Relevant bibliographies by topics / Plasminogen activator inhibitor type I (PAI-1)

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Plasminogen activator inhibitor type I (PAI-1)'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Plasminogen activator inhibitor type I (PAI-1)"

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Rossignol, Patrick, Eduardo Anglès-Cano, and Henri Lijnen. "Plasminogen activator inhibitor-1 impairs plasminogen activationmediated vascular smooth muscle cell apoptosis." Thrombosis and Haemostasis 96, no. 11 (2006): 665–70. http://dx.doi.org/10.1160/th06-06-0321.

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SummaryThe role of plasminogen activator inhibitor-1 (PAI-1) in vascular smooth muscle cell (VSMC) apoptosis mediated by plasminogen activation was studied with the use of aorticVSMC derived from mice with deficiency of PAI-1 (PAI-1-/-), tissue-type (t-PA-/-) or urokinase-type (u-PA-/-) plasminogen activator or from wildtype (WT) mice with corresponding genetic background. Plasminogen incubated with confluentVSMC was activated ina concentration-dependent and saturable manner for all four cell types, with maximal activation rates that were comparable for WT,u-PA-/and t-PA-/cells,but about two-f
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Zeheb, Ron, Usha M. Rafferty, Miguel A. Rodriguez, Peter Andreasen, and Thomas D. Gelehrter. "Immunoaffinity Purification of HTC Rat Hepatoma Cell Plasminogen Activator-Inhibitor-1." Thrombosis and Haemostasis 58, no. 04 (1987): 1017–23. http://dx.doi.org/10.1055/s-0038-1646047.

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SummaryIncubation of HTC rat hepatoma cells with the synthetic glucocorticoid dexamethasone rapidly inhibits tissue-type plasminogen activator activity by inducing a specific plasminogen activator-inhibitor (PAI-1). Using immobilized polyclonal antibodies raised against HT-1080 human fibrosarcoma PAI-1, we have purified HTC PAI-1 from serum-free medium conditioned by dexamethasone-treated HTC hepatoma cells and shown it to be antigenically related to human PAI-1. Greater than 100-fold purification with greater than 75% yield was achieved in a single step. The purified PAI-1 migrates on SDS-pol
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Yasar Yildiz, Songul, Pinar Kuru, Ebru Toksoy Oner, and Mehmet Agirbasli. "Functional Stability of Plasminogen Activator Inhibitor-1." Scientific World Journal 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/858293.

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Plasminogen activator inhibitor-1 (PAI-1) is the main inhibitor of plasminogen activators, such as tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA), and a major regulator of the fibrinolytic system. PAI-1 plays a pivotal role in acute thrombotic events such as deep vein thrombosis (DVT) and myocardial infarction (MI). The biological effects of PAI-1 extend far beyond thrombosis including its critical role in fibrotic disorders, atherosclerosis, renal and pulmonary fibrosis, type-2 diabetes, and cancer. The conversion of PAI-1 from the active to the laten
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Jørgensen, Maja, Malou Philips, Sixtus Thorsen, Johan Selmer, and Jesper Zeuthen. "Plasminogen Activator Inhibitor-1 Is the Primary Inhibitor of Tissue-Type Plasminogen Activator in Pregnancy Plasma." Thrombosis and Haemostasis 58, no. 03 (1987): 872–78. http://dx.doi.org/10.1055/s-0038-1646006.

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SummaryThe aim of the present work was to clarify to what extent plasminogen activator inhibitor-1 (PAI-1) and plasminogen activator inhibitor-2 (PAI-2) contribute to the increase in plasma inhibition of tissue-type plasminogen activator (t-PA) observed during pregnancy. It was demonstrated that a monoclonal antibody against PAI-1 almost completely quenched inhibition of single-chain t-PA and most of the inhibition of two-chain t-PA in plasma during the third trimester of piegnancy. The remaining inhibition of two-chain t-PA was to a great extent abolished by a PAI-2 antibody. The second order
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Ikegami, Masahisa, Tetsuro Nagano, Yasushi Hara, et al. "TISSUE TYPE PLASMINOGEN ACTIVATOR (t-PA) AND PLASMINOGEN ACTIVATOR INHIBITOR (PAI) IN TRANSPLANTED KIDNEYS." Japanese Journal of Urology 86, no. 5 (1995): 991–95. http://dx.doi.org/10.5980/jpnjurol1989.86.991.

