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Provedor de dados:  Biological Sciences
País:  Brazil
Título:  Study of comparative proteome between normal and inverted karyotypes of human mesenchymal stem cells
Study of comparative proteome between normal and inverted karyotypes of human mesenchymal stem cells
Autores:  de Souza Santos, John Lenon
Câmara, Alice Barros
Meira, Isabella Tanus Job e
Oliveira, Jonas Ivan Nobre
Data:  2020-04-03
Ano:  2020
Palavras-chave:  Genetic instability
Protein profile
Umbilical cord
Interaction network. genetic instability
Protein profile
Umbilical cord
Interaction network.
Resumo:   Multipotent mesenchymal stem cells have been expanded in vitro for cellular therapy in numerous clinical settings without standardized culture conditions or quality-control schemes. The in vitro expansion is necessary to obtain sufficient cells for clinical applications. However, the expansion may induce genetic and functional abnormalities which may affect the safety and functionality of MSC, especially the chromosomal stability. This study aimed to investigate the protein profile of umbilical cord-derived MSC with normal and inverted karyotypes after expansion in the laboratory. Mass spectrometry analysis was performed and the Bradford method, Scaffold software, String and Cytoscape databases were employed to measure and characterize the protein content of umbilical cord-derived MSC. Networks of protein interactions, hub and bottleneck proteins were identified by proteomics and systems biology approaches. We found that proteins related to cellular stress were super expressed in inverted karyotype cells. Moreover, a high expression of Serpine 1, RHOA, and CTSB was found in these cells, which are proteins related to cancer. The albumin and ubiquitin proteins have been associated with a positive prognosis in cancer and cellular stress, and were up- and down-regulated in normal karyotype cells, respectively. The results suggests that the paracentric inversion inv(3)(p25p13) induced some type of cellular stress and genetic instability in human mesenchymal stem cells. These analyses showed the importance of carrying out studies related to the genetic instability of human mesenchymal stem cells using the protein expression profile as a parameter.

 Multipotent mesenchymal stem cells have been expanded in vitro for cellular therapy in numerous clinical settings without standardized culture conditions or quality-control schemes. The in vitro expansion is necessary to obtain sufficient cells for clinical applications. However, the expansion may induce genetic and functional abnormalities which may affect the safety and functionality of MSC, especially the chromosomal stability. This study aimed to investigate the protein profile of umbilical cord-derived MSC with normal and inverted karyotypes after expansion in the laboratory. Mass spectrometry analysis was performed and the Bradford method, Scaffold software, String and Cytoscape databases were employed to measure and characterize the protein content of umbilical cord-derived MSC. Networks of protein interactions, hub and bottleneck proteins were identified by proteomics and systems biology approaches. We found that proteins related to cellular stress were super expressed in inverted karyotype cells. Moreover, a high expression of Serpine 1, RHOA, and CTSB was found in these cells, which are proteins related to cancer. The albumin and ubiquitin proteins have been associated with a positive prognosis in cancer and cellular stress, and were up- and down-regulated in normal karyotype cells, respectively. The results suggests that the paracentric inversion inv(3)(p25p13) induced some type of cellular stress and genetic instability in human mesenchymal stem cells. These analyses showed the importance of carrying out studies related to the genetic instability of human mesenchymal stem cells using the protein expression profile as a parameter.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/50260

10.4025/actascibiolsci.v42i1.50260
Editor:  Universidade Estadual De Maringá
Relação:  http://periodicos.uem.br/ojs/index.php/ActaSciBiolSci/article/view/50260/751375149817
Formato:  application/pdf
Fonte:  Acta Scientiarum. Biological Sciences; Vol 42 (2020): Publicação contínua; e50260

Acta Scientiarum. Biological Sciences; v. 42 (2020): Publicação contínua; e50260

1807-863X

1679-9283
Direitos:  Copyright (c) 2020 Acta Scientiarum. Biological Sciences

http://creativecommons.org/licenses/by/4.0
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