Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane.

@article{Burgess2000PhysicalPA,
  title={Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane.},
  author={Jack K Burgess and Kylie A. Hotchkiss and Catherine Suter and Nicholas Peter Dudman and J{\'a}nos Sz{\"o}ll{\"o}si and Colin N. Chesterman and Beng Hock Chong and Philip J Hogg},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 13},
  pages={9758-66}
}
Platelet function is influenced by the platelet thiol-disulfide balance. Platelet activation resulted in 440% increase in surface protein thiol groups. Two proteins that presented free thiol(s) on the activated platelet surface were protein-disulfide isomerase (PDI) and glycoprotein 1balpha (GP1balpha). PDI contains two active site dithiols/disulfides. The active sites of 26% of the PDI on resting platelets was in the dithiol form, compared with 81% in the dithiol form on activated platelets… CONTINUE READING

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