Endothelin-B-Receptors-Dependent-Inhibition of Platelet Aggregation in the CD-1 Mouse

2000 ◽  
Vol 36 (Supplement 1) ◽  
pp. S184-S186 ◽  
Author(s):  
Julie Labonté ◽  
Ghassan Bkaily ◽  
Pedro DʼOrléans-Juste
Keyword(s):  
Platelet Aggregation ◽  
Inhibition Of Platelet Aggregation ◽  
Dependent Inhibition ◽  
Endothelin B

scholarly journals Endothelium-dependent inhibition of platelet aggregation

1986 ◽  
Vol 88 (2) ◽  
pp. 411-415 ◽  
Author(s):  
Hiroshi Azuma ◽  
Masayuki Ishikawa ◽  
Satomi Sekizaki
Keyword(s):  
Platelet Aggregation ◽  
Inhibition Of Platelet Aggregation ◽  
Dependent Inhibition

scholarly journals Anti-Platelet Aggregation and Anti-Cyclooxygenase Activities for a Range of Coffee Extracts (Coffea arabica)

Molecules ◽  
2020 ◽  
Vol 26 (1) ◽  
pp. 10
Author(s):  
Nuntouchaporn Hutachok ◽  
Pongsak Angkasith ◽  
Chaiwat Chumpun ◽  
Suthat Fucharoen ◽  
Ian J. Mackie ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Biological Activities ◽  
Total Phenolic ◽  
Inhibitory Effects ◽  
Phenolic Contents ◽  
Inhibition Of Platelet Aggregation ◽  
Dependent Inhibition ◽  
Cox 2 ◽  
Activation Pathways ◽  
Cox 1

Coffee is rich in caffeine (CF), chlorogenic acid (CGA) and phenolics. Differing types of coffee beverages and brewing procedures may result in differences in total phenolic contents (TPC) and biological activities. Inflammation and increases of platelet activation and aggregation can lead to thrombosis. We focused on determining the chemical composition, antioxidant activity and inhibitory effects on agonist-induced platelet aggregation and cyclooxygenase (COX) of coffee beverages in relation to their preparation method. We prepared instant coffee and brewed coffee beverages using drip, espresso, and boiling techniques. Coffee extracts were assayed for their CF and CGA contents using HPLC, TPC using colorimetry, platelet aggregation with an aggregometer, and COX activity using ELISA. The findings have shown all coffee extracts, except the decaffeinated types, contained nearly equal amounts of CF, CGA, and TPC. Inhibitory effects of coffee extracts on platelet aggregation differed depending on the activation pathways induced by different agonists. All espresso, drip and boiled coffee extracts caused dose dependent inhibition of platelet aggregation induced by ADP, collagen, epinephrine, and arachidonic acid (ARA). The most marked inhibition was seen at low doses of collagen or ARA. Espresso and drip extracts inhibited collagen-induced platelet aggregation more than purified caffeine or CGA. Espresso, boiled and drip coffee extracts were also a more potent inhibitors of COX-1 and COX-2 than purified caffeine or CGA. We conclude that inhibition of platelet aggregation and COX-1 and COX-2 may contribute to anti-platelet and anti-inflammatory effects of espresso and drip coffee extracts.

scholarly journals Anti-Platelet Aggregation and Anti-Cyclooxygenase Activities for a Range of Coffee Extracts (Coffea arabica)

2020 ◽  
Author(s):  
Nuntouchporn Hutachok ◽  
Pongsak Angkasith ◽  
Chaiwat Chumpun ◽  
Suthat Fucharoen ◽  
Ian Mackie ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Biological Activities ◽  
Total Phenolic ◽  
Inhibitory Effects ◽  
Phenolic Contents ◽  
Inhibition Of Platelet Aggregation ◽  
Dependent Inhibition ◽  
Cox 2 ◽  
Activation Pathways ◽  
Cox 1

Coffee is rich in caffeine (CF), chlorogenic acid (CGA) and phenolics. Differing types of coffee beverages and brewing procedures may result in differences in total phenolic contents (TPC) and biological activities. Inflammation and increases of platelet activation and aggregation can lead to thrombosis. We focused on determining the chemical composition, antioxidant activity and inhibitory effects on agonist-induced platelet aggregation and cyclooxygenase (COX) of coffee beverages in relation to their preparation method. We prepared instant coffee and brewed coffee beverages using drip, espresso and boiling techniques. Coffee extracts were assayed for their CF and CGA contents using HPLC, TPC using colourimetry, platelet aggregation with an aggregometer and COX activity using ELISA. The findings have shown all coffee extracts, except the decaffeinated types, contained nearly equal amounts of CF, CGA and TPC. Inhibitory effects of coffee extracts on platelet aggregation differed depending on the activation pathways induced by different agonists. All espresso, drip and boiled coffee extracts caused dose dependent inhibition of platelet aggregation induced by ADP, collagen, epinephrine, and arachidonic acid (ARA). The most marked inhibition was seen at low doses of collagen or ARA. Espresso and drip extracts inhibited collagen-induced platelet aggregation more than purified caffeine or CGA. Espresso, boiled and drip coffee extracts were also a more potent inhibitors of COX-1 and COX-2 than purified caffeine or CGA. We conclude that inhibition of platelet aggregation and COX-1 and COX-2 may contribute to anti-platelet and anti-inflammatory effects of espresso and drip coffee extracts.

