The N-glycome of human embryonic stem cells
<p>Abstract</p> <p>Background</p> <p>Complex carbohydrate structures, glycans, are essential components of glycoproteins, glycolipids, and proteoglycans. While individual glycan structures including the SSEA and Tra antigens are already used to define undifferentiated h...
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doaj-ecc08e773a214b6680aceb506226cd892020-11-24T21:23:12ZengBMCBMC Cell Biology1471-21212009-06-011014210.1186/1471-2121-10-42The N-glycome of human embryonic stem cellsOlonen AnneAitio OlliJaatinen TainaTiittanen MinnaBlomqvist MariaOlsson CiaMikkola MillaHeiskanen AnnamariSatomaa TeroHelin JariHiltunen JukkaNatunen JariTuuri TimoOtonkoski TimoSaarinen JuhaniLaine Jarmo<p>Abstract</p> <p>Background</p> <p>Complex carbohydrate structures, glycans, are essential components of glycoproteins, glycolipids, and proteoglycans. While individual glycan structures including the SSEA and Tra antigens are already used to define undifferentiated human embryonic stem cells (hESC), the whole spectrum of stem cell glycans has remained unknown. We undertook a global study of the asparagine-linked glycoprotein glycans (N-glycans) of hESC and their differentiated progeny using MALDI-TOF mass spectrometric and NMR spectroscopic profiling. Structural analyses were performed by specific glycosidase enzymes and mass spectrometric fragmentation analyses.</p> <p>Results</p> <p>The data demonstrated that hESC have a characteristic N-glycome which consists of both a constant part and a variable part that changes during hESC differentiation. hESC-associated N-glycans were downregulated and new structures emerged in the differentiated cells. Previously mouse embryonic stem cells have been associated with complex fucosylation by use of SSEA-1 antibody. In the present study we found that complex fucosylation was the most characteristic glycosylation feature also in undifferentiated hESC. The most abundant complex fucosylated structures were Le<sup>x </sup>and H type 2 antennae in sialylated complex-type N-glycans.</p> <p>Conclusion</p> <p>The N-glycan phenotype of hESC was shown to reflect their differentiation stage. During differentiation, hESC-associated N-glycan features were replaced by differentiated cell-associated structures. The results indicated that hESC differentiation stage can be determined by direct analysis of the N-glycan profile. These results provide the first overview of the N-glycan profile of hESC and form the basis for future strategies to target stem cell glycans.</p> http://www.biomedcentral.com/1471-2121/10/42 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Olonen Anne Aitio Olli Jaatinen Taina Tiittanen Minna Blomqvist Maria Olsson Cia Mikkola Milla Heiskanen Annamari Satomaa Tero Helin Jari Hiltunen Jukka Natunen Jari Tuuri Timo Otonkoski Timo Saarinen Juhani Laine Jarmo |
spellingShingle |
Olonen Anne Aitio Olli Jaatinen Taina Tiittanen Minna Blomqvist Maria Olsson Cia Mikkola Milla Heiskanen Annamari Satomaa Tero Helin Jari Hiltunen Jukka Natunen Jari Tuuri Timo Otonkoski Timo Saarinen Juhani Laine Jarmo The N-glycome of human embryonic stem cells BMC Cell Biology |
author_facet |
Olonen Anne Aitio Olli Jaatinen Taina Tiittanen Minna Blomqvist Maria Olsson Cia Mikkola Milla Heiskanen Annamari Satomaa Tero Helin Jari Hiltunen Jukka Natunen Jari Tuuri Timo Otonkoski Timo Saarinen Juhani Laine Jarmo |
author_sort |
Olonen Anne |
title |
The N-glycome of human embryonic stem cells |
title_short |
The N-glycome of human embryonic stem cells |
title_full |
The N-glycome of human embryonic stem cells |
title_fullStr |
The N-glycome of human embryonic stem cells |
title_full_unstemmed |
The N-glycome of human embryonic stem cells |
title_sort |
n-glycome of human embryonic stem cells |
publisher |
BMC |
series |
BMC Cell Biology |
issn |
1471-2121 |
publishDate |
2009-06-01 |
description |
<p>Abstract</p> <p>Background</p> <p>Complex carbohydrate structures, glycans, are essential components of glycoproteins, glycolipids, and proteoglycans. While individual glycan structures including the SSEA and Tra antigens are already used to define undifferentiated human embryonic stem cells (hESC), the whole spectrum of stem cell glycans has remained unknown. We undertook a global study of the asparagine-linked glycoprotein glycans (N-glycans) of hESC and their differentiated progeny using MALDI-TOF mass spectrometric and NMR spectroscopic profiling. Structural analyses were performed by specific glycosidase enzymes and mass spectrometric fragmentation analyses.</p> <p>Results</p> <p>The data demonstrated that hESC have a characteristic N-glycome which consists of both a constant part and a variable part that changes during hESC differentiation. hESC-associated N-glycans were downregulated and new structures emerged in the differentiated cells. Previously mouse embryonic stem cells have been associated with complex fucosylation by use of SSEA-1 antibody. In the present study we found that complex fucosylation was the most characteristic glycosylation feature also in undifferentiated hESC. The most abundant complex fucosylated structures were Le<sup>x </sup>and H type 2 antennae in sialylated complex-type N-glycans.</p> <p>Conclusion</p> <p>The N-glycan phenotype of hESC was shown to reflect their differentiation stage. During differentiation, hESC-associated N-glycan features were replaced by differentiated cell-associated structures. The results indicated that hESC differentiation stage can be determined by direct analysis of the N-glycan profile. These results provide the first overview of the N-glycan profile of hESC and form the basis for future strategies to target stem cell glycans.</p> |
url |
http://www.biomedcentral.com/1471-2121/10/42 |
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