Results 221 to 230 of about 81,875 (260)
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Regulation of Tissue Plasminogen Activator Expression

Annual Review of Physiology, 1989
Widespread interest in the biology of the fibrinolytic system has developed with the recognition of the role of intravascular thrombosis in the pathogene­ sis of human disease. The therapeutic application of thrombolytic agents is a result of the rapid evolution of our understanding of the biochemistry and physiological importance of this system.
R D, Gerard, R S, Meidell
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Tissue Plasminogen Activator and the Corneal Endothelium

American Journal of Ophthalmology, 1989
• There is a potential risk of bacterial or fungal contamination of the initial preparation, which could then result in contamination of each of the individual doses. It is essential, therefore, that the tissue plasminogen activator be reconstituted under strict aseptic conditions in a sterile hood.
M L, McDermott   +3 more
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Tissue Plasminogen Activator Activity in Prostatic Cancer

European Urology, 1984
19 patients with carcinoma of the prostate and 6 controls with hyperplasia of the prostate, have been investigated to elucidate the relationship between tumor fibrinolytic activity, the degree of malignancy, tumor stage and metastatic spread. Significantly (p less than 0.001) higher tissue plasminogen activator activities were found in metastatic ...
A, Köller   +3 more
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Tissue Plasminogen Activator (t-PA)

Therapeutic Drug Monitoring, 1993
Tissue plasminogen activator (t-PA) developed from recombinant DNA technology is a highly effective thrombolytic agent. Its main clinical application is in the treatment of acute myocardial infarction (MI), with most beneficial results occurring in patients treated early after the onset of symptoms. When t-PA was compared with other thrombolytic agents,
J, Madhani, H, Movsowitz, M N, Kotler
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Ontogenesis of Tissue Plasminogen Activator in the Human

Thrombosis and Haemostasis, 1971
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
B, Astedt, M, Pandolfi
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Tissue plasminogen activators in breast cancer

Thrombosis Research, 1987
Increased levels of tissue fibrinolytic activity have been detected in some malignant tumours and they have been implicated in metastatic spread. We have investigated tissue plasminogen activator (tPA) and urokinase (UK) in 26 breast carcinomas and 13 benign breast biopsies.
G T, Layer   +6 more
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Plasminogen activators and inhibitors in peritoneal tissue

APMIS, 1997
Serosal trauma elicits an inflammatory response which leads to the deposition of fibrin at injured sites, the residuals of which appear to be essential in excessive tissue repair and formation of intraabdominal adhesions. Local plasminogen activity may modulate this early phase of tissue repair.
L, Holmdahl   +3 more
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Effectors of the activation of human [Glu1]plasminogen by human tissue plasminogen activator

Biochemistry, 1988
The activation of human [Glu1]plasminogen [( Glu1]Pg) by human recombinant (rec) two-chain tissue plasminogen activator (t-PA) is inhibited by Cl-, at physiological concentrations, and stimulated by epsilon-aminocaproic acid (EACA), as well as fibrin(ogen).
T, Urano   +3 more
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Plasminogen Activators, Tissue Degradation, and Cancer

1985
Publisher Summary This chapter discusses the role of plasminogen activators in various biological processes. In specific, it describes two types of plasminogen activators—namely, the urokinase-type plasminogen activator (u-PA) and the tissue-type plasminogen activator (t-PA), which are essentially different gene products.
K, Danø   +5 more
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Plasminogen and Tissue Plasminogen Activator Interact with Antithrombin III

Thrombosis Research, 2000
Human antithrombin III was demonstrated to bind plasminogen specifically in a time and concentration-dependent manner. The above binding was also confirmed using ligand western blot assays. The interaction of plasminogen was significantly (>90%) inhibited by lysine, indicating the involvement of kringles in binding antithrombin III.
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