Platelet aggregation was induced by collagen or ADP and epinephrine. Integrin αIIbβ3-fibrinogen binding was evaluated on prostaglandins E1 (PGE1)-treated washed platelets or baby hamster kidney (BHK) cells expressing human αIIbβ3. Integrin was directly activated by an anti-ligand induced binding site (LIBS) PT25-2 antibody. The effect of sulfhydryl-reactive agents, such as allicin, glutathione, dithiobis nitrobenzoic acid (DTNB) and disulfiram, was tested on αIIbβ3 activity.
Allicin (40 µM) completely inhibited washed platelets agonist-induced aggregation. Both allicin and disulfiram (40 µM) inhibited αIIbβ3-fibrinogen binding and P-selectin expression in washed platelets. However, there was an increase in αIIbβ3-fibrinogen binding but not P-selectin expression in PGE1-treated washed platelets activated by PT25-2 antibody. At a high concentration (400 µM) both inhibited αIIbβ3-fibrinogen binding. Similarly, in BHK cells expressing αIIbβ3 activated by PT25-2 antibody, allicin at a low concentration increased αIIbβ3 activity.
Allicin and disulfiram inhibit agonist-induced washed platelet activation probably via inhibition of platelet signaling, but enhance PT25-2 antibody-induced αIIbβ3 integrin activity most likely by preventing reformation of disulfide bridges thereby stabilizing the active conformation of the integrin.
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