期刊
NATURE MEDICINE
卷 15, 期 11, 页码 1273-U68出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nm.2030
关键词
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资金
- US National Institutes of Health [PO1 HL056949, HL089224]
- The Pew Scholars Award
- Howard Hughes Medical Institute
- The Swedish Medical Research Council
- Goteborg University Jubileums
- ZymeQuest, Inc
- [PO1HL57345]
Rapid chilling causes glycoprotein-Ib (GPIb) receptors to cluster on blood platelets. Hepatic macrophage beta(2) integrin binding to beta-N-acetylglucosamine (beta-GlcNAc) residues in the clusters leads to rapid clearance of acutely chilled platelets after transfusion. Although capping the beta-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 beta(2) integrin and Ashwell-Morell receptors may afford a potentially simple method for storing platelets in the cold.
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