Equol is more active than soy isoflavone itself to compete for binding to thromboxane A2 receptor in human platelets
| Autor: | Luis Valladares, Argelia Garrido, Yenny Muñoz |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
medicine.medical_specialty
Platelet Aggregation Genistein Binding Competitive Receptors Thromboxane A2 Prostaglandin H2 Biochanin A chemistry.chemical_compound Thromboxane A2 Internal medicine medicine Humans Platelet activation Daidzein food and beverages Hematology Equol Isoflavones Bridged Bicyclo Compounds Heterocyclic Platelet Activation Hydrazines Endocrinology chemistry Fatty Acids Unsaturated Platelet aggregation inhibitor Calcium lipids (amino acids peptides and proteins) Platelet Aggregation Inhibitors circulatory and respiratory physiology |
| Zdroj: | THROMBOSIS RESEARCH Artículos CONICYT CONICYT Chile instacron:CONICYT |
| ISSN: | 0049-3848 |
| DOI: | 10.1016/j.thromres.2008.07.011 |
| Popis: | Introduction Several dietary intervention studies examining the health effect of soy isoflavones allude to the importance of equol in establishing the cardiovascular response to soy protein. Although, the specific mechanism by which this action occurs has not been established. The aim of this study was to investigate the inhibitory effect of soy-isoflavones and the metabolite of daidzein, equol, on agonist-induced platelet responses dependent on thromboxane A2 (TxA2) receptor. Material and methods Competitive radioligand binding assay was used to screen for affinity of these compounds to the TxA2 receptor. The effect of equol on platelet activation, evaluate through of release of the ATP, by analogs of TxA2 was analyzed. The effect of equol on platelet aggregation was investigated with ADP, U46619 (a TxA2 mimic) and the calcium ionophore A23187. Results The data showed that aglycone isoflavones and equol bind to TxA2 receptor in the µmol/L range, whereas their glucoside derivates had very low binding activity for this receptor. Under equilibrium conditions, the following order of the relative affinity in inhibiting [3H]-SQ29585 binding was: equol > genistein > daidzein > glycitein ≫ genistin, daidzin, glycitin. Equol interaction was reversible and competitive for labeled-SQ29548 with not apparent decrease in the number of TxA2 binding sites. In addition, from platelet activation studies, equol effectively inhibited ATP secretion elicited by the TxA2 analog U46619. On the other hand, equol inhibited the platelet aggregation induced by U46619 and A23187, while it failed to inhibit that induced by ADP. Conclusions The aglycone isoflavones from soy, and particularly equol, have been found to have biological effects attributable to thromboxane A2 receptor antagonism. These findings may help elucidate how dietary isoflavone modulate platelet function and explain why soy-rich foods are claimed to have beneficial effects in the prevention of thrombotic events. |
| Databáze: | OpenAIRE |
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