Lysophosphatidic Acid Induction of Tissue Factor Expression in Aortic Smooth Muscle Cells

Cui, Mei‐Zhen; Zhao, Guo-Jun; Winokur, Allison L.; Laag, Essam; Bydash, Jason R.; Penn, Marc S.; Chisolm, Guy M.; Xu, Xuemin

doi:10.1161/01.atv.0000054660.61191.7d

Cited by 47 publications

(45 citation statements)

References 56 publications

(47 reference statements)

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“…16 In contrast, ERK, but not p38, regulates lysophosphatic acid-induced TF expression in vascular smooth muscle cells. 19 Interestingly, in both LPS-stimulated monocytes and thrombin-stimulated en- dothelial cells, TF expression occurs through activation of all 3 MAP kinase pathways. 27,39 We show here that specific inhibition of any of the 3 MAP kinases leads to a marked reduction in histamine-induced TF expression in HAECs even at low concentrations of the respective inhibitor.…”

Section: Discussionmentioning

confidence: 99%

“…19 Cells were grown in 6-well plates; after stimulation, cells were washed twice with PBS, followed by incubation with human FVIIa and FX at 37°, allowing the formation of a TF/FVIIa complex at the cell surface. The TF/FVIIa complex converted human FX to activated FX, which was measured by its ability to metabolize a chromogenic substrate.…”

Section: Tf Surface Activitymentioning

confidence: 99%

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Histamine Induces Tissue Factor Expression

et al. 2005

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Background— Histamine can induce coronary vasospasm, leading to variant angina and acute myocardial infarction. However, the role of histamine in thrombus formation is ill defined. Hence, this study investigates whether histamine induces tissue factor (TF) expression in vascular cells. Methods and Results— Histamine (10 −8 to 10 −5 mol/L) induced TF expression in a concentration-dependent manner in human aortic endothelial and vascular smooth muscle cells, whereas TF pathway inhibitor expression remained unaffected. RT-PCR and Northern blotting revealed that histamine stimulated TF mRNA transcription, peaking at 1 hour. Protein expression increased 18-fold ( P <0.02) with a maximum at 5 hours, which was paralleled by a 4-fold augmentation in surface activity ( P <0.01). These effects were completely prevented by pretreatment with the H 1 receptor antagonists mepyramine ( P <0.0001), chlorpheniramine, and diphenhydramine but not the H 2 receptor antagonist cimetidine ( P =NS). Histamine induced a time-dependent, H 1 receptor–mediated activation of p38 MAP kinase (p38), p44/42 MAP kinase (ERK), and c-jun terminal NH 2 kinase (JNK). Blocking of p38, ERK, or JNK with SB203580 ( P <0.0001), PD98059 ( P <0.0001), or SP600125 ( P <0.0001), respectively, impaired histamine-induced TF expression in a concentration-dependent manner. In contrast, histamine-stimulated TF expression was increased by phosphatidylinositol 3-kinase inhibition with LY294002 or wortmannin, whereas it was not affected by Rho-kinase inhibition with Y-27632 or hydroxyfasudil. Conclusions— Histamine induces expression of TF, but not TF pathway inhibitor, in vascular cells via activation of the H 1 , but not H 2 , receptor. This effect is mediated by the MAP kinases p38, ERK, and JNK. This observation may open novel perspectives in the treatment of variant angina and acute coronary syndromes.

