All-trans retinoic acid is partially effective against lipopolysaccharide-induced but not against tissue-factor-induced disseminated intravascular coagulation in rat models

Asakura, Hitoshi; Aoshima, Keiji; Ichino, Tsukasa; Suga, Yukio; Saitô, Masanori; Morishita, Eriko; Yamazaki, Masahide; Ontachi, Yasuo; Mizutani, Tomoe; Kato, Minori; Ki, Miyamoto; Nakao, Shinji

doi:10.1097/00001721-200106000-00011

Cited by 8 publications

(2 citation statements)

References 24 publications

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“…Our results are in agreement with a previous study demonstrating that retinoic acid repressed LPS-induced expression of tumor necrosis factor-α and inducible nitric oxide synthase in cultured rat microglia cells [18] through inhibition of NF-κB activation. Other studies have shown that retinoic acid represses the cellular and physiologic effects of LPS [18,28,[33][34][35].…”

Section: Discussionmentioning

confidence: 99%

Retinoic acid dampens LPS-induced NF-κB activity: results from human monoblasts and in vivo imaging of NF-κB reporter mice

Austenaa

Carlsen

Hollung

et al. 2009

The Journal of Nutritional Biochemistry

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Section: Discussionmentioning

confidence: 99%

Retinoic acid dampens LPS-induced NF-κB activity: results from human monoblasts and in vivo imaging of NF-κB reporter mice

Austenaa

Carlsen

Hollung

et al. 2009

The Journal of Nutritional Biochemistry

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“…The absorbance was read at 405 nm and the PI activity was calculated by comparison with the standard serum [11] . The PIC and D-dimer, which is the stable end product of fi brin degradation by plasmin, were determined using a Latex Agglutination Kit (International Reagents Co., Kobe, Japan) [20,21] . The activity of PAI was determined using its substrate H-D -isoleucyl-prolyl-arginine-p -nitroaniline dihydrochloride (Chromogenix Co.) (S-2288), which releases p -nitroaniline cleaved by t-PA [22] .…”

Section: Fibrinolysis Parameters Assaymentioning

confidence: 99%

Fish Protein Stimulated the Fibrinolysis in Rats

Murata

Sano²,

Bannai³

et al. 2004

Ann Nutr Metab

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Objective: We hypothesized that fish protein affects blood coagulation and/or fibrinolysis, and compared the activity and amounts of factors involved in blood coagulation and fibrinolysis in rats fed the fish protein, which was treated to remove water-soluble and ethanol-soluble elements, from sardine (sardine protein). Methods: In the first experiment, rats were fed for 21 days an AIN-93G-based control diet, and diets in which the casein of the control diet was exchanged for sardine protein at 5, 10 and 20% levels. In the second experiment, rats were fed an AIN-93G control diet and diets containing 5% fish oil, 10% sardine protein or both (5% fish oil + 10% sardine protein) for 21 days. At the end of the experiments, blood coagulation time, hemostatic parameters and fibrinolysis parameters were measured. Results: The activated partial thromboplastin time (APTT), which is an assay for blood coagulation time in the intrinsic blood coagulation pathway, of rats fed the 20% sardine protein diet was significantly prolonged compared to that of rats fed the control diet. The prolonged APTT by dietary sardine protein was due to a significant decrease of the activities of plasma blood coagulation factors VIII, IX, XI and XII. On the other hand, dietary sardine protein significantly increased the activity of tissue-type plasminogen activator, and the amount of plasma plasmin–α₂-plasmin inhibitor complex, which are markers of activated plasmin. Moreover, we observed that the 20% sardine protein diet increased the amount of plasma D-dimer, which is a degraded product of the fibrin polymer by plasmin. In the second experiment, the APTT and PT of rats fed the F diet were prolonged compared to those of rats fed the control diet, however the concentration and amount of fibrinolytic parameters in the plasma were almost the same as those of rats fed the control diet. In contrast, the F+S diet not only prolonged APTT and PT, but also increased the concentration and amount of fibrinolytic parameters in plasma. Conclusions: We consider that the beneficial effects to health and amelioration of cardiovascular and cerebrovascular diseases by fish consumption are caused by a combination of the suppressing effect on blood coagulation of n–3 polyunsaturated fatty acids and the promoting effect on fibrinolysis of fish protein.

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Acute promyelocytic leukemia cell adhesion to vascular endothelium is reduced by heparins

2018

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Adhesion of acute promyelocytic leukemia (APL) cells to endothelial cells (EC) is among the mechanisms of the APL-associated coagulopathy, responsible for early hemorrhagic deaths in affected patients. We compared the effects of dalteparin and enoxaparin, two low-molecular-weight heparins (LMWH), and unfractionated heparin (UFH), on APL NB4 adhesion to micro- (HMEC-1) and macro-vascular EC (HUVEC), in resting and interleukin-1β (IL-1β)-stimulated conditions. The heparin effect on EC adhesion molecule (ICAM-1, VCAM-1, E-selectin) expression was also assessed. In HMEC-1, dalteparin inhibited IL1β-induced NB4 adhesion by 80%, enoxaparin by 52%, and UFH by 44%. Similar results were obtained in HUVEC. This was associated with a significant decrease of VCAM-1 and ICAM-1 expression. In conclusion, we show that LMWH significantly counteract APL cell adhesion to the vessel wall, by modulating EC adhesion molecule expression. This property of heparins may represent one approach for hampering excess clotting activation and microthrombi deposition in APL.

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All-trans retinoic acid is partially effective against lipopolysaccharide-induced but not against tissue-factor-induced disseminated intravascular coagulation in rat models

Cited by 8 publications

References 24 publications

Retinoic acid dampens LPS-induced NF-κB activity: results from human monoblasts and in vivo imaging of NF-κB reporter mice

Retinoic acid dampens LPS-induced NF-κB activity: results from human monoblasts and in vivo imaging of NF-κB reporter mice

Fish Protein Stimulated the Fibrinolysis in Rats

Acute promyelocytic leukemia cell adhesion to vascular endothelium is reduced by heparins

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