Supporting data on combined transcriptomic and phosphoproteomic analysis of BMP4 signaling in human embryonic stem cells
Angelos Papadopoulos,
Varvara Chalmantzi,
Marko Hyvönen,
Dimitris Stellas,
Marika Syrrou,
Theodore Fotsis,
Carol Murphy
Affiliations
Angelos Papadopoulos
School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, United Kingdom; Cardiovascular Division, King's College London British Heart Foundation Centre of Excellence, London, SE5 9NU, United Kingdom
Varvara Chalmantzi
School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, United Kingdom
Marko Hyvönen
Department of Biochemistry, University of Cambridge, United Kingdom
Dimitris Stellas
Institute of Chemical Biology, National Hellenic Research Foundation, 11635 Athens, Greece
Marika Syrrou
Laboratory of Biology, Medical School, University of Ioannina, 45110 Ioannina, Greece
Theodore Fotsis
Department of Biomedical Research, Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, University Campus of Ioannina, 45110 Ioannina, Greece; Laboratory of Biological Chemistry, Medical School, University of Ioannina, 45110 Ioannina, Greece
Carol Murphy
School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, United Kingdom; Department of Biomedical Research, Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, University Campus of Ioannina, 45110 Ioannina, Greece; Corresponding author.
Human embryonic stem cells exhibit great potential as a therapeutic tool in regenerative medicine due to their self-renewal and trilineage differentiation capacity. Maintaining this unique cellular state has been shown to rely primarily on the Activin A / TGFβ signaling pathway. While most conventional culture media are supplemented with TGFβ, in the current study we utilize a modified version of the commercially available mTeSR1, substituting TGFβ for Activin A in order to preserve pluripotency. (1) Cells cultured in ActA-mTesR express pluripotency factors NANOG, OCT4 and SOX2 at comparable levels with cells cultured in TGFβ-mTeSR. (2) ActA-mTeSR cultured cells retain a physiological karyotype. (3) Cells in ActA-mTeSR maintain their trilineage differentiation capacity as shown in the teratoma formation assay. This system can be used to dissect the role of Activin A, downstream effectors and signaling cascades in human embryonic stem cell responses.