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pubmed-article:12468595pubmed:abstractTextVitamin B-6 inhibits platelet aggregation. However, the effect of the occupancy of GPIIb/IIIa, a major receptor responsible for aggregation on platelet membranes, by B-6 vitamers on platelet aggregation is unknown. This study was carried out to quantify GPIIb/IIIa occupancy in platelets treated with B-6 vitamers [pyridoxal-5-phosphate (PLP); pyridoxal (PL); pyridoxine (PN); pyridoxamine (PM)], using a monoclonal antibody-based assay, by flow cytometry. Antibody binding was compared with inhibition of platelet aggregation. PLP, PL, PN and PM occupied GPIIb/IIIa with dissociation constants of 1.83 +/- 1.15, 19.43 +/- 7.86, 3.63 +/- 1.67 and 10.89 +/- 2.93 mmol/L, respectively. Occupancy of GPIIb/IIIa by the four B-6 vitamers was negatively correlated with platelet aggregation (r = -0.90 to -0.94, P < 0.001). The concentrations of the four B-6 vitamers that inhibited maximal platelet aggregation were in the order of PLP < PN <PM < PL, the same order in which they occupied > or =80% of the GPII/IIIa receptor. Platelet aggregation was inhibited by B-6 vitamers via the occupancy of GPIIb/IIIa with the potency of PLP > PN > PM > PL.lld:pubmed
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pubmed-article:12468595pubmed:authorpubmed-author:ChangS-JSJlld:pubmed
pubmed-article:12468595pubmed:authorpubmed-author:ChangC-NCNlld:pubmed
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pubmed-article:12468595pubmed:volume132lld:pubmed
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pubmed-article:12468595pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:12468595pubmed:year2002lld:pubmed
pubmed-article:12468595pubmed:articleTitleOccupancy of glycoprotein IIb/IIIa by B-6 vitamers inhibits human platelet aggregation.lld:pubmed
pubmed-article:12468595pubmed:affiliationDepartment of Biology, National Cheng Kung University, Tainan, Taiwan. sjchang@mail.ncku.edu.twlld:pubmed
pubmed-article:12468595pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12468595pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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