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A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system BJMBR
Yarzábal,A.; Avilán,L.; Hoelzl,K.; Muñoz,M. de; Puig,J.; Kansau,I..
The interaction of plasminogen, tissue plasminogen activator (t-PA) and urokinase with a clinical strain of Helicobacter pylori was studied. Plasminogen bound to the surface of H. pylori cells in a concentration-dependent manner and could be activated to the enzymatic form, plasmin, by t-PA. Affinity chromatography assays revealed a plasminogen-binding protein of 58.9 kDa in water extracts of surface proteins. Surface-associated plasmin activity, detected with the chromogenic substrate CBS 00.65, was observed only when plasminogen and an exogenous activator were added to the cell suspension. The two physiologic plasminogen activators, t-PA and urokinase, were also shown to bind to and remain active on the surface of bacterial cells. epsilon-Aminocaproic...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Helicobacter pylori; Plasminogen; T-PA; Urokinase; Plasminogen activation.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000900004
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Analysis of five streptokinase formulations using the euglobulin lysis test and the plasminogen activation assay BJMBR
Couto,L.T.; Donato,J.L.; Nucci,G. de.
Streptokinase, a 47-kDa protein isolated and secreted by most group A, C and G ß-hemolytic streptococci, interacts with and activates human protein plasminogen to form an active complex capable of converting other plasminogen molecules to plasmin. Our objective was to compare five streptokinase formulations commercially available in Brazil in terms of their activity in the in vitro tests of euglobulin clot formation and of the hydrolysis of the plasmin-specific substrate S-2251™. Euglobulin lysis time was determined using a 96-well microtiter plate. Initially, human thrombin (10 IU/ml) and streptokinase were placed in individual wells, clot formation was initiated by the addition of plasma euglobulin, and turbidity was measured at 340 nm every 30 s. In the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Streptokinase; Plasminogen; Plasmin; Substrate S-2251™.
Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004001200015
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Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors BJMBR
Gozzo,A.J.; Nunes,V.A.; Nader,H.B.; Dietrich,C.P.; Carmona,A.K.; Sampaio,M.U.; Sampaio,C.A.M.; Araújo,M.S..
Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glycosaminoglycans; Human plasma kallikrein; Plasminogen; Factor XII; C1-inhibitor; Antithrombin.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000800011
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Structural basis for the pathophysiology of lipoprotein(a) in the athero-thrombotic process BJMBR
Anglés-Cano,E..
Lipoprotein Lp(a) is a major and independent genetic risk factor for atherosclerosis and cardiovascular disease. The essential difference between Lp(a) and low density lipoproteins (LDL) is apolipoprotein apo(a), a glycoprotein structurally similar to plasminogen, the precursor of plasmin, the fibrinolytic enzyme. This structural homology endows Lp(a) with the capacity to bind to fibrin and to membrane proteins of endothelial cells and monocytes, and thereby to inhibit plasminogen binding and plasmin generation. The inhibition of plasmin generation and the accumulation of Lp(a) on the surface of fibrin and cell membranes favor fibrin and cholesterol deposition at sites of vascular injury. Moreover, insufficient activation of TGF-ß due to low plasmin...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Atherosclerosis; Apolipoprotein(a); Thrombosis; Atheroma; Plasminogen; Lipoprotein; Fibrin; Fibrinolysis.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001100002
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TRANSFORMING GROWTH FACTOR BETA HAS DUAL EFFECTS ON MMP9 AND uPA EXPRESSION IN HTR-8/SVneo HUMAN TROPHOBLASTIC CELL LINE Acta biol.Colomb.
NOVOA HERRÁN,Sandra Susana; CASTELBLANCO,Mariela; SÁNCHEZ -GÓMEZ,Myriam; UMAÑA PÉREZ,Adriana.
ABSTRACT Invasion of trophoblast into endometrium is vital for successful pregnancy development. MMP9 and uPA are key proteases in this process, but it is still not clear the regulation of its expression by Transforming Growth Factor Beta (TGF-β), a known negative regulator of trophoblast invasion. We evaluated the effect of TGF-β on the transcriptional expression of uPA and MMP9 over time, in HTR-8/SVneo trophoblast cells cultured with or without 0.5 % fetal bovine serum, via RT qPCR. The involved transcription factors and signaling pathways were analyzed in silico, using Proscan, Enrich, PCViz and Wiki Pathway. Results showed that TGF-β temporarily regulates the expression of uPA and MMP9. Serum modified the nature of TGF-β's effects on uPA expression,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Computational biology; Matrix metalloproteinase; Placenta; Plasminogen; Polymerase chain reaction.
Ano: 2019 URL: http://www.scielo.org.co/scielo.php?script=sci_arttext&pid=S0120-548X2019000100026
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