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Define patterns of tyrosine phosphorylation associated with self-renewal of human embryonic stem cells.

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Abstract:

Signaling pathways controlled by protein tyrosine phosphorylation are known to play a major role in maintaining the self-renewal capacity of human embryonic stem cells (hESCs). To characterize the global tyrosine phosphorylation state of hESCs, we performed a proteomic binding assay using the human complement of Src homology 2 (SH2) domains (termed SH2 profiling). The SH2 domain is the most prevalent type of the phosphotyrosine-recognizing domain and there are 110 SH2 domain-containing proteins in different cell signaling pathways. Thus binding patterns of SH2 domains would provide snapshots of cell signaling status of hESCs in various culture conditions.

ESCs are conventionally maintained in culture with feeder cells containing exogenous factors such as FGFs, although chemically defined media are becoming popular for controlling signaling inputs that regulate self-renewal of ESCs without multiple unknown factors. We investigate the tyrosine phosphorylation status of hESCs cultured in conditioned medium (CM) and chemically defined medium (TeSR). Overall phosphorylation profiles were very similar between the two conditions, however, distinctive profiles were also detected by either an anti-phosphotyrosine antibody and a subset of SH2 domain probes. Efforts are undrway to characterize those specific proteins and to distinguish the culture conditions based on the SH2 binding patterns.

Elucidation of signaling events that regulate the pluripotency and self-renewal is important for understanding their physiology and devising optimal culture conditions for their large-scale growth. This study provides useful information to identify molecular mechanisms underlying self-renewal of hESCs and to develop further optimized culture conditions.

This study is supported by the CT-DPH Stem Cell Research Program.
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Association:
Name: Connecticut's Stem Cell Research International Symposium
URL:
http://stemconn.org


Citation:
URL: http://citation.allacademic.com/meta/p369382_index.html
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MLA Citation:

Jia, Lin., Machida, Kazuya., Mayer, Bruce., Thompson, Christopher., Lin, Ge. and Xu, Ren-He. "Define patterns of tyrosine phosphorylation associated with self-renewal of human embryonic stem cells." Paper presented at the annual meeting of the Connecticut's Stem Cell Research International Symposium, Omni Hotel, New Haven, CT, Mar 23, 2009 <Not Available>. 2014-11-29 <http://citation.allacademic.com/meta/p369382_index.html>

APA Citation:

Jia, L. , Machida, K. , Mayer, B. J., Thompson, C. M., Lin, G. and Xu, R. , 2009-03-23 "Define patterns of tyrosine phosphorylation associated with self-renewal of human embryonic stem cells." Paper presented at the annual meeting of the Connecticut's Stem Cell Research International Symposium, Omni Hotel, New Haven, CT <Not Available>. 2014-11-29 from http://citation.allacademic.com/meta/p369382_index.html

Publication Type: Poster
Review Method: Peer Reviewed
Abstract: Signaling pathways controlled by protein tyrosine phosphorylation are known to play a major role in maintaining the self-renewal capacity of human embryonic stem cells (hESCs). To characterize the global tyrosine phosphorylation state of hESCs, we performed a proteomic binding assay using the human complement of Src homology 2 (SH2) domains (termed SH2 profiling). The SH2 domain is the most prevalent type of the phosphotyrosine-recognizing domain and there are 110 SH2 domain-containing proteins in different cell signaling pathways. Thus binding patterns of SH2 domains would provide snapshots of cell signaling status of hESCs in various culture conditions.

ESCs are conventionally maintained in culture with feeder cells containing exogenous factors such as FGFs, although chemically defined media are becoming popular for controlling signaling inputs that regulate self-renewal of ESCs without multiple unknown factors. We investigate the tyrosine phosphorylation status of hESCs cultured in conditioned medium (CM) and chemically defined medium (TeSR). Overall phosphorylation profiles were very similar between the two conditions, however, distinctive profiles were also detected by either an anti-phosphotyrosine antibody and a subset of SH2 domain probes. Efforts are undrway to characterize those specific proteins and to distinguish the culture conditions based on the SH2 binding patterns.

Elucidation of signaling events that regulate the pluripotency and self-renewal is important for understanding their physiology and devising optimal culture conditions for their large-scale growth. This study provides useful information to identify molecular mechanisms underlying self-renewal of hESCs and to develop further optimized culture conditions.

This study is supported by the CT-DPH Stem Cell Research Program.


Similar Titles:
An Efficient Protocol for Generating Neural Stem Cells (NSCs) from Human Embryonic Stem Cells

Expression of Genes involved in Self-Renewal or Lineage Priming in Mouse Embryonic Stem Cells

Generation of Myeloid Cells from Human Embryonic Stem Cells.


 
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