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Biochemical and Molecular Actions of Nutrients
Research Communication

Occupancy of Glycoprotein IIb/IIIa by B-6 Vitamers Inhibits Human Platelet Aggregation¹

Department of Biology, National Cheng Kung University, Tainan, Taiwan, 701 and ^* Department of Neurosurgery, Chang Gung University and Memorial Hospital, Taipei, Taiwan, 105

²To whom correspondence should be addressed. E-mail: sjchang{at}mail.ncku.edu.tw.

Vitamin 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 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.

KEY WORDS: • vitamin B-6 • GPIIb/IIIa • platelet aggregation

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