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Haemostasis and Thrombosis
Published in Karl H. Pang, Nadir I. Osman, James W.F. Catto, Christopher R. Chapple, Basic Urological Sciences, 2021
Vascular spasm (vasoconstriction) and the endotheliumVasoconstrictionA brief intense contraction of blood vessels.Decreases blood flow to the area of injury.In response to vascular injury or inflammation, the endothelium becomes prothrombotic.It downregulates the expression of anti-thrombotic molecules.It expresses procoagulant tissue factor (TF).It expresses adhesion molecules which mediate platelet and leucocyte capture.It releases the von Willebrand factor (VWF) which mediates platelet capture and aggregation.It releases plasminogen activator inhibitor-1 (PAI-1: inhibits fibrinolysis).
Fibrinolysis and Diabetes Mellitus
Published in Pia Glas-Greenwalt, Fibrinolysis in Disease Molecular and Hemovascular Aspects of Fibrinolysis, 2019
Michael W. Mansfield, Peter J. Grant
Plasminogen activator inhibitor-1 (PAI-1) is a rapid, and physiologically the most important, inhibitor of both t-PA and u-PA.3 Plasma levels of PAI-1 are attributed with being the principal determinant of fibrinolytic activity.4,5 PAI-1 is synthesized by endothelial cells, hepatocytes, and probably vascular smooth muscle cells, and it is also found in high concentration in the alpha granules of platelets.6-8
Coagulation Theory, Principles, and Concepts
Published in Harold R. Schumacher, William A. Rock, Sanford A. Stass, Handbook of Hematologic Pathology, 2019
A number of inhibitors have been identified which inhibit the activity of tPA and urokinase. These inhibitors are related to antithrombin III and are classified as serpins. Plasminogen activator inhibitor 1 (PAI-1) is found in plasma and platelets, and is produced by endothelial cells, hepatocytes, smooth muscle cells, fibroblasts, and various malignant cell types. PAI-1 inhibits the activity of both forms of tPA, and two-chained urokinase, but not prourokinase or the streptokinase-plasminogen complex (103,104).
Effects of saturated versus unsaturated fatty acids on metabolism, gliosis, and hypothalamic leptin sensitivity in male mice
Published in Nutritional Neuroscience, 2023
Jesús Fernández-Felipe, Maria Valencia-Avezuela, Beatriz Merino, Beatriz Somoza, Victoria Cano, Ana B. Sanz-Martos, Laura M. Frago, Maria S. Fernández-Alfonso, Mariano Ruiz-Gayo, Julie A. Chowen
Adipose tissue produces high levels of PAI1 and knockout mice for PAI1 are more resistant to HFD-induced obesity with this effect possibly being mediated through PAI-1 modulation of hypothalamic leptin resistance [35]. Here circulating levels of PAI-1 were elevated in both groups ingesting fatty acid-enriched diets, which is in accordance with their increased weight gain. In contrast, only SOLF mice were found to exhibit attenuated responses to leptin at the hypothalamic level, suggesting that other factors are also involved in the development of this phenomenon. Indeed, both leptin production and signaling were differentially modulated by the fatty acid-enriched diets employed here. Circulating leptin levels were increased by both diets, but this rise was significantly greater in mice on the unsaturated fatty acid diet. These modifications in serum leptin levels were coincident with a significant rise in leptin mRNA levels in the adipose tissue of UOLF mice, while this increase was not significant in SOLF animals. Increased circulating leptin levels in obesity are due to increased fat mass and/or increased synthesis of this adipokine. Although we found that the weights of the WAT deposits were not statistically different between SOLF and UOLF mice, there was a tendency for UOLF mice to have higher levels of adipose tissue compared to SOLF mice and this most likely would be more apparent with more precise measurements. Thus, it appears that plasma leptin levels are higher in UOLF mice in accordance with higher Lep expression levels, as well as possibly the amount of WAT.
Triglyceride/HDL-cholesterol ratio and plasminogen activator inhibitor-1 independently predict high pulse pressure in sickle cell trait and disease
Published in Archives of Physiology and Biochemistry, 2020
Olatunde P. Olabode, Olawale M. Akinlade, Abiola S. Babatunde, Musbau I. Abdulazeez, Sikiru A. Biliaminu, Adewumi O. Oyabambi, Victoria A. Olatunji, Ayodele O. Soladoye, Lawrence A. Olatunji
Plasminogen activator inhibitor-1 (PAI-1), a marker of atherothrombotic CVD, is a key regulator of fibrinolysis which acts by inhibiting tissue plasminogen activator (tPA). In normal individuals, increased levels of PAI-1 have been shown to be associated with insulin resistance (IR), obesity, diabetes mellitus (DM), and CVD (Cesari et al.2010). Evidence has also established a positive link between PAI-1, TC, LDL-C, and TG, suggesting that an elevated PAI-1 level may increase cardiometabolic disease (CMD) risk (Lira et al.2010). Additionally, studies strongly suggest that C-reactive protein (CRP), also a biomarker of systemic pro-inflammation is directly involved in atherosclerosis. Interestingly, CRP stimulates PAI-1 synthesis and may promote CVD via the PAI-1 induction (Devaraj et al.2003). In SCD patients, elevated PAI-1 level has also been reported in steady state which is further elevated during sickle vaso-occlusive crisis (Nsiri et al.1997), predisposing them to devastating complications such as pulmonary hypertension and stroke (Hillery and Panepinto 2004). Moreover, SCD itself is considered to be an inflammatory process (Platt 2000) capable of promoting oxidative stress. However, there is paucity of information on the association between SCT and PAI-1 levels.
Plasminogen activator inhibitor-1 is involved in interleukin-1β-induced matrix metalloproteinase expression in murine chondrocytes
Published in Modern Rheumatology, 2019
Akihiro Moritake, Naoyuki Kawao, Kiyotaka Okada, Masayoshi Ishida, Kohei Tatsumi, Osamu Matsuo, Masao Akagi, Hiroshi Kaji
Plasminogen activator inhibitor-1 (PAI-1) is a serine protease inhibitor that suppresses activity of plasminogen activators, then primarily acting as an inhibitor of fibrinolysis [4]. PAI-1, expressed in various tissues including cartilage and regulated by numerous factors, exerts both fibrinolysis-dependent and -independent functions in various tissues, and it is related to the pathogenesis of cardiovascular diseases, cancers and diabetes [4]. We recently revealed that PAI-1 is involved in the pathogenesis of diabetes- and glucocorticoid-induced bone metabolism abnormality in mice [4–6]. Moreover, we reported that PAI-1 deficiency accelerated the subchondral osteopenia eight weeks after induction of OA with destabilization of the medial meniscus surgery in ovariectomized mice [7], although we could not clarify the roles of PAI-1 in the chondrocytes for the significant influences of the subchondral bone changes on the cartilage tissues in vivo in that study. It has previously reported that IL-1β enhances the expression of PAI-1 in the cartilage tissue and rodent chondrocytes [3,8]. Van Ness et al. [9] reported that PAI-1 deficiency attenuated joint inflammation measured by 99mTc uptake and synovial inflammation evaluated by the histological score by day-10 during antigen-induced arthritis in mice. However, the functional roles of PAI-1 in the chondrocytes have still remained unknown.