Preserved functional and biochemical characteristics of platelet components prepared with amotosalen and ultraviolet A for pathogen inactivation

Authors

  • Béatrice Hechler,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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    • BH and PO contributed equally to this study.
  • Philippe Ohlmann,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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    • BH and PO contributed equally to this study.
  • Philippe Chafey,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Catherine Ravanat,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Anita Eckly,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Eric Maurer,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Pierre Mangin,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Hervé Isola,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Jean-Pierre Cazenave,

    1. INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
    2. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
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  • Christian Gachet

    Corresponding author
    1. INSERM, U1016; CNRS UMR8104, Plateforme Protéomique Institut Cochin, Paris Descartes University, Paris, France
    • INSERM, UMR_S949, Université de Strasbourg, Etablissement Français du Sang-Alsace (EFS-Alsace), Strasbourg, France
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  • This work was supported by INSERM, EFS, and ARMESA (Association de Recherche et Développement en Médecine et Santé Publique). BH is the recipient of a "contrat d'interface" between the EFS and INSERM.

Address reprint requests to: Christian Gachet, MD, PhD, UMR_S949 INSERM, Université de Strasbourg, Etablissement Français du Sang-Alsace, 10 rue Spielmann, BP 36, F-67065 Strasbourg Cedex, France; e-mail: christian.gachet@efs-alsace.fr.

Abstract

Background

Platelet concentrate (PC) functionality decreases during storage. This is referred to as the storage lesion. Pathogen inactivation may accelerate or induce lesions, potentially accounting for reduced viability. Our aim was to characterize functional and biochemical properties of platelets (PLTs) from photochemically treated buffy-coat PCs (PCT-PCs) compared to those from conventional PCs.

Study Design and Methods

Four PCT-PCs and four conventional PCs were stored for 6.5 days and PLT function and proteomic profiles were examined at various time points during storage. To evaluate their intrinsic properties, samples of stored PLTs were taken, washed, and suspended in Tyrode's buffer before testing.

Results

PLT counts and morphology were conserved although a slight increase in the PLT volume was observed after PCT. Glycoprotein (GP) IIbIIIa, IaIIa, and VI expression remained stable while GPIbα declined similarly in both types of PCs. A steep decrease (50%) in GPV occurred on Day 1.5 in PCT-PCs and Day 2.5 in control PCs. For both PCT- and control PCs, P-selectin expression and activated GPIIbIIIa remained low during storage. PCT- and control PCs were fully responsive to aggregation agonists up to Day 4.5 and exhibited similar perfusion functionality. Mitochondrial membrane potential and annexin A5 binding of PCT-PCs and control PCs were comparable. Two-dimensional differential in-gel electrophoresis and mass spectrometry profiles for 1882 protein spots revealed only three proteins selectively changed in PCT-PCs compared to control-PCs.

Conclusion

Washed treated and untreated PCs have similar functional, morphologic, and proteomic characteristics provided that PLTs are suspended in an appropriate medium during testing.

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