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Lobov, Sergei, David R. Croucher, Darren N. Saunders, and Marie Ranson. "Plasminogen activator inhibitor type 2 inhibits cell surface associated tissue plasminogen activator in vitro." Thrombosis and Haemostasis 100, no. 08 (2008): 319–29. http://dx.doi.org/10.1160/th08-02-0119.

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SummaryRegulation of cellular plasminogen activation is necessary for maintenance of tissue homeostasis. Despite increasing evidence for co-expression of tissue type plasminogen activator (tPA) and plasminogen activator inhibitor type-2 (PAI-2;SERPINB2) under patho/physiological conditions, the inhibition of cell-bound tPAmediated plasminogen activation by PAI-2 has not been addressed. Here we show that PAI-2 can inhibit cell-bound tPA activity in vitro and thus prevent plasmin formation. We also examined the potential involvement in this inhibition of the annexin II heterotetramer (AIIt), one
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Carr, Marcus E., C. Krishnamurti, and B. M. Alving. "Effect of Plasminogen Activator Inhibitor-1 on Tissue-Type Plasminogen Activator-Induced Fibrinolysis." Thrombosis and Haemostasis 67, no. 01 (1992): 106–10. http://dx.doi.org/10.1055/s-0038-1648389.

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SummaryThe effect of fibrin on the interaction of human recombinant single-chain tissue plasminogen activator (t-PA) and plasminogen activator inhibitor-1 (PAI-1) was studied in normal rabbit plasma and in plasma with high levels of native PAI-1. t-PA was added to diluted plasma containing calcium (10 mM) and 125I-fibrinogen at 37° C. Clotting was initiated with human thrombin, and lysis was monitored both turbidimetrically and by release of 125I-fibrin degradation products (fdp). The activity of t-PA (50 IU/ml) was rapidly reduced to 15% of the initial value in plasma containing PAI-1 (23 AU/
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Sillen, Machteld, and Paul J. Declerck. "A Narrative Review on Plasminogen Activator Inhibitor-1 and Its (Patho)Physiological Role: To Target or Not to Target?" International Journal of Molecular Sciences 22, no. 5 (2021): 2721. http://dx.doi.org/10.3390/ijms22052721.

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Plasminogen activator inhibitor-1 (PAI-1) is the main physiological inhibitor of plasminogen activators (PAs) and is therefore an important inhibitor of the plasminogen/plasmin system. Being the fast-acting inhibitor of tissue-type PA (tPA), PAI-1 primarily attenuates fibrinolysis. Through inhibition of urokinase-type PA (uPA) and interaction with biological ligands such as vitronectin and cell-surface receptors, the function of PAI-1 extends to pericellular proteolysis, tissue remodeling and other processes including cell migration. This review aims at providing a general overview of the prop
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Ozel Demiralp, Duygu, Huseyin Aktas, and Nejat Akar. "The Effect of Plasminogen Activator Inhibitor-1 −675 4G/5G Polymorphism on PAI-1 Gene Expression and Adipocyte Differentiation." Clinical and Applied Thrombosis/Hemostasis 14, no. 4 (2007): 438–46. http://dx.doi.org/10.1177/1076029607305081.

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Obesity is a complex, multifactorial chronic disease frequently associated with cardiovascular risks, hypertriglyceridemia, low high-density lipoprotein-cholesterol, high blood pressure, and the insulin resistance that appears to be central to the pathogenesis of Type II diabetes. Plasminogen activator inhibitor-1 expression induced in differentiating adipose tissue, but its role in adipogenesis and obesity is poorly understood. Circulating plasminogen activator inhibitor-1 levels are elevated at an early stage of impaired glucose tolerance, resulting in diabetes and metabolic syndrome. Plasmi
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Masson, C., and E. Angles-Cano. "Kinetic analysis of the interaction between plasminogen activator inhibitor-1 and tissue-type plasminogen activator." Biochemical Journal 256, no. 1 (1988): 237–44. http://dx.doi.org/10.1042/bj2560237.

