Academic literature on the topic 'Plasminogen activator inhibitor type-1'

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Journal articles on the topic "Plasminogen activator inhibitor type-1"

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MIMURO, Jun. "Type 1 plasminogen activator inhibitor." Japanese Journal of Thrombosis and Hemostasis 1, no. 1 (1990): 17–24. http://dx.doi.org/10.2491/jjsth.1.17.

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Reilly, T. M., S. A. Mousa, R. Seetharam, and A. L. Racanelli. "Recombinant plasminogen activator inhibitor type 1." Blood Coagulation & Fibrinolysis 5, no. 1 (1994): 73–82. http://dx.doi.org/10.1097/00001721-199402000-00011.

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MEHTA, R., and A. D. SHAPIRO. "Plasminogen activator inhibitor type 1 deficiency." Haemophilia 14, no. 6 (2008): 1255–60. http://dx.doi.org/10.1111/j.1365-2516.2008.01834.x.

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Svendsen, Ole Lander, Christian Hassager, Claus Christiansen, Jørn Dalsgaard Nielsen, and Kaj Winther. "Plasminogen Activator Inhibitor–1, Tissue-Type Plasminogen Activator, and Fibrinogen." Arteriosclerosis, Thrombosis, and Vascular Biology 16, no. 3 (1996): 381–85. http://dx.doi.org/10.1161/01.atv.16.3.381.

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Hua, Ya, Guohua Xi, Richard F. Keep, Jimin Wu, Yajun Jiang, and Julian T. Hoff. "Plasminogen Activator Inhibitor-1 Induction after Experimental Intracerebral Hemorrhage." Journal of Cerebral Blood Flow & Metabolism 22, no. 1 (2002): 55–61. http://dx.doi.org/10.1097/00004647-200201000-00007.

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Serine proteases, such as thrombin and tissue-type plasminogen activator, play an important role in brain injury after intracerebral hemorrhage and other neurologic disorders. Plasminogen activator inhibitor-1 is one of the serine protease inhibitors, or serpins. The balance between serine proteases and serpins may affect the outcome of intracerebral hemorrhage. The purpose of this study was to determine whether plasminogen activator inhibitor-1 and tissue-type plasminogen activator are upregulated after intracerebral hemorrhage and the role that thrombin plays in that induction. Plasminogen a
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Gilabert, Juan, Amparo Estellés, Justo Aznar, et al. "Contribution of Platelets to Increased Plasminogen Activator Inhibitor Type 1 in Severe Preeclampsia." Thrombosis and Haemostasis 63, no. 03 (1990): 361–66. http://dx.doi.org/10.1055/s-0038-1645047.

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SummaryPlasminogen activator inhibitor activity and antigen were evaluated in plasma, serum and platelet lysate in patients with severe preeclampsia (n = 12), and in normal pregnant women (n = 21). Other parameters, including β-thromboglobulin and platelet count, were also evaluated. A significant increase (p <0.05) in β-thromboglobulin was observed in platelet poor plasma of preeclamptic women when compared with that of normal pregnant women, and the platelet count was lower in the preeclamptic group than in the normal pregnant group. A significant increase in plasminogen activator inhibit
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Yang, Hong, Xiangyu Wang, and Mohan K. Raizada. "Characterization of Signal Transduction Pathway in Neurotropic Action of Angiotensin II in Brain Neurons." Endocrinology 142, no. 8 (2001): 3502–11. http://dx.doi.org/10.1210/endo.142.8.8348.

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Abstract Interaction of angiotensin II with the neuronal angiotensin type 1 receptor stimulates the PI3K signaling pathway. Our objective in this study was to investigate the hypothesis that the PI3K cascade regulates the neurotropic actions of angiotensin II in rat brain neurons. We followed growth associated protein-43 expression and neurite extension as markers of neurotropic activity. Angiotensin II, through its interaction with the angiotensin type 1 receptor, increased growth associated protein-43 expression and neurite extension. These effects were abolished by pretreatment of neurons w
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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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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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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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Dissertations / Theses on the topic "Plasminogen activator inhibitor type-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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Alotaibi, Fahad T. "Plasminogen activator inhibitor-1 in endometriosis." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/59961.

