Progesterone regulation of plasminogen activator inhibitor 1 (PAI-1) antigen and mRNA levels in human endometrial stromal cells

1992 ◽  
Vol 66 (1) ◽  
pp. 75-87 ◽  
Author(s):  
B Casslén ◽  
S Urano ◽  
T Ny
Keyword(s):  
Plasminogen Activator ◽  
Stromal Cells ◽  
Plasminogen Activator Inhibitor ◽  
Mrna Levels ◽  
Plasminogen Activator Inhibitor 1 ◽  
Endometrial Stromal Cells ◽  
Activator Inhibitor ◽  
Pai 1

scholarly journals Sex Steroids Regulate the Expression of Plasminogen Activator Inhibitor-1 and its mRNA in Fibroblasts Derived from Uterine Endometrium

1996 ◽  
Vol 33 (6) ◽  
pp. 545-550 ◽  
Author(s):  
Jiro Fujimoto ◽  
Masashi Hori ◽  
Satoshi Ichigo ◽  
Teruhiko Tamaya
Keyword(s):  
Plasminogen Activator ◽  
Stromal Cells ◽  
Sex Steroids ◽  
Plasminogen Activator Inhibitor ◽  
Tissue Type ◽  
Endometrial Stromal Cells ◽  
Uterine Endometrium ◽  
Type Plasminogen Activator ◽  
Activator Inhibitor ◽  
Pai 1

In order to clarify a role of stromal cells in sex steroidal neovascularization, plasminogen activator inhibitor (PAI)-1 [an inhibitor of tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA)] and its messenger ribonucleic acid (mRNA) were analysed in fibroblasts derived from uterine endometrium as a model for endometrial stromal cells under the influence of sex steroids. The determinations were carried out by an enzyme-linked immunosorbent assay (ELISA) and reverse transcription-polymerase chain reaction-Southern blotting, respectively. In the fibroblasts, either estradiol or progestogens (progesterone, medroxy progesterone acetate or 17α-hydroxyprogesterone) induced expressions of PAI-1 and its mRNA, and their combination further increased their expression by approximately twofold. PAI-1 from endometrial stromal cells under the influence of sex steroids might contribute to endometrial neovascularization through its effect on endothelial cells in endometrial vessels.

scholarly journals Plasminogen Activator Inhibitor-1 Regulates LPS Induced Inflammation in Rat Macrophages through Autophagy Activation

2014 ◽  
Vol 2014 ◽  
pp. 1-12 ◽  
Author(s):  
Zhong-Hui Wang ◽  
Wei-Ying Ren ◽  
Lei Zhu ◽  
Li-Juan Hu
Keyword(s):  
Western Blot ◽  
Plasminogen Activator ◽  
Plasminogen Activator Inhibitor ◽  
Mrna Levels ◽  
Plasminogen Activator Inhibitor 1 ◽  
Inflammatory Reactions ◽  
Protein Levels ◽  
Nr8383 Cells ◽  
Activator Inhibitor ◽  
Pai 1

Background. The mechanisms by which plasminogen activator inhibitor-1 (PAI-1) regulates inflammation, especially in acute respiratory distress syndrome (ARDS), are largely unknown.Objective. To assess the relationship between PAI-1 and autophagy in inflammatory reactions induced by LPS in rat NR8383 cells.Methods. ELISA was used to assess the amounts of TNF-α, IL-1β, and PAI-1 in cell culture supernatants; TLR4, MyD88, PAI-1, LC3, Beclin1, and mTOR protein and mRNA levels were determined by western blot and quantitative RT-PCR, respectively; western blot was used to determine NF-κB protein levels. To further evaluate the role of PAI-1, the PAI-1 gene was downregulated and overexpressed using the siRNA transfection technology and the pCDH-PAI-1, respectively. Finally, the GFP Positive Expression Rate Method was used to determine the rate of GFP-LC3 positive NR8383 cells.Results. In LPS-induced NR8383 cells, TNF-α, IL-1β, and PAI-1 expression levels increased remarkably. Upon PAI-1 knockdown, TNF-α, IL-1β, PAI-1, TLR4, MyD88, NF-κB, LC3, and Beclin1 levels were decreased, while mTOR increased. Conversely, overexpression of PAI-1 resulted in increased amounts of TNF-α, IL-1β, PAI-1, TLR4, MyD88, NF-κB, LC3, and Beclin1. However, no significant change was observed in mTOR expression.Conclusions.In NR8383 cells, PAI-1 contributes in the regulation of LPS-induced inflammation, likely by promoting autophagy.