Species-Dependent Inhibition of Platelet Aggregation by Adenosine and Dipyridamole: Paradoxical Potentiation in the Rat

1970 ◽  
Vol 23 (01) ◽  
pp. 129-139 ◽  
Author(s):  
R. B Philp ◽  
B Bishop ◽  
Keyword(s):  
Platelet Aggregation ◽  
Guinea Pig ◽  
Adenosine Receptors ◽  
Guinea Pigs ◽  
Human Subjects ◽  
Adenosine Diphosphate ◽  
Inhibition Of Platelet Aggregation ◽  
Rabbit Platelets ◽  
Dependent Inhibition ◽  
Rat Platelets

SummaryPlatelets of cats, rabbits, guinea pigs, rats and human subjects were aggregated with adenosine diphosphate after having been in contact with adenosine or dipyridamole for 5 to 60 min. The species profiles of both agents were the same. Both inhibited aggregation of human and rabbit platelets and the degree of inhibition increased with the time of contact. Neither inhibited aggregation of cat or guinea-pig platelets and both potentiated the rate and extent of aggregation of rat platelets: the degree of potentiation increased with the time of contact. Some reports on the related effects of adenosine and dipyridamole are reviewed and it is suggested that the effects of dipyridamole might be due to an affinity for adenosine receptors.

Effects of Acetylsalicylic Acid on Inhibition of Ex Vivo Platelet Aggregation and Secretion by SKF 107260, a Novel GPIIb/IIIa Receptor Antagonist

1994 ◽  
Vol 72 (04) ◽  
pp. 622-626 ◽  
Author(s):  
Martin I Freed ◽  
Steven Boike ◽  
Nevine Zariffa ◽  
Diane K Jorkasky
Keyword(s):  
Platelet Aggregation ◽  
Acetylsalicylic Acid ◽  
Whole Blood ◽  
Ex Vivo ◽  
Atp Release ◽  
Blood Platelet ◽  
Inhibition Of Platelet Aggregation ◽  
Dependent Inhibition ◽  
Platelet Secretion

SummarySKF 107260 is a potent pentapeptide antagonist of the platelet membrane glycoprotein receptor GP IIb/IIIa. The in vitro platelet inhibitory effects of SKF 107260, acetylsalicylic acid (ASA), and their combination, on collagen-induced platelet aggregation and secretion (ATP release) were assessed in human whole blood. Additionally, the con-centration-response relationships for these inhibitors were compared for males and females in order to explore gender differences in platelet responsiveness. SKF 107260 caused a concentration-dependent inhibition of platelet aggregation which was significant at concentrations ≥30 nM. ASA also caused a concentration-dependent inhibition of platelet aggregation which was significant at concentrations ≥ 1 mg/dl. The addition of ASA 1 mg/dl to increasing concentrations of SKF 107260 resulted in a more pronounced inhibition of platelet aggregation than when either agent was used alone. These data suggest a pharmacologic interaction, especially at SKF 107260 concentrations ≤30 nM. Since ATP release was significantly inhibited at concentrations ≥ 1 nM, platelet secretion appears to be more sensitive than aggregation to inhibition by SKF 107260. These data suggest that platelet secretion in response to collagen is dependent on the aggregation response mediated by GP IIb/IIIa. In conclusion, SKF 107260 is a potent inhibitor of both whole blood platelet aggregation and secretion and these anti-aggregatory effects may be augmented by concomitant ASA administration.

Time-dependent inhibition of platelet aggregation by dopamine and 3-methoxytyramine

1984 ◽  
Vol 33 (3) ◽  
pp. 435-441 ◽  
Author(s):  
Haruyoshi Kodaira ◽  
Masayuki Ishikawa ◽  
Yasuo Komoda ◽  
Terumi Nakajima
Keyword(s):  
Platelet Aggregation ◽  
Time Dependent ◽  
Inhibition Of Platelet Aggregation ◽  
Dependent Inhibition ◽  
Time Dependent Inhibition

scholarly journals IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation

Blood ◽  
2006 ◽  
Vol 109 (2) ◽  
pp. 552-559 ◽  
Author(s):  
Melanie Antl ◽  
Marie-Luise von Brühl ◽  
Christina Eiglsperger ◽  
Matthias Werner ◽  
Ildiko Konrad ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Platelet Activation ◽  
Arterial Thrombosis ◽  
Receptor Activation ◽  
Type I ◽  
Inhibition Of Platelet Aggregation ◽  
Regulatory Cascade ◽  
Inositol 1,4,5 Trisphosphate ◽  
Dependent Inhibition ◽  
Trisphosphate Receptor

Abstract Defective regulation of platelet activation/aggregation is a predominant cause for arterial thrombosis, the major complication of atherosclerosis triggering myocardial infarction and stroke. A central regulatory pathway conveying inhibition of platelet activation/aggregation is nitric oxide (NO)/cyclic GMP (cGMP) signaling by cGMP-dependent protein kinase I (cGKI). However, the regulatory cascade downstream of cGKI mediating platelet inhibition is still unclear. Here, we show that the inositol-1,4,5-trisphosphate receptor–associated cGMP kinase substrate (IRAG) is abundantly expressed in platelets and assembled in a macrocomplex together with cGKIβ and the inositol-1,4,5-trisphosphate receptor type I (InsP3RI). cGKI phosphorylates IRAG at Ser664 and Ser677 in intact platelets. Targeted deletion of the IRAG-InsP3RI interaction in IRAGΔ12/Δ12 mutant mice leads to a loss of NO/cGMP-dependent inhibition of fibrinogen-receptor activation and platelet aggregation. Intracellular calcium transients were not affected by DEA/NO or cGMP in mutant platelets. Furthermore, intravital microscopy shows that NO fails to prevent arterial thrombosis of the injured carotid artery in IRAGΔ12/Δ12 mutants. These findings reveal that interaction between IRAG and InsP3RI has a central role in NO/cGMP-dependent inhibition of platelet aggregation and in vivo thrombosis.

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