. 102, pp. 183- 186 ,(1979) , 10.1016/0014-5793(79)80955-2
I Schousboe, beta 2-Glycoprotein I: a plasma inhibitor of the contact activation of the intrinsic blood coagulation pathway. Blood. ,vol. 66, pp. 1086- 1091 ,(1985) , 10.1182/BLOOD.V66.5.1086.1086
David A. Kandiah, Steven A. Krilis, Beta 2-glycoprotein I. Lupus. ,vol. 3, pp. 207- 212 ,(1994) , 10.1177/096120339400300401
MICHAEL NESHEIM, JOHN WALKER, WEI WANG, MICHAEL BOFFA, ANTON HORREVOETS, LASZLO BAJZAR, Modulation of fibrin cofactor activity in plasminogen activation. Annals of the New York Academy of Sciences. ,vol. 936, pp. 247- 260 ,(2006) , 10.1111/J.1749-6632.2001.TB03513.X
Keying Ma, Ronit Simantov, Jing-Chuan Zhang, Roy Silverstein, Katherine A. Hajjar, Keith R. McCrae, High Affinity Binding of β2-Glycoprotein I to Human Endothelial Cells Is Mediated by Annexin II Journal of Biological Chemistry. ,vol. 275, pp. 15541- 15548 ,(2000) , 10.1074/JBC.275.20.15541
A. T. BRUNGER, J. KURIYAN, M. KARPLUS, Crystallographic R Factor Refinement by Molecular Dynamics Science. ,vol. 235, pp. 458- 460 ,(1987) , 10.1126/SCIENCE.235.4787.458
Miri Blank, David Faden, Angela Tincani, Juri Kopolovic, Iris Goldberg, Boris Gilburd, Flavio Allegri, Genesid Balestrieri, Guido Valesini, Yehuda Shoenfeld, Immunization with Anticardiolipin Cofactor (Beta-2-Glycoprotein I) Induces Experimental Antiphospholipid Syndrome in Naive Mice Journal of Autoimmunity. ,vol. 7, pp. 441- 455 ,(1994) , 10.1006/JAUT.1994.1032