Fluvastatin Inhibits Basal and Stimulated Plasminogen Activator Inhibitor 1, but Induces Tissue Type Plasminogen Activator in Cultured Human Endothelial Cells

2000 ◽  
Vol 84 (07) ◽  
pp. 59-64 ◽  
Author(s):  
Luciana Mussoni ◽  
Cristina Banfi ◽  
Luigi Sironi ◽  
Magda Arpaia ◽  
Elena Tremoli
Keyword(s):  
Endothelial Cells ◽  
Plasminogen Activator ◽  
De Novo ◽  
Umbilical Vein ◽  
Plasminogen Activator Inhibitor ◽  
Tissue Type ◽  
Mrna Levels ◽  
Plasminogen Activator Inhibitor 1 ◽  
Activator Inhibitor ◽  
Pai 1

SummaryThe effects of fluvastatin, a synthetic hydroxymethylglutaryl coenzyme A (HMG-CoA) inhibitor, on the biosynthesis of tissue plasminogen activator (t-PA) and of its major physiological inhibitor (plasminogen activator inhibitor type 1, PAI-1) were investigated in cultured human umbilical vein endothelial cells (HUVEC). Fluvastatin (0.1 to 2.5 µM), concentration-dependently reduced the release of PAI-1 antigen by unstimulated HUVEC, subsequent to a reduction in PAI-1 steady-state mRNA levels and de novo protein synthesis. In contrast, it increased t-PA secretion.The drug also reduced PAI-1 antigen secreted in response to 10 µg/ml bacterial lipopolysaccharide (LPS), 100 U/ml tumour necrosis factor α (TNFα) or 0.1 µM phorbol myristate acetate (PMA).Mevalonate (100 µM), a precursor of isoprenoids, added to cells simultaneously with fluvastatin, suppressed the effect of the drug on PAI-1 both in unstimulated and stimulated cells as well as on t-PA antigen. Among intermediates of the isoprenoid pathway, all-trans-geranylgeraniol (5 µM) but not farnesol (10 µM) prevented the effect of 2.5 µM fluvastatin on PAI-1 antigen, which suggests that the former intermediate of the isoprenoid synthesis is responsible for the observed effects.

Plasminogen Activator Inhibitor 1: Biosynthesis and mRNA Level Are Increased by Insulin in Cultured Human Hepatocytes

1989 ◽  
Vol 62 (02) ◽  
pp. 723-728 ◽  
Author(s):  
T Kooistra ◽  
P J Bosma ◽  
H A M Töns ◽  
A P van den Berg ◽  
P Meyer ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Insulin Dose ◽  
Mrna Level ◽  
Primary Cultures ◽  
Plasminogen Activator Inhibitor ◽  
Human Hepatocytes ◽  
Mrna Levels ◽  
Plasminogen Activator Inhibitor 1 ◽  
Activator Inhibitor ◽  
Pai 1

SummaryClinical studies have shown that plasma insulin levels are closely related to plasma plasminogen activator inhibitor 1 (PAI-1) levels. To investigate a possible involvement of hepatocytes we have studied the effect of insulin on PAI-1 production by primary cultures of human hepatocytes. We have isolated human hepatocytes from seven left liver lobes. PAI-1 activity measured in 24 hours conditioned medium varied considerably between the various hepatocyte preparations (from 2.9 to 8.5 units per 5 cm2of cells) possibly as a result of interindividual variability in basal PAI-1 production by hepatocytes from different donors. In all cases, however, the relative extent, time profile and dose-dependency of the insulin-induced increase in PAI-1 synthesis were consistent. Up to about 7 nM, insulin dose-dependently increased both PAI-1 activity and PAI-1 antigen production. The increase in PAI-1 synthesis became measurable between 4 and 8 hours after addition of the hormone, and maximally reached twofold control values. The increase in PAI-1 synthesis could be fully explained by a concomitant increase in PAI-1 mRNA levels. The effect of insulin seems fairly specific for the synthesis of PAI-1: overall protein synthesis and mRNA levels of some control proteins (albumin and fibrinogen) did not markedly change after insulin addition. These results, obtained with primary cultures of human hepatocytes, are fully comparable with those obtained with the hepatocellular carcinoma cell line Hep G2. They strengthen the suggestion that the elevated level of PAI-1 in high insulin plasma might be the result of increased hepatic synthesis of PAI-1.