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The kinetics of inhibition of tissue-type plasminogen activator (t-PA) by the fast-acting plasminogen activator inhibitor-1 (PAI-1) was investigated in homogeneous (plasma) and heterogeneous (solid-phase fibrin) systems by using radioisotopic and spectrophotometric analysis. It is demonstrated that fibrin-bound t-PA is protected from inhibition by PAI-1, whereas t-PA in soluble phase is rapidly inhibited (K1 = 10(7) M-1.s-1) even in the presence of 2 microM-plasminogen. The inhibitor interferes with the binding of t-PA to fibrin in a competitive manner. As a consequence the Kd of t-PA for fibr
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Dissertations / Theses on the topic "Plasminogen activator inhibitor type I (PAI-1)"

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Sancho, Elena. "Conformation and activity of plasminogen activator inhibitor type 1 (PAI-1)." Thesis, University of Aberdeen, 1994. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU552562.

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Plasminogen activator inhibitor type 1 (PAI-1) is a unique member of the serpins in that it can adopt various conformations. It is synthesized as an active inhibitor which rapidly converts to a latent form that is not inhibitory. Conformational studies on this protein have been made difficult by this property. The production of recombinant PAI-1 was studied. The expression of r-PAI-1 by the bacterial strain MSD 1005 accounted for some 15-20% of the total cell protein, although some was produced in the form of inclusion bodies. As an attempt to improve the yields of PAI-1 antigen and activity,
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Hasenstab, David R. "Animal models of atherosclerosis : overexpression of plasminogen activator inhibitor type 1 (PAI-1) and tissue factor in the rat carotid artery /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/6315.

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Sundell-Rånby, Birgitta. "Food intake, fibrinolysis and risk factors for cardiovascular disease : studies with special focus on plasminogen activator inhibitor type 1 (PAI-1)." Doctoral thesis, Umeå universitet, Patologi, 1993. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-101290.

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Elevated plasminogen activator inhibitor (PAI-1) activity levels, hyperlipemia, hypertension, impaired glucose tolerance and obesity, in particular central obesity, are all related to increased risk for the development of cardiovascular disease.Some risk factors are known to be and shown to be influenced by dietary habits. One aim of this study was to determine the distribution of PAI-1 activity and its linkage to serum lipids, body build, glucose and insulin (including glucose tolerance) among healthy men and women. Another aim was to elucidate the effects of different diet programes on the r
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Kendziora, Elena Stephanie [Verfasser], Viktor [Akademischer Betreuer] Magdolen, Wilko [Gutachter] Weichert, and Viktor [Gutachter] Magdolen. "Analysis of Urokinase-type Plasminogen Activator (uPA), Plasminogen Activator Inhibitor Type-1 (PAI-1), and Urokinase Plasminogen Activator Receptor (uPAR) Protein Expression by Immunohistochemistry in Triple-Negative Breast Cancer (TNBC) / Elena Stephanie Kendziora ; Gutachter: Wilko Weichert, Viktor Magdolen ; Betreuer: Viktor Magdolen." München : Universitätsbibliothek der TU München, 2020. http://d-nb.info/1208325000/34.

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Hägglöf, Peter. "Plasminogen activator inhibitor type-1 : structure-function studies and its use as a reference for intramolecular distance measurements." Doctoral thesis, Umeå University, Medical Biochemistry and Biophsyics, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-177.

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<p>Inhibitors belonging to the serpin (serine protease inhibitor) family control proteases involved in various physiological processes. All serpins have a common tertiary structure based on the dominant b-sheet A, but they have different inhibitory specificity. The specificity of a serpin is determined by the Pl-Pl’ peptide bond acting as a bait for the target protease which is made up of an exposed reactive centre loop (RCL). The serpin plasminogen activator inhibitor type-1 (PAI-1) is the main physiological inhibitor of urokinase-type and tissue-type plasminogen activators (uPA and tPA, resp
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Bauerfeind, Ursula Katharina [Verfasser], Jürgen [Akademischer Betreuer] Dittmer, and Matthias [Akademischer Betreuer] Dürst. "Einfluss von Biopsie-, Aufarbeitungs- und Asservierungsbedingungen auf den Nachweis von urokinase type plasminogen activator (uPA) und plasminogen activator inhibitor-1 (PAI-1) beim Mammakarzinom / Ursula Katharina Bauerfeind. Betreuer: Jürgen Dittmer ; Matthias Dürst." Halle, Saale : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2009. http://d-nb.info/1024874478/34.

