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Nature Medicine 15, 1273–1280 (1 November 2009) | doi:10.1038/nm.2030

Dual roles for hepatic lectin receptors in the clearance of chilled platelets

Viktoria Rumjantseva , Prabhjit K Grewal , Hans H Wandall , Emma C Josefsson , Anne Louise S|[oslash]|rensen , G|[ouml]|ran Larson , Jamey D Marth , John H Hartwig & Karin M Hoffmeister

Rapid chilling causes glycoprotein-Ib (GPIb) receptors to cluster on blood platelets. Hepatic macrophage β2 integrin binding to β-N-acetylglucosamine (β-GlcNAc) residues in the clusters leads to rapid clearance of acutely chilled platelets after transfusion. Although capping the β-GlcNAc moieties by galactosylation prevents clearance of short-term–cooled platelets, this strategy is ineffective after prolonged refrigeration. We report here that prolonged refrigeration increased the density and concentration of exposed galactose residues on platelets such that hepatocytes, through Ashwell-Morell receptor binding, become increasingly involved in platelet removal. Macrophages rapidly removed a large fraction of transfused platelets independent of their storage conditions. With prolonged platelet chilling, hepatocyte-dependent clearance further diminishes platelet recovery and survival after transfusion. Inhibition of chilled platelet clearance by both β2 integrin and Ashwell-Morell receptors may afford a potentially simple method for storing platelets in the cold.