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 in | Cell research Vol. 21; no. 11; pp. 1551 - 1563 |
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Main Authors | , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
01.11.2011
Nature Publishing Group |
Subjects | |
Online Access | Get full text |
ISSN | 1001-0602 1748-7838 1748-7838 |
DOI | 10.1038/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 |
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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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Copyright | The Author(s) 2011 Copyright Nature Publishing Group Nov 2011 Copyright © 2011 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences 2011 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences |
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Keywords | glycosylation induced pluripotent stem cells human pluripotent stem cell embryonic stem cells lectins pluripotency biomarkers |
Language | English |
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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 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Article-2 ObjectType-Feature-1 content type line 23 |
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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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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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