Glycosylation restores survival of chilled blood platelets.
作者： Karin M Hoffmeister , Emma C Josefsson , Natasha A Isaac , Henrik Clausen , John H Hartwig
关键词: Von Willebrand factor 、 Platelet 、 Uridine 、 Biology 、 Integrin 、 Galactosyltransferase 、 Platelet membrane glycoprotein 、 Glycosylation 、 Receptor complex 、 Biochemistry
摘要: Cooling of blood platelets clusters the von Willebrand factor receptor complex. Macrophage alphaMbeta2 integrins bind to GPIbalpha subunit clustered complex, resulting in rapid clearance transfused, cooled platelets. This precludes refrigeration for transfusion, but current practice room temperature storage has major drawbacks. We document that is a lectin recognizes exposed beta-N-acetylglucosamine residues N-linked glycans on GPIbalpha. Enzymatic galactosylation chilled blocks recognition, prolonging circulation functional Platelet-associated galactosyltransferase produces efficient when uridine diphosphate-galactose added, affording potentially simple method storing cold.
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