Pastel Info

Pastel is a relational web-accessible database that hosts data from proteomic analysis of stem cells. Furthermore, it facilitates data mining and information extraction as well as it provides the scientific community with a reliable stem cells proteomics data repository to facilitate further research. Pastel has been developed and hosted by the Academy of Athens Foundation for Biomedical Research

For more information about the responsible research group, you can visit BioAcademy Stem Cells Group

Proteomics Analysis & Stem Cells

Stem Cells

firefox Embryonic stem cells (ESCs) are derived from the inner cell mass (ICM) of embryos at the blastocyst stage. They can be expanded in culture and when introduced back into blastocyst, they retain their ability to differentiate to all three embryonic germ layers. There is, currently, considerable interest to take advantage of their pluripotent properties and provide renewable source of material for a diversity of conditions such as burn traumas, diabetes type I, myocardial infarction and several lethal neurodegenerative diseases (reviewed by Tutter et al., 2006). For this, several protocols have been developed to drive ESCs into various cell lineages (reviewed by Turksen K and Troy TC, 2006). There has been extensive work into the molecular mechanisms that underline the characteristics of stem cells, especially their self-renewal potential. We, now, know that mouse ESCs depend upon the Wnt and LIF-JAK-STAT3 pathways to remain undifferentiated (reviewed by Kristensen et al., 2005, Darr and Benvenisty, 2006). However, despite these extensive studies we know very little of the remaining physiological processes inside these cells. It is imperative we, also, examine the regulation of gene expression as well as the processes regulating protein turnover, transport and functional protein-protein interactions. To this end, proteomics provide a reliable methodology along side existing large-scale gene expression analyses (Richards et al., 2004; Araki et al., 2006). Here, we report the use of 2-DE and MALDI-TOF-MS protein sequencing techniques to identify the mESCs proteome. We complement our finding with co-IPs and immunocytochemistry to further characterize protein-protein interactions in the context of functional networks.