N-glycan structures and associated gene expression reflect the characteristic N-glycosylation pattern of human hematopoietic stem and progenitor cells

被引:48
作者
Hemmoranta, Heidi
Satomaa, Tero
Blomqvist, Maria
Heiskanen, Annamari
Aitio, Ollio
Saarinen, Juhani
Natunen, Jari
Partanen, Jukka
Laine, Jarmo
Jaatinen, Taina
机构
[1] Finnish Red Cross Blood Serv, Res & Dev, Helsinki 00310, Finland
[2] Glykos Finland Ltd, Helsinki, Finland
[3] Univ Helsinki, Inst Biotechnol, Program Struct Biol & Biophys, Helsinki, Finland
关键词
D O I
10.1016/j.exphem.2007.05.006
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
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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页码:1279 / 1292
页数:14
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