Exploring analytical proteomics platforms toward the definition of human cardiac stem cells receptome
Autor: | Margarida Serra, Catarina Brito, Antonio Bernad, Paula M. Alves, Juan Antonio López, Jesús Vázquez, Luis R.-Borlado, Patrícia Gomes-Alves, Manuel J.T. Carrondo |
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Přispěvatelé: | European Commission |
Rok vydání: | 2015 |
Předmět: |
Proteomics
Proteome Myocardial Infarction Receptors Cell Surface Computational biology Biology Bioinformatics Biochemistry 03 medical and health sciences Paracrine signalling Tandem Mass Spectrometry Humans Regeneration Receptor Molecular Biology Cells Cultured 030304 developmental biology 0303 health sciences Regeneration (biology) Myocardium 030302 biochemistry & molecular biology Prefractionation Chromatography Ion Exchange Transmembrane protein Nano-LC-MS/MS Biomedicine Adult Stem Cells Human cardiac stem cells Stem cell Receptome Adult stem cell |
Zdroj: | Repisalud Instituto de Salud Carlos III (ISCIII) |
Popis: | Human cardiac stem cells (hCSC) express a portfolio of plasma membrane receptors that are involved in the regulatory auto/paracrine feedback loop mechanism of activation of these cells, and consequently contribute to myocardial regeneration. In order to attain a comprehensive description of hCSC receptome and overcoming the inability demonstrated by other technologies applied in receptor identification, mainly due to the transmembrane nature, high hydrophobic character and relative low concentration of these proteins, we have exploited and improved a proteomics workflow. This approach was based on the enrichment of hCSC plasma membrane fraction and addition of prefractionation steps prior to MS analysis. More than 100 plasma membrane receptors were identified. The data reported herein constitute a valuable source of information to further understand cardiac stem cells activation mechanisms and the subsequent cardiac repair process. All MS data have been deposited in the ProteomeXchange with identifier PXD001117 (http://proteomecentral.proteomexchange.org/dataset/PXD001117). Authors acknowledge FP7 EU project CARE-MI (HEALTH-2009_242038) and the Portuguese Foundation for Science and Technology (PTDC/BBBBIO/1414) for financial support. PGA is a recipient of the FCT fellowship SFRH/BPD/86513/2012. MALDI-TOF/TOF analyses were performed at the Mass Spectrometry Unit (UniMS), ITQB/iBET, Oeiras, Portugal. The data deposition to the ProteomeXchange Consortium was supported by PRIDETeam, EBI. Sí |
Databáze: | OpenAIRE |
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