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Billström, Anita. "The significance of urokinase-type plasminogen activator (u-PA) in tumour growth and linomide-induced upregulation of u-PA's endogenous inhibitor PAI-2." Lund : Research Laboratory, Dept. of Obstetrics and Gynaecology, Lund University Hospital, 1997. http://catalog.hathitrust.org/api/volumes/oclc/39751812.html.

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Hertig, Alexandre. "Rôle de l'inhibiteur de type 1 des activateurs du plasminogène dans la régulation de la fibrinolyse glomérulaire : application au modèle de glomérulonéphrite par anticorps anti-membrane basale glomérulaire." Paris 6, 2004. http://www.theses.fr/2004PA066590.

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Hägglöf, Peter. "Plasminogen activator inhibitor type-1 : structure-function studies and its use as a reference for intramolecular distance measurements /." Umeå : Umeå University, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-177.

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North, Christina Johanna. "Effect of dietary fibre on selected haemostatic variables and C-reactive protein / Christina Johanna North." Thesis, North-West University, 2006. http://hdl.handle.net/10394/1417.

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Motivation: Cardiovascular heart disease (CVD) is the leading cause of death worldwide. Risk markers for CVD include, amongst others, the haemostatic factors tissue-type plasminogen activator (t-PA), plasminogen activator inhibitor type 1 (PAI-1), factor VII (FVII) and fibrinogen and more recently, C-reactive protein (CRP), a sensitive marker of inflammation. Epidemiological studies have demonstrated an inverse association between dietary fibre (DF) consumption and risk factors for CVD and CVD prevalence. Some research indicates that this protection may be related to favourable changes in the
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Book chapters on the topic "Plasminogen activator inhibitor type I (PAI-1)"

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Ny, Tor, and Peter Mikus. "Plasminogen Activator Inhibitor Type-2." In Advances in Experimental Medicine and Biology. Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5_12.

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Johnson, Tierra A., Marguerite S. Buzza, Ekemini A. U. Riley, and Toni M. Antalis. "Plasminogen Activator Inhibitor Type-2 (PAI-2)/SerpinB2: A Unique Multifunctional Serpin." In The Serpin Family. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22711-5_8.

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Seiffert, Dietmar, Benien E. Aken, and David J. Loskutoff. "Regulation of Vascular Fibrinolysis by Type 1 Plasminogen Activator Inhibitor." In Cardiovascular Disease 2. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1959-1_26.

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Heaton, Joanne H., and Thomas D. Gelehrter. "Post-Transcriptional Control of Type-1 Plasminogen Activator Inhibitor mRNA." In Endocrine Updates. Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-6446-8_8.

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Loskutoff, David J. "The Biochemistry, Cell and Molecular Biology of Type 1 Plasminogen Activator Inhibitor." In Vascular Endothelium. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3736-6_9.

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Newman, Jonathan. "Plasminogen Activator Inhibitor (PAI-1)." In Encyclopedia of Behavioral Medicine. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1005-9_1279.

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Newman, Jonathan. "Plasminogen Activator Inhibitor (PAI-1)." In Encyclopedia of Behavioral Medicine. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-39903-0_1279.

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Brünner, Nils, Charles Pyke, Claus Holst Hansen, John Rømer, Jan Grøndahl-Hansen, and Keld Danø. "Urokinase plasminogen activator (uPA) and its type 1 inhibitor (PAI-1): Regulators of proteolysis during cancer invasion and prognostic parameters in Breast cancer." In Cancer Treatment and Research. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2592-9_16.

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Sawdey, M., and D. J. Loskutoff. "Regulation of Type One Plasminogen Activator Inhibitor Gene Expression in Cultured Endothelial Cells and the Vessel Wall." In Atherosclerosis. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3754-0_15.

