Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks
Protein kinase C (PKC) activation induces cellular reprogramming and differentiation in various cell models. Although many effectors of PKC physiological actions have been elucidated, the molecular mechanisms regulating oligodendrocyte differentiation after PKC activation are still unclear. Here, we...
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doaj-516636de86b5464a882a73fb595bf4592021-06-01T00:08:58ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-05-01225245524510.3390/ijms22105245Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological NetworksMarina Damato0Tristan Cardon1Maxence Wisztorski2Isabelle Fournier3Damiana Pieragostino4Ilaria Cicalini5Michel Salzet6Daniele Vergara7Michele Maffia8Department of Biological and Environmental Sciences and Technologies, University of Salento, 73100 Lecce, ItalyLaboratoire Protéomique, Réponse Inflammatoire et Spectrométrie de Masse (PRISM), Université de Lille, INSERM, U1192, F-59000 Lille, FranceLaboratoire Protéomique, Réponse Inflammatoire et Spectrométrie de Masse (PRISM), Université de Lille, INSERM, U1192, F-59000 Lille, FranceLaboratoire Protéomique, Réponse Inflammatoire et Spectrométrie de Masse (PRISM), Université de Lille, INSERM, U1192, F-59000 Lille, FranceCenter for Advanced Studies and Technology (CAST), University “G. d’Annunzio” of Chieti-Pescara, 66100 Chieti, ItalyCenter for Advanced Studies and Technology (CAST), University “G. d’Annunzio” of Chieti-Pescara, 66100 Chieti, ItalyLaboratoire Protéomique, Réponse Inflammatoire et Spectrométrie de Masse (PRISM), Université de Lille, INSERM, U1192, F-59000 Lille, FranceDepartment of Biological and Environmental Sciences and Technologies, University of Salento, 73100 Lecce, ItalyDepartment of Biological and Environmental Sciences and Technologies, University of Salento, 73100 Lecce, ItalyProtein kinase C (PKC) activation induces cellular reprogramming and differentiation in various cell models. Although many effectors of PKC physiological actions have been elucidated, the molecular mechanisms regulating oligodendrocyte differentiation after PKC activation are still unclear. Here, we applied a liquid chromatography–mass spectrometry (LC–MS/MS) approach to provide a comprehensive analysis of the proteome expression changes in the MO3.13 oligodendroglial cell line after PKC activation. Our findings suggest that multiple networks that communicate and coordinate with each other may finally determine the fate of MO3.13 cells, thus identifying a modular and functional biological structure. In this work, we provide a detailed description of these networks and their participating components and interactions. Such assembly allows perturbing each module, thus describing its physiological significance in the differentiation program. We applied this approach by targeting the Rho-associated protein kinase (ROCK) in PKC-activated cells. Overall, our findings provide a resource for elucidating the PKC-mediated network modules that contribute to a more robust knowledge of the molecular dynamics leading to this cell fate transition.https://www.mdpi.com/1422-0067/22/10/5245PKCdifferentiationoligodendrocytessignalingmass spectrometrycytoskeleton |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Marina Damato Tristan Cardon Maxence Wisztorski Isabelle Fournier Damiana Pieragostino Ilaria Cicalini Michel Salzet Daniele Vergara Michele Maffia |
spellingShingle |
Marina Damato Tristan Cardon Maxence Wisztorski Isabelle Fournier Damiana Pieragostino Ilaria Cicalini Michel Salzet Daniele Vergara Michele Maffia Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks International Journal of Molecular Sciences PKC differentiation oligodendrocytes signaling mass spectrometry cytoskeleton |
author_facet |
Marina Damato Tristan Cardon Maxence Wisztorski Isabelle Fournier Damiana Pieragostino Ilaria Cicalini Michel Salzet Daniele Vergara Michele Maffia |
author_sort |
Marina Damato |
title |
Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks |
title_short |
Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks |
title_full |
Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks |
title_fullStr |
Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks |
title_full_unstemmed |
Protein Kinase C Activation Drives a Differentiation Program in an Oligodendroglial Precursor Model through the Modulation of Specific Biological Networks |
title_sort |
protein kinase c activation drives a differentiation program in an oligodendroglial precursor model through the modulation of specific biological networks |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-05-01 |
description |
Protein kinase C (PKC) activation induces cellular reprogramming and differentiation in various cell models. Although many effectors of PKC physiological actions have been elucidated, the molecular mechanisms regulating oligodendrocyte differentiation after PKC activation are still unclear. Here, we applied a liquid chromatography–mass spectrometry (LC–MS/MS) approach to provide a comprehensive analysis of the proteome expression changes in the MO3.13 oligodendroglial cell line after PKC activation. Our findings suggest that multiple networks that communicate and coordinate with each other may finally determine the fate of MO3.13 cells, thus identifying a modular and functional biological structure. In this work, we provide a detailed description of these networks and their participating components and interactions. Such assembly allows perturbing each module, thus describing its physiological significance in the differentiation program. We applied this approach by targeting the Rho-associated protein kinase (ROCK) in PKC-activated cells. Overall, our findings provide a resource for elucidating the PKC-mediated network modules that contribute to a more robust knowledge of the molecular dynamics leading to this cell fate transition. |
topic |
PKC differentiation oligodendrocytes signaling mass spectrometry cytoskeleton |
url |
https://www.mdpi.com/1422-0067/22/10/5245 |
work_keys_str_mv |
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