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Endometriosis is a disease that affects almost 10% of reproductive-age women, where 50 % of these women have pelvic pain with sexual intercourse. Deep endometriosis is defined as an endometriotic lesion penetrating to a depth of 5 mm or more, and is characterized by both fibrosis (forming nodules) and invasion (into structures such as the colon). Other groups have found that increased plasminogen activator inhibitor-1 (PAI-1) or (SERPINE1) expression was associated with fibrosis and tumor invasion. In addition, a previous study found that the SERPINE1 4G allele (and thus increased gene express
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Dawson, Sally. "Genetic variation at the plasminogen activator inhibitor-1 locus and its effect on plasminogen activator inhibitor-1 expression." Thesis, Imperial College London, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298676.

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Panahloo, Archia. "Plasminogen activator inhibitor-1 and cardiovascular risk." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.286442.

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Sui, Guang-Chao. "Structure-function studies of plasminogen activator inhibitor-1 /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-3255-7/.

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Tierney, Marcus John 1973. "Post-transcriptional regulation of plasminogen activator inhibitor type 2." Monash University, Dept. of Medicine, 2002. http://arrow.monash.edu.au/hdl/1959.1/8496.

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Miyazaki, Hiroshi. "Studies on Inhibitors of Plasminogen Activator Inhibitor-1(PAI-1) and Inhibitors of PAI-1 Production as Antithrombotic Agents." 京都大学 (Kyoto University), 2010. http://hdl.handle.net/2433/126818.

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Byberg, Liisa. "Plasminogen Activator Inhibitor-1 and the Insulin Resistance Syndrome." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2002. http://publications.uu.se/theses/91-554-5307-4/.

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Dickinson, Joanne L. "The regulation and function of plasminogen activator inhibitor type 2 /." [St Lucia, Qld.], 1995. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe18712.pdf.

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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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Books on the topic "Plasminogen activator inhibitor type-1"

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Byberg, Liisa. Plasminogen Activator Inhibitor-1 & the Insulin Resistance Syndrome. Uppsala Universitet, 2002.

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Book chapters on the topic "Plasminogen activator inhibitor type-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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Agirbasli, Deniz, and Mehmet Agirbasli. "Plasminogen Activator Inhibitor-1." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101797.

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Agirbasli, Deniz, and Mehmet Agirbasli. "Plasminogen Activator Inhibitor-1." In Encyclopedia of Signaling Molecules. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_101797-1.

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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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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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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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Huber, Kurt, I. Lang, M. Joerg, P. Probst, and B. R. Binder. "Plasminogen activator inhibitor-1 and transient myocardial ischemia." In Predisposing Conditions for Acute Ischemic Syndromes. Steinkopff, 1989. http://dx.doi.org/10.1007/978-3-662-09434-1_7.

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Fay, William P., and David Ginsburg. "Fibrinogen, Factor VII, and Plasminogen Activator Inhibitor-1." In Genetic factors in coronary heart disease. Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-1130-0_9.

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Conference papers on the topic "Plasminogen activator inhibitor type-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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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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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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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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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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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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Booth, N. A., A. Reith, and B. Bennett. "A PLASMINOGEN ACTIVATOR INHIBITOR (PAI-2) CIRCULATES IN TWO HIGH MOLECULAR WEIGHT FORMS IN PREGNANCY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644459.

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Normal vascular endothelium and platelet α-granules contain an inhibitor of plasminogen activator (PAI-1) of about 48000 molecular weight, which is released by stimuli such as thrombin. An immunologically distinct inhibitor (PAI-2) of about 47000 molecular weight has been purified from placenta and from a histiocytic cell line U-937. The level of PA-inhibition in plasma is raised in late pregnancy and this may be due to increases in PAI-1 or in PAI-2 or in both.Using SDS-PAGE and zymography on fibrin/plasminogen /u-PA detector gels, we have found that normal plasma contains a band of inhibitio
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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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Chmielewska, J., and B. Wiman. "ON THE KINETICS OF THE INHIBITION OF PLASMINOGEN ACTIVATORS BY THE PLASMINOGEN ACTIVATOR INHIBITOR PAI-1." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642808.

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The kinetics of the inhibition of the following plasminogen activators: one- and two-chain tissue plasminogen activator (t-PA) and low and high molecular weight urokinase (UK) by PAI-1 was studied. For this purpose direct systems were employed and the reactions were studied in the presence of different concentrations of plasminogen activator chromogenic substrates. The second-order rate constant of the association reaction was estimated from the initial decline in plasminogen activator activity. Determination of the rate constants in the absence of substrates was performed by plotting the rate
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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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Reports on the topic "Plasminogen activator inhibitor type-1"

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Song, Xiaoling. Plasminogen activator inhibitor 1: Mechanisms of its synergistic regulation by growth factors. Office of Scientific and Technical Information (OSTI), 2010. http://dx.doi.org/10.2172/1048513.

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