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Declerck, P. J. "Plasminogen activator inhibitor-1 (PAI-1) antigen." In Laboratory Techniques in Thrombosis - a Manual. Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4722-4_26.

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Conference papers on the topic "Plasminogen activator inhibitor type I (PAI-1)"

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Loskutoff, D. J., J. Mimuro, and C. Hekman. "PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644763.

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Plasminogen activation provides an important source of localized proteolytic activity not only during fibrinolysis, but also during ovulation, cell migration, epithelial cell differentiation, tumor invasion and a variety of other physiological processes. Precise regulation of plasminogen activator (PA) activity thus constitutes a critical feature of many biological processes. This control is achieved in large part through the action of specific PA inhibitors (PAIs). Although 4 distinct PAIs have been detected,1the endothelial cellTderived inhibitor (PAI-1) is the only one that efficiently inhi
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Andreasen, P. A., A. Riccio, L. R. Lund, K. G. Welinder, F. Blasi, and K. Danø. "PLASMINOGEN ACTIVATOR INHIBITOR TYPE 1: STUDIES ON STRUCTURE AND REGULATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642810.

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Human plasminogen activator inhibitor type-1 is an Mr∼54,000 protein which specifically inhibits urokinase-type (u-PA) and tissue-type (t-PA) plasminogen activators. During inhibition, u-PA and t-PA convert PAI-1 to an inactive form with Mr∼50,000. We have determined the amino-terminal amino acid sequence of native and converted PAI-1, and isolated and partly sequenced PAI-1 cDNA. The data show that the conversion of PAI-1 consists of cleavage of an Arg-Met bond 33 residues from the carboxy-terminus, thus localizing the reactive center of the inhibitor to that position, and identifying PAI-1 a
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Kruithof, E. KO, W. D. Schleuning, and F. Bachman. "PLASMINOGEN ACTIVATOR INHIBITOR BIOCHEMICAL AND CLINICAL ASPECTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644764.

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Plasminogen activator (PAs) are enzymes that convert the zymogen plasminogen into the trypsin-like protease plasmin, which degrades extracellular matrix proteins and fibrin in the course of fibrinolysis, embryogenesis, tissue remodeling and in tumor metastasis. Plasminogen activator inhibitors (PAIs) are important modulators of PA activity. Several proteins have been identified which inhibit at fast rates urokinase (u-PA) and tissue-type PA (t-PA). In the order of inhibition rate constants these are: a) PAI-1, present in human plasma and platelet extracts and purified from human endothelial ce
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Lambers, J. W. J., M. Cammenga, B. Konig, H. Pannekoek, and J. A. van Mourik. "ACTIVATION OF HUMAN ENDOTHELIAL TYPE PLASMINOGEN ACTIVATOR INHIBITOR (PAI-1) BY NEGATIVELY CHARGED PHOSPHOLIPIDS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642807.

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The endothelial cell type plasminogen activator inhibitor (PAI-1) may exist in an active, latent form that can be converted into an active form upon exposure to denaturants such as sodium dodecyl sulphate (SDS), guanidine-HCl or urea. Here we show that latent PAI-1 can be activated with lipid vesicles, consisting of the negatively charged phospholipids phosphatidylserine (PS) or phosphatidylinositol (PI). The presence of a net negative charge on the phospholipid headgroup is essential for activation. Incubation with lipid vesicles, consisting of the zwitterionic phospholipids phosphatidylcholi
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Strandberg, L., D. Lawrence, and T. Ny. "ISOLATION OF THE GENOMIC REGION CODING FOR TYPE-1 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644439.

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The type-1 Plasminogen Activator Inhibitor (PAI-1) has recently been identified as a member of the Serine Protease Inhibitor family (SERPINS). This family of proteins contain many serine protease inhibitors but also functionally unrelated proteins like ovalbumin and anginotensinogen. PAI-1 inhibits both u-PA and t-PA and might therefore be an important regulator of the fibrinolytic system.In order to study the evolution of the Serpin family as well as PAI-1 gene expression we have isolated the genomic region carrying the PAI-1 gene. A cDNA sequence for PAI-1 was used as probe to screen a human
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de Boer, K., I. Lecander, J. W. ten Cate, J. J. J. Borm, and P. E. Treffers. "PLASMINOGEN ACTIVATOR INHIBITOR OF PLACENTAL TYPE IN PREECLAMPSIA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644461.

