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Related Experiment Videos

Protein disulphide isomerase in platelet function.

Nagaraj Manickam1, Xiuhua Sun, Mengru Li

  • 1Division of Hematology, Department of Medicine, The University of Texas Health Science Center at San Antonio, San Antonio, TX, USA.

British Journal of Haematology
|November 22, 2007
PubMed
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Platelet protein disulphide isomerase (PDI) targets a non-P2Y(12) receptor on the platelet surface, likely the alphaIIbbeta3 integrin, influencing platelet aggregation. This study reveals a mechanism for surface PDI activation during platelet activation.

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Platelet protein disulphide isomerase (PDI) is implicated in platelet aggregation.
  • The P2Y(12) ADP receptor, a thiol-containing protein, is a known mediator of platelet aggregation.
  • The precise target of PDI in platelet aggregation remains to be fully elucidated.

Purpose of the Study:

  • To investigate the specific target of platelet PDI during platelet aggregation.
  • To determine if PDI targets the P2Y(12) receptor or another thiol-containing protein.
  • To explore the role of PDI in the activation of the alphaIIbbeta3 integrin.

Main Methods:

  • Utilized anti-PDI antibody RL90 to exclude the P2Y(12) pathway.
  • Investigated signaling-independent activation of the alphaIIbbeta3 integrin by Mn(2+).

Related Experiment Videos

  • Assessed surface expression of thiol-containing PDI upon platelet activation.
  • Compared the disulfide bond isomerization activity of purified PDI and alphaIIbbeta3 integrin.

    • Main Results:

    • PDI targets a non-P2Y(12) thiol-protein involved in platelet aggregation.
    • Anti-PDI antibody inhibited the activation of the alphaIIbbeta3 integrin, suggesting a direct interaction.
    • The active, thiol-containing form of PDI increases on the platelet surface during activation.
    • Purified PDI exhibits greater disulfide bond isomerization activity than alphaIIbbeta3 integrin.

    Conclusions:

    • Platelets possess a mechanism to enhance surface PDI activity.
    • This surface PDI likely targets the alphaIIbbeta3 integrin in a non-P2Y(12) dependent manner.
    • PDI plays a significant role in the redox regulation of alphaIIbbeta3 and platelet aggregation.