Journal
EXPERIMENTAL HEMATOLOGY
Volume 35, Issue 8, Pages 1279-1292Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.exphem.2007.05.006
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Objective. Cell surface glycans contribute to the adhesion capacity of cells and are essential in cellular signal transduction. Yet, the glycosylation of hematopoietic stem and progenitor cells (HSPC), such as CD133(+) cells, is poorly explored. Matetials and Methods. N-glycan structures of cord blood-derived CD133(+) and CD133(-) cells were analyzed with mass spectrometric profiling and exoglycosidase digestion, cell surface glycan epitopes with lectin binding assay, and expression of N-glycan biosynthesis-related genes with microarray analysis. Results. Over 10% difference was demonstrated in the N-glycan profiles of CD133(+) and CD133(-) cells. Biantennary complex-type N-glycans were enriched in CD133(+) cells. Of the genes regulating the synthesis of these structures, CD133(+) cells overexpressed MGAT2 and underexpressed MGAT4. Moreover, the amount of high-marmose type N-glycans and terminal oE2,3-sialylation was increased in CD133(+) cells. Elevated alpha 2,3-sialylation was supported by the overexpression of ST3GAL6. Conclusion. Our work presents new information on the characters of HSPCs. The new knowledge of HSPC-specific N-glycosylation advances their identification and provides tools to promote HSPC homing and mobilization or targeting to specific tissues. (c) 2007 ISEH - Society for Hematology and Stem Cells. Published by Elsevier Inc.
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