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In 24 patients with preeclampsia and in 24 normal pregnant controls, matched for gestational age, fibrinolytic parameters were determined. Aim of the study was to investigate plasminogen activator inhibitory activity (PAI activity) levels and plasminogen activator inhibitor of placental type (PAI 2) in preeclamptic and normal pregnancy and to establish the clinical relevance of these assays. PAI activity was measured by titrating the plasma with single chain t-PA. PAI 2 was measured by means of an ELISA using monoclonal and polyclonal antibodies against the placental inhibitor. Therefore we re
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Ny, T., L. Hansson, and B. Åstedt. "ISOLATION OF cDNA FOR TYPE-2 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642855.

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The placental type plasminogen activator inhibitor (PAI-2) has been purified from extracts of human placenta and from a histiocytic lymphoma cell line. It is mainly an uPA inhibitor but it also inhibits the two-chain form of tPA.In order to determine the factors regulating PAI-2 gene expression and thereby clarify the physiological role of PAI-2 we have undertaken the molecular cloning of PAI-2 cDNA. A λgt11 expression library prepared from placental mRNA, was screened, immunologically using a monoclonal antibody probe developed against PAI-2 purified from human placenta. When 1.7×105 recombin
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Bosma, P. J., E. A. van den Berg, and T. Kooistra. "ISOLATION OF THE GENE CODING FOR HUMAN PLASMINOGEN ACTIVATOR INHIBITOR TYPE 1 (PAI-1)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644440.

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A human placenta genomic DNA cosmid library was screened for the presence of the PAI-1 gene using a cDNA probe coding for PAI-1. Two overlapping recombinant cosmids were obtained that contain human DNA spanning 55 kb. The cosmids were mapped using 3' and 5' end probes isolated from an almost full-length cDNA clone of 2.5 kb. The two cosmids were found to contain the entire structural PAI-1 gene (approximately 15 kb) and also included 25 kb 5' flanking sequences. The transcription initiation site was identified by SI nuclease protection experiments and the promotor region was sequenced. Further
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Schleef, R. R., M. P. Bevilacqua, M. Sawdey, M. A. Gimbrone, and D. J. Loskutoff. "INTERLEUKIN 1 (IL-1) AND TUMOR NECROSIS FACTOR (TNF) ACTIVATION OF VASCULAR ENDOTHELIUM: EFFECTS ON PLASMINOGEN ACTIVATOR INHIBITOR (PAI-1) AND TISSUE-TYPE PLASMINOGEN ACTIVATOR (tPA)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642864.

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The regulation of the fibrinolytic system of cultured human umbilical vein endothelial cells (ECs) by two distinct monokines (IL-1 and TNF) was investigated. Conditioned media (CM) was collected from ECs cultured for 24 h in the presence of the monokines and analyzed in quantitative immunological assays for PAI-1 activity and tPA antigen. Both monokines induced a dose-dependent increase in extracellular PAI-1 activity, with a concomitant decrease in tPA antigen. Maximal effects were achieved with either 10 U/ml IL-1 or 200 U/ml of TNF, and resulted in a 4 fold increase in PAI-1 and a 50% decre
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Okada, M., Y. Sakata, and M. Matsuda. "INTERACTION OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (tPA)-INHIBITOR COMPLEX WITH FIBRIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644441.

Full text
Abstract:
Tissue type plasminogen activator (tPA) binds to fibrin resulting in marked enhancement of its activity, but also binds to its some specific fast acting inhibitors (PAIs). The ternary interaction of tPA, PAI and fibrin has not been fully elucidated, however. We studied the interaction of the tPA-PAI complex with fibrin using PAI-1 derived from human umbilical vein endothelial cells (ECs), either as a denaturant activated purified form (dPAI) or a native form (nPAI).When ECs were incubated with125I-tPA, nPAI formed a complex with 125I-tPA (125I-complex) in dose and time dependent manners. Resul
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