The role of adenosine diphosphate mediated platelet responsiveness for the stability of platelet integrity in citrated whole blood under ex vivo conditions

PLoS One. 2017 Nov 20;12(11):e0188193. doi: 10.1371/journal.pone.0188193. eCollection 2017.

Abstract

Background: Platelets are important for effective hemostasis and considered to be involved in pathophysiological processes, e.g. in cardiovascular diseases. Platelets provided for research or for therapeutic use are frequently separated from citrated whole blood (WB) stored for different periods of time. Although functionally intact platelets are required, the stability of platelet integrity, e.g. adenosine diphosphate (ADP) mediated responsiveness, has never been thoroughly investigated in citrated WB under ex vivo conditions.

Objectives: Platelet integrity was evaluated at different time points in citrated WB units, collected from healthy donors and stored for 5 days at ambient temperature. The analysis included the measurement of activation markers, of induced light transmission aggregometry and of purinergic receptor expression or function. Inhibitory pathways were explored by determination of basal vasodilator-stimulated phosphoprotein (VASP)-phosphorylation, intracellular cyclic nucleotide levels and the content of phosphodiesterase 5A. Fresh peripheral blood (PB) samples served as controls.

Results: On day 5 of storage, thrombin receptor activating peptide-6 (TRAP-6) stimulated CD62P expression and fibrinogen binding were comparable to PB samples. ADP induced aggregation continuously decreased during storage. Purinergic receptor expression remained unchanged, whereas the P2Y1 activity progressively declined in contrast to preserved P2Y12 and P2X1 function. Inhibitory pathways were unaffected except for a slight elevation of VASP phosphorylation at Ser239 on day 5.

Conclusion: After 5 days of storage in citrated WB, platelet responsiveness to TRAP-6 is sufficiently maintained. However, ADP-mediated platelet integrity is more sensitive to deterioration, especially after storage for more than 2 days. Decreasing ADP-induced aggregation is particularly caused by the impairment of the purinergic receptor P2Y1 activity. These characteristics should be considered in the use of platelets from stored citrated WB for experimental or therapeutic issues.

MeSH terms

  • Adenosine Diphosphate / pharmacology*
  • Adult
  • Blood Platelets / cytology
  • Blood Platelets / drug effects*
  • Blood Platelets / metabolism
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism
  • Cell Survival / genetics
  • Citric Acid / pharmacology*
  • Cyclic AMP / metabolism
  • Cyclic GMP / metabolism
  • Cyclic Nucleotide Phosphodiesterases, Type 5 / genetics
  • Cyclic Nucleotide Phosphodiesterases, Type 5 / metabolism
  • Female
  • Fibrinogen / metabolism
  • Gene Expression Regulation
  • Humans
  • Male
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • P-Selectin / genetics
  • P-Selectin / metabolism
  • Peptide Fragments / pharmacology
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism
  • Phosphorylation / drug effects
  • Platelet Activation / drug effects
  • Platelet Aggregation / drug effects
  • Platelet Aggregation Inhibitors / pharmacology*
  • Primary Cell Culture
  • Protein Binding / drug effects
  • Receptors, Purinergic P2X1 / genetics
  • Receptors, Purinergic P2X1 / metabolism
  • Receptors, Purinergic P2Y1 / genetics*
  • Receptors, Purinergic P2Y1 / metabolism
  • Receptors, Purinergic P2Y12 / genetics
  • Receptors, Purinergic P2Y12 / metabolism

Substances

  • Cell Adhesion Molecules
  • Microfilament Proteins
  • P-Selectin
  • Peptide Fragments
  • Phosphoproteins
  • Platelet Aggregation Inhibitors
  • Receptors, Purinergic P2X1
  • Receptors, Purinergic P2Y1
  • Receptors, Purinergic P2Y12
  • SELP protein, human
  • thrombin receptor peptide (42-47)
  • vasodilator-stimulated phosphoprotein
  • Citric Acid
  • Adenosine Diphosphate
  • Fibrinogen
  • Cyclic AMP
  • Cyclic Nucleotide Phosphodiesterases, Type 5
  • Cyclic GMP

Grants and funding

This publication was funded by the German Research Foundation (DFG) and the University of Wuerzburg in the funding programme Open Access Publishing. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.