Tranexamic acid: a clinical review

2015 ◽  
Vol 47 (4) ◽  
pp. 339-350 ◽  
Author(s):  
William Chuk Kit Ng ◽  
Angela Jerath ◽  
Marcin Wasowicz
Keyword(s):  
Tranexamic Acid ◽  
Clinical Review

scholarly journals Tranexamic Acid in the Treatment of Hip Fractures: A Clinical Review

2019 ◽  
Author(s):  
Nathan M. Krebs ◽  
Michael J. VanWagner ◽  
Tiffany Marchewka ◽  
Usama Faraj ◽  
Christopher R. Vitale
Keyword(s):  
Tranexamic Acid ◽  
Clinical Review ◽  
Hip Fractures

Personal neglect: A comprehensive theoretical and anatomo–clinical review.

2018 ◽  
Vol 32 (3) ◽  
pp. 269-279 ◽  
Author(s):  
Giorgia Committeri ◽  
Claudia Piervincenzi ◽  
Luigi Pizzamiglio
Keyword(s):  
Clinical Review

Comparison of Tranexamic-Acid and Aprotinin regarding the outcome after cardiac surgery

2011 ◽  
Vol 59 (S 01) ◽  
Author(s):  
A Cetinkaya ◽  
A Van Linden ◽  
Z Szalay ◽  
A Afflerbach ◽  
J Blumenstein ◽  
...  
Keyword(s):  
Cardiac Surgery ◽  
Tranexamic Acid

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

Evaluation of the Fibrin Plate Method for Estimating Plasminogen Activators

1972 ◽  
Vol 28 (01) ◽  
pp. 075-088 ◽  
Author(s):  
N. A Marsh ◽  
C. L Arocha-Pinango
Keyword(s):  
Tranexamic Acid ◽  
Plasminogen Activators ◽  
Heated Plate ◽  
Plasminogen Activation ◽  
Response Curves ◽  
Plate Method ◽  
Single Plate ◽  
Effect Of Additives ◽  
Threefold Increase ◽  
Fibrin Plate

SummaryA study was carried out in order to evaluate the Astrup and Mullertz fibrin plate method for estimating plasminogen activators.Choice of a suitable fibrinogen substrate was found to be the most important factor in setting up a workable assay. Many preparations contained a large proportion of non-clottable protein and plates made from these fibrinogens were usually unreliable. In addition, plasminogen content varied appreciably between preparations so that sensitivity of the method required careful calibration with each new batch of fibrinogen.The effect of additives in the fibrin plate was considered and it was found that calcium chloride alone was sufficient to ensure a stabilised plate which could be stored at 4° C for some time. The addition of tranexamic acid (AMCHA) was found to be a slightly more convenient way of estimating direct proteolytic activity, compared with the traditional heated plate. However neither method distinguished completely between proteolysis and plasminogen activation.In order to improve the precision of the method, the use of an analysis of variance technique has been studied. This technique provides information on the dose-response curves of test and unknown substances, and in addition produces an approximately threefold increase in precision over single plate tests.

Tranexamic acid promotes matrix mineralization in osteoblasts and inhibits osteoclastogenesis in vitro.

2020 ◽  
Author(s):  
J Keller ◽  
J Appelt ◽  
K Tseneva ◽  
D Jahn ◽  
S Jiang ◽  
...  
Keyword(s):  
Tranexamic Acid ◽  
Matrix Mineralization
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