Specific lectin biomarkers for isolation of human pluripotent stem cells identified through array-based glycomic analysis

Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glyco- proteins extracted from 26 hPSC samples and 22 differentiated cell sampl...

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Published inCell research Vol. 21; no. 11; pp. 1551 - 1563
Main Authors Wang, Yu-Chieh, Nakagawa, Masato, Garitaonandia, Ibon, Slavin, Ileana, Altun, Gulsah, Lacharite, Robert M, Nazor, Kristopher L, Tran, Ha T, Lynch, Candace L, Leonardo, Trevor R, Liu, Ying, Peterson, Suzanne E, Laurent, Louise C, Yamanaka, Shinya, Loring, Jeanne F
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.11.2011
Nature Publishing Group
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Online AccessGet full text
ISSN1001-0602
1748-7838
1748-7838
DOI10.1038/cr.2011.148

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Abstract Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glyco- proteins extracted from 26 hPSC samples and 22 differentiated cell samples, and identified a small group of lectins with distinctive binding signatures that were sufficient to distinguish hPSCs from a variety of non-pluripotent cell types. These specific biomarkers were shared by all the 12 human embryonic stem cell and the 14 human induced pluripotent stem cell samples examined, regardless of the laboratory of origin, the culture conditions, the somatic cell type reprogrammed, or the reprogramming method used. We demonstrated a practical application of specific lectin binding by detecting hPSCs within a differentiated cell population with lectin-mediated staining followed by fluores- cence microscopy and flow cytometry, and by enriching and purging viable hPSCs from mixed cell populations using lectin-mediated cell separation. Global gene expression analysis showed pluripotency-associated differential expres- sion of specific fucosyltransferases and sialyltransferases, which may underlie these differences in protein glycosy- lation and lectin binding. Taken together, our results show that protein glycosylation differs considerably between pluripotent and non-pluripotent cells, and demonstrate that lectins may be used as biomarkers to monitor pluripo- tency in stem cell populations and for removal of viable hPSCs from mixed cell population
AbstractList Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glycoproteins extracted from 26 hPSC samples and 22 differentiated cell samples, and identified a small group of lectins with distinctive binding signatures that were sufficient to distinguish hPSCs from a variety of non-pluripotent cell types. These specific biomarkers were shared by all the 12 human embryonic stem cell and the 14 human induced pluripotent stem cell samples examined, regardless of the laboratory of origin, the culture conditions, the somatic cell type reprogrammed, or the reprogramming method used. We demonstrated a practical application of specific lectin binding by detecting hPSCs within a differentiated cell population with lectin-mediated staining followed by fluorescence microscopy and flow cytometry, and by enriching and purging viable hPSCs from mixed cell populations using lectin-mediated cell separation. Global gene expression analysis showed pluripotency-associated differential expression of specific fucosyltransferases and sialyltransferases, which may underlie these differences in protein glycosylation and lectin binding. Taken together, our results show that protein glycosylation differs considerably between pluripotent and non-pluripotent cells, and demonstrate that lectins may be used as biomarkers to monitor pluripotency in stem cell populations and for removal of viable hPSCs from mixed cell populations.
Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glycoproteins extracted from 26 hPSC samples and 22 differentiated cell samples, and identified a small group of lectins with distinctive binding signatures that were sufficient to distinguish hPSCs from a variety of non-pluripotent cell types. These specific biomarkers were shared by all the 12 human embryonic stem cell and the 14 human induced pluripotent stem cell samples examined, regardless of the laboratory of origin, the culture conditions, the somatic cell type reprogrammed, or the reprogramming method used. We demonstrated a practical application of specific lectin binding by detecting hPSCs within a differentiated cell population with lectin-mediated staining followed by fluorescence microscopy and flow cytometry, and by enriching and purging viable hPSCs from mixed cell populations using lectin-mediated cell separation. Global gene expression analysis showed pluripotency-associated differential expression of specific fucosyltransferases and sialyltransferases, which may underlie these differences in protein glycosylation and lectin binding. Taken together, our results show that protein glycosylation differs considerably between pluripotent and non-pluripotent cells, and demonstrate that lectins may be used as biomarkers to monitor pluripotency in stem cell populations and for removal of viable hPSCs from mixed cell populations.Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glycoproteins extracted from 26 hPSC samples and 22 differentiated cell samples, and identified a small group of lectins with distinctive binding signatures that were sufficient to distinguish hPSCs from a variety of non-pluripotent cell types. These specific biomarkers were shared by all the 12 human embryonic stem cell and the 14 human induced pluripotent stem cell samples examined, regardless of the laboratory of origin, the culture conditions, the somatic cell type reprogrammed, or the reprogramming method used. We demonstrated a practical application of specific lectin binding by detecting hPSCs within a differentiated cell population with lectin-mediated staining followed by fluorescence microscopy and flow cytometry, and by enriching and purging viable hPSCs from mixed cell populations using lectin-mediated cell separation. Global gene expression analysis showed pluripotency-associated differential expression of specific fucosyltransferases and sialyltransferases, which may underlie these differences in protein glycosylation and lectin binding. Taken together, our results show that protein glycosylation differs considerably between pluripotent and non-pluripotent cells, and demonstrate that lectins may be used as biomarkers to monitor pluripotency in stem cell populations and for removal of viable hPSCs from mixed cell populations.
Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glyco- proteins extracted from 26 hPSC samples and 22 differentiated cell samples, and identified a small group of lectins with distinctive binding signatures that were sufficient to distinguish hPSCs from a variety of non-pluripotent cell types. These specific biomarkers were shared by all the 12 human embryonic stem cell and the 14 human induced pluripotent stem cell samples examined, regardless of the laboratory of origin, the culture conditions, the somatic cell type reprogrammed, or the reprogramming method used. We demonstrated a practical application of specific lectin binding by detecting hPSCs within a differentiated cell population with lectin-mediated staining followed by fluores- cence microscopy and flow cytometry, and by enriching and purging viable hPSCs from mixed cell populations using lectin-mediated cell separation. Global gene expression analysis showed pluripotency-associated differential expres- sion of specific fucosyltransferases and sialyltransferases, which may underlie these differences in protein glycosy- lation and lectin binding. Taken together, our results show that protein glycosylation differs considerably between pluripotent and non-pluripotent cells, and demonstrate that lectins may be used as biomarkers to monitor pluripo- tency in stem cell populations and for removal of viable hPSCs from mixed cell population
Author Tran, Ha T
Loring, Jeanne F
Garitaonandia, Ibon
Leonardo, Trevor R
Altun, Gulsah
Peterson, Suzanne E
Slavin, Ileana
Nazor, Kristopher L
Yamanaka, Shinya
Liu, Ying
Nakagawa, Masato
Lynch, Candace L
Wang, Yu-Chieh
Laurent, Louise C
Lacharite, Robert M
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  organization: Department of Chemical Physiology, The Scripps Research Institute, The Scripps Research Institute, Center for Regenerative Medicine, Department of Reproductive Medicine, University of California, San Diego
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/21894191$$D View this record in MEDLINE/PubMed
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DocumentTitleAlternate Specific lectin biomarkers for isolation of human pluripotent stem cells identified through array-based glycomic analysis
Lectin biomarkers of pluripotency
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Issue 11
Keywords glycosylation
induced pluripotent stem cells
human pluripotent stem cell
embryonic stem cells
lectins
pluripotency biomarkers
Language English
License https://creativecommons.org/licenses/by-nc-nd/3.0
This work is licensed under the Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0
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Notes Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in cell-based therapy applications. Using lectin arrays, we analyzed glyco- proteins extracted from 26 hPSC samples and 22 differentiated cell samples, and identified a small group of lectins with distinctive binding signatures that were sufficient to distinguish hPSCs from a variety of non-pluripotent cell types. These specific biomarkers were shared by all the 12 human embryonic stem cell and the 14 human induced pluripotent stem cell samples examined, regardless of the laboratory of origin, the culture conditions, the somatic cell type reprogrammed, or the reprogramming method used. We demonstrated a practical application of specific lectin binding by detecting hPSCs within a differentiated cell population with lectin-mediated staining followed by fluores- cence microscopy and flow cytometry, and by enriching and purging viable hPSCs from mixed cell populations using lectin-mediated cell separation. Global gene expression analysis showed pluripotency-associated differential expres- sion of specific fucosyltransferases and sialyltransferases, which may underlie these differences in protein glycosy- lation and lectin binding. Taken together, our results show that protein glycosylation differs considerably between pluripotent and non-pluripotent cells, and demonstrate that lectins may be used as biomarkers to monitor pluripo- tency in stem cell populations and for removal of viable hPSCs from mixed cell population
Yu-Chieh Wang , Masato Nakagawa3, Ibon Garitaonandia Ileana Slavin1' 2 Gulsah Altun, Robert M Lacharite Kristopher L Nazor1' 2, Ha T Tran1' 2 Candace L Lynch, Trevor R Leonardo, Ying Liu, Suzanne E Peterson Louise C Laurent, 7, Shinya Yamanaka , 6, Jeanne F Loring, The Scripps Research Institute, Department of Chemical Physiology, La Jolla, CA 92037, USA; 2The Scripps Research Institute, Center for Regenerative Medicine, 10550 N. Torrey Pines Rd, SP-3021, La Jolla, CA 92037, USA," 3Center for iPS Cell Research and Application (CiRA), Kyoto University, Kyoto, Japan; 4Institute for Integrated Cell-Material Sciences, Kyoto University, Kyoto, Japan; 5Japan Science and Technology Agency, Yamanaka iPS Cell Special Project, Kawaguchi, Japan; 6Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94158-2261, USA; 7Department of Reproductive Medicine, University of California, San Diego, La Jolla, CA, USA
31-1568/Q
lectins; glycosylation; pluripotency biomarkers; human pluripotent stem cell; induced pluripotent stem cells; em- bryonic stem cells
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Snippet Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in...
Rapid and dependable methods for isolating human pluripotent stem cell (hPSC) populations are urgently needed for quality control in basic research and in...
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StartPage 1551
SubjectTerms 631/136/2444
631/136/532/2064
631/45/612/1235
631/80/458/1524
biomarkers
Biomarkers - metabolism
Biomedical and Life Sciences
Biotin - chemistry
Biotin - metabolism
Cell Biology
Cell culture
Cell Separation
Cells, Cultured
Embryo cells
Embryonic Stem Cells - cytology
Flow cytometry
Fluorescence
Fluorescence microscopy
Fucosyltransferases - metabolism
Gene expression
Gene Expression Profiling
Glycomics
Glycoproteins
Glycosylation
Humans
Induced Pluripotent Stem Cells - cytology
Lectins
Lectins - chemistry
Lectins - metabolism
Life Sciences
Neolactotetraosylceramide alpha -2,3-sialyltransferase
Original
original-article
Pluripotent Stem Cells - cytology
Pluripotent Stem Cells - metabolism
Protein Array Analysis
Protein Binding
Quality control
Sialyltransferases - metabolism
Somatic cells
Stem cells
人类胚胎干细胞
基因表达分析
外源凝集素
多能干细胞
生物标志物
细胞分离
细胞类型
阵列
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Title Specific lectin biomarkers for isolation of human pluripotent stem cells identified through array-based glycomic analysis
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Volume 21
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