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Glycosylation Restores Survival of Chilled Blood Platelets
Ist Teil von
Science (American Association for the Advancement of Science), 2003-09, Vol.301 (5639), p.1531-1534
Ort / Verlag
Washington, DC: American Association for the Advancement of Science
Erscheinungsjahr
2003
Quelle
American Association for the Advancement of Science
Beschreibungen/Notizen
Cooling of blood platelets clusters the von Willebrand factor receptor complex. Macrophage$\alpha_M\beta_2$integrins bind to the$GPIb\alpha$subunit of the clustered complex, resulting in rapid clearance of transfused, cooled platelets. This precludes refrigeration of platelets for transfusion, but the current practice of room temperature storage has major drawbacks. We document that$\alpha_M\beta_2$is a lectin that recognizes exposed$\beta-N-acetylglucosamine$residues of N-linked glycans on$GPIb\alpha$. Enzymatic galactosylation of chilled platelets blocks$\alpha_M\beta_2$recognition, prolonging the circulation of functional cooled platelets. Platelet-associated galactosyltransferase produces efficient galactosylation when uridine phosphate-galactose is added, affording a potentially simple method for storing platelets in the cold.