Food deprivation induces adipose plasminogen activator inhibitor-1 (PAI-1) expression without accumulation of plasma PAI-1 in genetically obese and diabetic db/db mice

2007 ◽  
Vol 98 (10) ◽  
pp. 864-870 ◽  
Author(s):  
Katsutaka Oishi ◽  
Naoki Ohkura ◽  
Juzo Matsuda ◽  
Norio Ishida
Keyword(s):  
Plasminogen Activator ◽  
Food Deprivation ◽  
Fibrinolytic Activity ◽  
Plasminogen Activator Inhibitor ◽  
Mrna Levels ◽  
Wild Type ◽  
Plasminogen Activator Inhibitor 1 ◽  
Adipose Tissues ◽  
Activator Inhibitor ◽  
Pai 1

SummaryRelationships between energy intake and fibrinolytic functions have been documented in detail. We evaluated food deprivation (FD) as a means of modulating fibrinolytic activity in genetically obese and diabetic db/db mice and in their lean counterparts. Twelve hours of FD induced considerable gene expression of plasminogen activator inhibitor-1 (PAI-1) in both epididymal (3.8-fold, p<0.05) and intestinal (2.4-fold, p<0.05) adipose tissues without affecting plasma PAI-1 levels in db/db mice, whereas the FD did not affect these parameters in wild-type mice. Importantly, 24 hours of FD increased the plasma PAI-1 content in wild-type (1.9-fold, p<0.01) but not in db/db mice, although adipose PAI-1 mRNA levels were significantly increased in db/db mice. The plasma PAI-1 content significantly correlated with hepatic PAI-1 mRNA levels in wild-type (r=0.84, p<0.01) and in db/db (r=0.63, p<0.01) mice. However, plasma PAI-1 did not correlate with adipose PAI-1 expression in db/db mice, although adipose tissue in general is thought to be the principal site of PAI-1 production in obesity. Hepatic PAI-1 expression was closely correlated with serum levels of free fatty acids in wild-type (r=0.72, p<0.01), but not in db/db mice. Adipose PAI-1 expression significantly correlated with serum corticosterone levels in both genotypes (wild-type, r=0.52, p<0.05; db/db, r=0.51, p<0.01), suggesting that adipose PAI-1 expression is up-regulated by fastinginduced glucocorticoids. The present findings suggested that fasting differentially affects fibrinolytic activity in obese and lean subjects and that PAI-1 expression in the liver as well as in adipose tissues comprises an important determinant of increased risk for cardiovascular disease in obesity.

Regulation of Plasminogen Activator Inhibitor-1 mRNA in Human Endothelial Cells

1988 ◽  
Vol 60 (01) ◽  
pp. 063-067 ◽  
Author(s):  
E A van den Berg ◽  
E D Sprengers ◽  
M Jaye ◽  
W Burgess ◽  
T Maciag ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasminogen Activator ◽  
Growth Medium ◽  
Cdna Probe ◽  
Plasminogen Activator Inhibitor ◽  
Mrna Levels ◽  
Human Endothelial Cells ◽  
Plasminogen Activator Inhibitor 1 ◽  
Activator Inhibitor ◽  
Pai 1

SummaryThe plasminogen activator inhibitor (PAI-1) from endothelial cells is a potentially important regulator of plasminogen activator activity. Cultured human endothelial cells increase their PAI-1 production upon stimulation with LPS and TNF, agents that are known to cause an increase in PAI-1 levels in vivo.We isolated a PAI-1 cDNA probe, and by RNA hybridization analysis studied the regulation of PAI-1 mRNA synthesis in human endothelial artery cells. Freshly isolated endothelial cells do not contain detectable amounts of PAI-1 mRNA, but after adherence and incubation for 18 h in growth medium produce considerable amounts of PAI-1 activity and contain PAI-1 mRNA levels comparable to those found in subcultured cells. When subcultured endothelial cells are incubated for 6 h with LPS or TNF, both species of PAI-1 mRNA increase 10 to 20 fold, while PAI-1 activity in the growth medium increases only 1.5 to 2 fold. Stimulation of endothelial cells in the presence of cycloheximide (CHX) results in superinduction of mainly the 3.0 kb PAI-1 mRNA. The 3' end of this mRNA contains a 60 bp AT-rich sequence, that resembles 3' sequences present in a number of other genes superinducible with CHX.

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