Results 161 to 170 of about 28,516 (205)

Mechanisms of plasminogen activation

Journal of Internal Medicine, 1994
The fibrinolytic system consists of an inactive proenzyme, plasminogen, that is converted by plasminogen activators to the active enzyme, plasmin, that degrades fibrin. Two immunologically distinct plasminogen activators have been identified: tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA).
H R, Lijnen, F, Bachmann, D, Collen, V, Ellis, H, Pannekoek, D C, Rijken, S, Thorsen   +6 more
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Zymographic Evaluation of Plasminogen Activators and Plasminogen Activator Inhibitors

2004
Publisher Summary The plasminogen activator/plasminogen activator inhibitor (PA/PAI) system is of considerable fundamental importance in elucidating the biochemical mechanisms of many physiological and patho-physiological processes. Although many techniques are available to assess the PA/PAI system, including ELISA and molecular assays, fibrin ...
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Plasminogen Activators and Angiogenesis

1996
The formation of capillaries from preexisting blood vessels (angiogenesis) occurs in a variety of normal and pathological conditions, including organ development, would healing and tumor growth. Angiogenesis requires a strict temporal modulation of opposing cell functions: cell proliferation and migration, and extracellular matrix (ECM) degradation in ...
P, Mignatti, D B, Rifkin
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Plasminogen activators: A comparison

Vascular Pharmacology, 2006
Thrombolytic drugs play a crucial role in the management of patients with acute myocardial infarction, pulmonary embolism, deep vein thrombosis, arterial thrombosis, acute thrombosis of retinal vessel, extensive coronary emboli, and peripheral vascular thromboembolism.
Dev B, Baruah, Rajendra N, Dash, M R, Chaudhari, S S, Kadam   +3 more
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Plasminogen activation and cancer

Thrombosis and Haemostasis, 2005
SummaryBreakdown of the extracellular matrix is crucial for cancer invasion and metastasis. It is accomplished by the concerted action of several proteases, including the serine protease plasmin and a number of matrix metalloproteases. The activity of each of these proteases is regulated by an array of activators, inhibitors and cellular receptors ...
Danø, Keld, Behrendt, N., Hoyer-Hansen, G., Johnsen, Morten, Lund, L. R., Ploug, Michael, Nielsen, John Rømer   +6 more
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Plasminogen activator and cancer

European Journal of Cancer and Clinical Oncology, 1984
Plasminogen activator is a protease which catalyses the conversion of the inactive plasminogen to the active plasmin. Most transformed cell lines and solid tumors produce elevated levels of plasminogen activator compared with nontransformed counterparts. This increased synthesis of plasminogen activator may play a role in tumorigenesis, cancer invasion
M J, Duffy, P, O'Grady
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Urokinase-type plasminogen activator

The International Journal of Biochemistry & Cell Biology, 2007
Urokinase-type plasminogen activator (uPA) is a serine protease involved in tissue remodeling and cell migration. At the gene level, the interplay between a complex enhancer, required for induced and basal transcription, and the minimal promoter finely tunes uPA expression.
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Tissue plasminogen activator

Neurology, 2007
Tissue-type plasminogen activator (tPA) is a serine protease that cleaves plasminogen into active plasmin. In plasma, the primary function of plasmin is the digestion of fibrin, and therefore, tPA is used as a thrombolytic agent for acute treatment of ischemic stroke.
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Tissue-Type Plasminogen Activator

Pathophysiology of Haemostasis and Thrombosis, 1986
Tissue-type plasminogen activator (t-PA) is a serine protease with a molecular weight of about 70,000. It activates plasminogen to plasmin by cleavage of the Arg 560-Val 561 peptide bond. Kinetic analysis showed that the activation obeys Michaelis-Menten kinetics and that the presence of fibrin strikingly enhances the activation rate.
H R, Lijnen, D, Collen
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Fibrin‐Mediated Plasminogen Activation

Annals of the New York Academy of Sciences, 2001
Abstract: Fibrin, but not fibrinogen, enhances the rate of activation of plasminogen by tissue type plasminogen activator (t‐PA). Studies with enzymatic and chemical fragments of fibrinogen showed that several sites in fibrinogen are involved in this rate enhancement; these are, Aα148–160 (located in CNBr fragment FCB‐2), and FCB‐5 (a CNBr fragment ...
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