Annexin A2 binds to endosomes following organelle destabilization by particulate wear debris

Brian Scharf, Cristina C. Clement, Xiao-Xuan Wu, Kateryna Morozova, Diego Zanolini, Antonia Follenzi, Jorge N. Larocca, Kalle Levon, Fayyaz S. Sutterwala, Jacob Rand, Neil Cobelli, Ed Purdue, Katherine A. Hajjar and Laura Santambrogio ()
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Brian Scharf: Albert Einstein College of Medicine
Cristina C. Clement: Albert Einstein College of Medicine
Xiao-Xuan Wu: Montefiore Medical Center
Kateryna Morozova: Albert Einstein College of Medicine
Diego Zanolini: Albert Einstein College of Medicine
Antonia Follenzi: Albert Einstein College of Medicine
Jorge N. Larocca: Albert Einstein College of Medicine
Kalle Levon: NYU-Poly
Fayyaz S. Sutterwala: University of Iowa
Jacob Rand: Albert Einstein College of Medicine
Neil Cobelli: Montefiore Medical Center
Ed Purdue: Hospital for Special Surgery
Katherine A. Hajjar: Weill Cornell Medical College
Laura Santambrogio: Albert Einstein College of Medicine

Nature Communications, 2012, vol. 3, issue 1, 1-10

Abstract: Abstract Endosomal functions are contingent on the integrity of the organelle-limiting membrane, whose disruption induces inflammation and cell death. Here we show that phagocytosis of ultrahigh molecular weight polyethylene particles induces damage to the endosomal-limiting membrane and results in the leakage of cathepsins into the cytosol and NLRP3-inflammasome activation. Annexin A2 recruitment to damaged organelles is shown by two-dimensional DIGE protein profiling, endosomal fractionation, confocal analysis of endogenous and annexin A2–GFP transfected cells, and immunogold labelling. Binding experiments, using fluorescent liposomes, confirms annexin A2 recruitment to endosomes containing phagocytosed polyethylene particles. Finally, an increase in cytosolic cathepsins, NLRP3-inflammasome activation, and IL-1 production is seen in dendritic cells from annexin A2-null mice, following exposure to polyethylene particles. Together, the results indicate a functional role of annexin A2 binding to endosomal membranes following organelle destabilization.

Date: 2012
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DOI: 10.1038/ncomms1754

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