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Section: Discussionmentioning

confidence: 99%

Section: Tf Surface Activitymentioning

confidence: 99%

Histamine Induces Tissue Factor Expression

et al. 2005

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“…17 Cells were grown to confluence in 12-well plates. After stimulation with TNF-␣, cells were washed twice with phosphate-buffered saline and incubated with human FVIIa and FX at 37°, allowing for the formation of the TF/FVIIa complex at the cell surface.…”

Section: Tf Surface Activitymentioning

confidence: 99%

Cardiac Glycosides Regulate Endothelial Tissue Factor Expression in Culture

Stähli

Berndt

Akhmedov

et al. 2007

ATVB

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Background-Tissue factor (TF) plays an important role in acute coronary syndromes and stent thrombosis. This study investigates whether Na ϩ /K ϩ -ATPase regulates TF expression in human endothelial cells. Methods and Results-Ouabain inhibited tumor necrosis factor (TNF)-␣-induced endothelial TF protein expression; maximal inhibition occurred at 10 Ϫ5 mol/L, reached more than 70%, and was observed throughout the 5 hours stimulation period. The decrease in protein expression was paralleled by a reduced TF surface activity. Similarly, lowering of extracellular potassium concentration inhibited TNF-␣-induced TF protein expression. In contrast, ouabain did not affect TNF-␣-induced expression of full-length TF mRNA for up to 5 hours of stimulation; instead, expression of alternatively-spliced TF mRNA was upregulated after 3 and 5 hours of stimulation. Ouabain did not affect TNF-␣-induced activation of the MAP kinases p38, extracellular signal-regulated kinase (ERK), and c-Jun terminal NH 2 kinase; activation of Akt and p70S6 kinase remained unaltered as well. Similar to the MAP kinases, ouabain did not affect TNF-␣-induced degradation of IB-␣. Ouabain had no effect on TF protein degradation. Conclusions-Naϩ /K ϩ -ATPase is required for protein translation of endothelial TF in culture. This observation provides novel insights into posttranscriptional regulation of TF expression. (Arterioscler Thromb Vasc Biol.

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“…22,25 Cells were grown in 6-well plates; after stimulation, cells were washed twice with phosphate-buffered saline and incubated with human FVIIa and FX at 37°C, resulting in the formation of a TF/FVIIa complex at the cell surface. The TF/FVIIa complex converted human FX to FXa, which was subsequently measured by its ability to cleave a chromogenic substrate.…”

Section: Tf Surface Activitymentioning

confidence: 99%

Rapamycin, but Not FK-506, Increases Endothelial Tissue Factor Expression

et al. 2005

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Background-Drugs released from stents affect the biology of vascular cells. We examined the effect of rapamycin and FK-506 on tissue factor (TF) expression in human aortic endothelial cells (HAECs) and vascular smooth muscle cells (HAVSMCs). Methods and Results-Rapamycin enhanced thrombin-and tumor necrosis factor (TNF)-␣-induced endothelial TF expression in a concentration-dependent manner. The maximal increase was 2.5-fold more pronounced than that by thrombin or TNF-␣ alone and was paralleled by a 1.4-fold higher TF surface activity compared with thrombin alone. Rapamycin by itself increased basal TF levels by 40%. In HAVSMCs, rapamycin did not affect thrombin-or TNF-␣-induced TF expression. In contrast to rapamycin, FK-506 did not enhance thrombin-or TNF-␣-induced endothelial TF expression. Thrombin induced a transient dephosphorylation of the mammalian target of rapamycin downstream target p70S6 kinase. Rapamycin completely abrogated p70S6 kinase phosphorylation, but FK-506 did not. FK-506 antagonized the effect of rapamycin on thrombin-induced TF expression. Rapamycin did not alter the pattern of p38, extracellular signal-regulated kinase, or c-Jun NH 2 -terminal kinase phosphorylation. Real-time polymerase chain reaction analysis revealed that rapamycin had no influence on thrombin-induced TF mRNA levels for up to 2 hours but led to an additional increase after 3 and 5 hours.

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Lysophosphatidic Acid Induction of Tissue Factor Expression in Aortic Smooth Muscle Cells

Cited by 47 publications

References 56 publications

Histamine Induces Tissue Factor Expression

Histamine Induces Tissue Factor Expression

Cardiac Glycosides Regulate Endothelial Tissue Factor Expression in Culture

Rapamycin, but Not FK-506, Increases Endothelial Tissue Factor Expression

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