A spectrophotometric solid-phase fibrin-tissue plasminogen activator activity assay (SOFIA-tPA) for high-fibrin-affinity tissue plasminogen activator

1986 ◽  
Vol 153 (2) ◽  
pp. 201-210 ◽  
Author(s):  
Eduardo Angles-Cano
1971 ◽  
Vol 25 (03) ◽  
pp. 469-480 ◽  
Author(s):  
B Åstedt ◽  
M Pandolfi

SummaryThe ontogenesis of tissue plasminogen activator in various tissues was studied in 10 embryos and 58 foetuses with a histochemical method.The first appearance of activator activity was seen in a 4-weeks old embryo. At 8-9 weeks it was seen in the eye, meninges, heart, lungs, kidney and vena cava. In the foetal heart high activity was found in the coronary vessels, which can be regarded as the vasa vasorum of the heart. In the lungs a moderate activity increased at 24 weeks of age, when vascularisation increases more rapidly. Intense activity was seen in the highly vascularized corneoscleral junction of the eye later involved in the drainage of aqueous humor.In the kidney the activity could be related to the vessels, while no activity was seen in the glomeruli, the collecting system or the pelvis. In the vessels the activator activity was fairly high. No activity was seen in any stage of development of the liver.The plasminogen activator activity may be of importance for maintaining the foetomaternal circulation and micro-circulation in rapidly growing foetal organs. In the embryo the enzyme pattern is dominated by protein synthetizing enzymes. During foetal development the enzyme pattern changes owing to supervention of enzymes necessary for the function of the various organs. Plasminogen activator belongs to this latter group. The appearance of plasminogen activator activity may therefore be regarded mainly as a sign of functional maturity of the foetal organs.


2004 ◽  
Vol 22 (1) ◽  
pp. 17-26 ◽  
Author(s):  
Denis Gingras ◽  
Dominique Labelle ◽  
Carine Nyalendo ◽  
Dominique Boivin ◽  
Michel Demeule ◽  
...  

1986 ◽  
Vol 42 (5) ◽  
pp. 717-718 ◽  
Author(s):  
E. Alexaki ◽  
N. Kokolis ◽  
Th. Ploumis ◽  
A. Smokovitis

1990 ◽  
Vol 64 (02) ◽  
pp. 260-266 ◽  
Author(s):  
Elizabeth E Branscomb ◽  
Marschall S Runge ◽  
Christopher E Savard ◽  
Keith M Adams ◽  
Gary R Matsueda ◽  
...  

SummaryBispecific monoclonal antibodies that bind simultaneously to human fibrin and tissue plasminogen activator (tPA) enhance the fibrinolytic potency of tPA. Two bispecific antibodies (F36.23 and F32.1) were generated by somatic cell fusion. Antibody F36.23 derives its tPA binding from monoclonal anti-tPA antibody TCL8 and its fibrin binding from monoclonal antifibrin antibody 59D8. After purification from cell supernatants and ascites by two steps of affinity chromatography, hybrid-hybridoma bispecific antibody F36.23 simultaneously bound tPA and fibrin in solution and in solid-phase assays. In an assay for the lysis of human fibrin monomer, F36.23 increased the fibrinolytic potency of tPA by 5 to 10 fold, regardless of whether the bispecific antibody had been combined with the tPA before or during the assay. Bispecific F36.23 F(ab′)2 also bound tPA and fibrin simultaneously, and the enhancement in fibrinolysis in the presence of F36.23 F(ab′)2 was identical to that in the presence of intact F36.23. The second bispecific antibody, F32.1, was produced by an alternative strategy that has a wider potential for applicaton in other systems. Hybridoma bispecific antibody F32.1 was derived from the fusion of immune splenocytes (in mice immunized with a synthetic oligopeptide representing the amino terminus of the α-chain of human fibrin) with the anti-tPA cell line TCL8. The properties of hybridoma bispecific antibody F32.1 and its F(ab′)2 were indistinguishable from those of hybrid-hybridoma bispecific antibody F36.23 in solid-phase binding assays and in assays of fibrinolysis. Bispecific antibodies produced by somatic cell fusion, particularly in the form of F(ab′)2, may have potential for use in clinical thrombolysis.


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