Plasminogen activator in human uterine tissue—Relationship to location of sampling and time in ovarian cycle

1980 ◽  
Vol 24 (2) ◽  
pp. 170-178 ◽  
Author(s):  
S.T. Shaw ◽  
L.K. Macaulay ◽  
M.S. Tanaka ◽  
W.R. Hohman ◽  
D.L. Moyer ◽  
...  
1979 ◽  
Vol 41 (04) ◽  
pp. 718-733 ◽  
Author(s):  
Preben Kok

SummaryThree types of plasminogen activator could be distinguished in extracts from human uterine tissue. The activators differed in thermostability or in mode of inhibition by EACA.All the extracts contained stable as well as labile activators. The saline extracts were uniformly inhibited by increasing concentrations of EACA. Extracts made with 2 M ammonium thiocyanate were either uniformly inhibited by EACA or showed deflections indicating contamination with an activator, which was inhibited in a biphasic manner. It was possible to distinguish between: (1) An activator, abundantly present in the tissue, which was uniformly inhibited and stable. (2) Another uniformly inhibited activator, which was labile. (3) An activator, inhibited in a biphasic manner, similar to urokinase, which was present in varying amounts in uteri with the endometrium in the proliferative phase.Gel filtration of the uterine extracts showed two major activity peaks corresponding to particle sizes of 60,000 dalton and about 10,000 dalton.Antiserum to purified plasminogen activator, prepared from porcine ovaries, inhibited the activity of the human uterine extracts, but not the activities of human urokinase or urine. Urokinase antiserum in a concentration completely inhibiting human urine or urokinase, inhibited only 10% or less of the activities of human uterine extracts.


1983 ◽  
Vol 50 (02) ◽  
pp. 518-523 ◽  
Author(s):  
C Kluft ◽  
A F H Jie ◽  
R A Allen

SummaryFunctional assay of extrinsic (tissue-type) plasminogen activator (EPA) in plasma on fibrin plates was evaluated. Using specific quenching antibodies, we demonstrated the method to be specific for EPA under all conditions tested. Contributions of urokinases and intrinsic activators were excluded. The quantity of EPA in blood samples, as compared with purified uterine tissue activator, shows 1 blood activator unit (BAU) to be comparable to 0.93 ng.The median values for EPA activity for healthy volunteers were: baseline, 1.9 BAU/ml (n = 123); diurnal, 5.5 BAU/ml (n = 12); DDAVP administration, 11.7 BAU/ml (n = 39); exhaustive exercise, 25 BAU/ml (n = 24); venous occlusion (15 min), 35 BAU/ml (n = 61). A large inter-individual variation in EPA activity was found, while individual baseline values tended to be constant for periods of weeks.In vitro in blood EPA activity shows a disappearance of 50% in about 90 min at 37° C; EPA activity in euglobulin fractions is stable for ≤2 hr at 37° C.A rapid decrease in EPA activity occurs in vivo, as noted after extracorporal circulation and exercise stimulation (t½ decay, 2-5 min).


2014 ◽  
Vol 116 (2) ◽  
pp. 377-381 ◽  
Author(s):  
Michał Dzięcioł ◽  
Ewa Stańczyk ◽  
Agnieszka Noszczyk-Nowak ◽  
Katarzyna Michlik ◽  
Roland Kozdrowski ◽  
...  

1972 ◽  
Vol 27 (01) ◽  
pp. 077-087 ◽  
Author(s):  
P Kok ◽  
T Astrup

SummaryThe differentiation between plasminogen activators from tissue and urine by means of the patterns of inhibition produced by epsilon-aminocaproic acid (EACA) in fibrin plate assays was investigated. Different inhibition patterns reflected genuine differences between two types of activators. The method allows the differentiation between two types of activators in weakly fibrinolytic and impure activator solutions.A biphasic pattern of inhibition by EACA was observed with human urine as well as with the purified urokinase preparations. The degree of enhancement of fibrinolysis observed in the millimolar concentration range of EACA fluctuated with the fibrin substrate and was, in part, related to its plasminogen content. Increasing concentrations of EACA produced a uniformly increasing inhibition of preparations of tissue activator obtained in various degrees of purity from porcine ovary and heart. Plasmin was uniformly inhibited by EACA. Inhibition of plasmin required about 100 times higher concentrations of EACA than inhibition of tissue activator-induced fibrinolysis. EACA produced a slightly biphasic pattern of inhibition with plasminogen activator from human uterine tissue.


1979 ◽  
Vol 41 (03) ◽  
pp. 590-600 ◽  
Author(s):  
G Wijngaards

SummaryThe assay of plasminogen activator activities on fibrin plates was re-evaluated with special reference to fibrinolysis inhibitors present in samples and in fibrin plates. The nature, action and stability of inhibiting material were studied in tissues with considerable differences in activator and inhibitor contents! human lung, liver and placenta. Extracts were tested for inhibitory capacity against purified human uterine tissue plasminogen activator, urokinase and plasmin on fibrin plates prepared from different grades of fibrinogens and fibrin.The tissue extracts inhibited fibrinolysis on fibrin plates to varying degrees, dependent on the sample medium, the type of fibrin plate and the kind of plasminogen activator. The influence of inhibitors in the sample and in the fibrin plate was partly abolished by the presence of 2 M KSCN in the sample. The procedure for preparing the samples as described by Astrup and Albrechtsen did not completely eliminate the inhibitory action against the added plasminogen activators.Comparison of urokinase inhibition with tissue activator inhibition by the tissue extracts as to the degree of denaturation in the Astrup and Albrechtsen procedure showed that they have much in common. Nevertheless, some differences were found which indicated the possible existence of separate urokinase and tissue activator inhibitors or of different inhibition mechanisms for these plasminogen activators.


DNA ◽  
1987 ◽  
Vol 6 (5) ◽  
pp. 461-472 ◽  
Author(s):  
VERMURI B. REDDY ◽  
ANTHONY J. GARRAMONE ◽  
HALINA SASAK ◽  
CHA-MER WEI ◽  
PATRICIA WATKINS ◽  
...  

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