Red blood cell microparticles show altered inflammatory chemokine binding and release ligand upon interaction with

Zeyu Xiong1, John Cavaretta, Lirong Qu

  • 1Division of Pulmonary, Allergy, and Critical Care Medicine, Department of Medicine, Vascular Medicine Institute, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.

Transfusion
|August 27, 2010
PubMed
Abstract

Insights

Red blood cell microparticles released during storage exhibit altered Duffy antigen binding, impacting inflammatory chemokine interactions. This suggests a significant, underestimated microparticle burden in transfusions that affects platelet activation.

Area of Science:

  • Hematology
  • Immunology
  • Biochemistry

Background:

  • Red blood cell (RBC) storage leads to microparticle formation, which express the Duffy antigen.
  • The functional chemokine binding properties of these storage-induced microparticles are not well understood.

Purpose of the Study:

  • To investigate the inflammatory chemokine binding capacity of RBC microparticles.
  • To compare microparticle chemokine binding to intact RBCs.
  • To assess microparticle interactions with activated platelets (PLTs).

Main Methods:

  • Determined Duffy antigen-mediated chemokine binding of microparticles and intact RBCs.
  • Assessed microparticle interactions with PLTs.
  • Quantified microparticles based on glycophorin A expression and size.

Main Results:

  • Microparticles showed impaired Duffy-dependent chemokine binding affinity compared to intact RBCs.
  • Increased microparticle counts and surface phosphatidylserine were observed with storage.
  • Altered microparticle binding affinity promoted ligand release upon PLT incubation, suggesting increased chemokine bioavailability.
  • Standard quantification methods underestimated the functional chemokine binding capacity of microparticles.

Conclusions:

  • The microparticle burden in transfusates, assessed by functional chemokine binding, is substantial.
  • Altered membrane properties of RBC microparticles enhance PLT interactions, increasing inflammatory chemokine bioavailability in vitro.