Glioma stem cells invasive phenotype at optimal stiffness is driven by MGAT5 dependent mechanosensing.

3D-nanofibre scaffold Biomaterial EMT Focal adhesion Galectin Glioblastoma Glycosylation Mechanotransduction Mgat5 Migration Stiffness

Journal

Journal of experimental & clinical cancer research : CR
ISSN: 1756-9966
Titre abrégé: J Exp Clin Cancer Res
Pays: England
ID NLM: 8308647

Informations de publication

Date de publication:
24 Apr 2021
Historique:
received: 14 12 2020
accepted: 23 03 2021
entrez: 25 4 2021
pubmed: 26 4 2021
medline: 25 11 2021
Statut: epublish

Résumé

Glioblastomas stem-like cells (GSCs) by invading the brain parenchyma, remains after resection and radiotherapy and the tumoral microenvironment become stiffer. GSC invasion is reported as stiffness sensitive and associated with altered N-glycosylation pattern. Glycocalyx thickness modulates integrins mechanosensing, but details remain elusive and glycosylation enzymes involved are unknown. Here, we studied the association between matrix stiffness modulation, GSC migration and MGAT5 induced N-glycosylation in fibrillar 3D context. To mimic the extracellular matrix fibrillar microenvironments, we designed 3D-ex-polyacrylonitrile nanofibers scaffolds (NFS) with adjustable stiffnesses by loading multiwall carbon nanotubes (MWCNT). GSCs neurosphere were plated on NFSs, allowing GSCs migration and MGAT5 was deleted using CRISPR-Cas9. We found that migration of GSCs was maximum at 166 kPa. Migration rate was correlated with cell shape, expression and maturation of focal adhesion (FA), Epithelial to Mesenchymal Transition (EMT) proteins and (β1,6) branched N-glycan binding, galectin-3. Mutation of MGAT5 in GSC inhibited N-glycans (β1-6) branching, suppressed the stiffness dependence of migration on 166 kPa NFS as well as the associated FA and EMT protein expression. MGAT5 catalysing multibranched N-glycans is a critical regulators of stiffness induced invasion and GSCs mechanotransduction, underpinning MGAT5 as a serious target to treat cancer.

Sections du résumé

BACKGROUND BACKGROUND
Glioblastomas stem-like cells (GSCs) by invading the brain parenchyma, remains after resection and radiotherapy and the tumoral microenvironment become stiffer. GSC invasion is reported as stiffness sensitive and associated with altered N-glycosylation pattern. Glycocalyx thickness modulates integrins mechanosensing, but details remain elusive and glycosylation enzymes involved are unknown. Here, we studied the association between matrix stiffness modulation, GSC migration and MGAT5 induced N-glycosylation in fibrillar 3D context.
METHOD METHODS
To mimic the extracellular matrix fibrillar microenvironments, we designed 3D-ex-polyacrylonitrile nanofibers scaffolds (NFS) with adjustable stiffnesses by loading multiwall carbon nanotubes (MWCNT). GSCs neurosphere were plated on NFSs, allowing GSCs migration and MGAT5 was deleted using CRISPR-Cas9.
RESULTS RESULTS
We found that migration of GSCs was maximum at 166 kPa. Migration rate was correlated with cell shape, expression and maturation of focal adhesion (FA), Epithelial to Mesenchymal Transition (EMT) proteins and (β1,6) branched N-glycan binding, galectin-3. Mutation of MGAT5 in GSC inhibited N-glycans (β1-6) branching, suppressed the stiffness dependence of migration on 166 kPa NFS as well as the associated FA and EMT protein expression.
CONCLUSION CONCLUSIONS
MGAT5 catalysing multibranched N-glycans is a critical regulators of stiffness induced invasion and GSCs mechanotransduction, underpinning MGAT5 as a serious target to treat cancer.

Identifiants

pubmed: 33894774
doi: 10.1186/s13046-021-01925-7
pii: 10.1186/s13046-021-01925-7
pmc: PMC8067292
doi:

Substances chimiques

Mgat5 protein, human EC 2.4.1.-
N-Acetylglucosaminyltransferases EC 2.4.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

139

Subventions

Organisme : Inserm (Plan Cancer 2012)
ID : PC201216
Organisme : SATT AxLR
ID : 17/0368

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Auteurs

Emilie Marhuenda (E)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France. e.marhuenda@qmul.ac.uk.
School of Engineering and Materials Science, Queen Mary University of London, London, E1 4NS, UK. e.marhuenda@qmul.ac.uk.
Institut Européen des Membranes, IEM, UMR 5635, University of Montpellier, ENSCM, CNRS, Montpellier, France. e.marhuenda@qmul.ac.uk.

Christine Fabre (C)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France.
École nationale supérieure de chimie de Montpellier, ENSCM, 240 Avenue du Professeur Emile Jeanbrau, 34090, Montpellier, France.

Cunjie Zhang (C)

Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Ave., Toronto, ON, M5G 1X5, Canada.
Department of Molecular Genetics, and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, M5S 1A8, Canada.

Martà Martin-Fernandez (M)

Institut Charles Coulomb, UMR 5221, University of Montpellier, CNRS, Montpellier, France.

Thomas Iskratsch (T)

School of Engineering and Materials Science, Queen Mary University of London, London, E1 4NS, UK.

Ali Saleh (A)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France.

Luc Bauchet (L)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France.

Julien Cambedouzou (J)

Institut Européen des Membranes, IEM, UMR 5635, University of Montpellier, ENSCM, CNRS, Montpellier, France.
École nationale supérieure de chimie de Montpellier, ENSCM, 240 Avenue du Professeur Emile Jeanbrau, 34090, Montpellier, France.

Jean-Philippe Hugnot (JP)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France.

Hugues Duffau (H)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France.

James W Dennis (JW)

Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Ave., Toronto, ON, M5G 1X5, Canada.
Department of Molecular Genetics, and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, M5S 1A8, Canada.

David Cornu (D)

Institut Européen des Membranes, IEM, UMR 5635, University of Montpellier, ENSCM, CNRS, Montpellier, France. david.cornu@enscm.fr.
École nationale supérieure de chimie de Montpellier, ENSCM, 240 Avenue du Professeur Emile Jeanbrau, 34090, Montpellier, France. david.cornu@enscm.fr.

Norbert Bakalara (N)

Institut des Neurosciences de Montpellier (INM) U-1051, University of Montpellier, 80 rue Augustin Fliche, Hôpital Saint-Eloi, 34091, Montpellier, Cedex 5, France. norbert.bakalara@enstbb.fr.
École nationale supérieure de chimie de Montpellier, ENSCM, 240 Avenue du Professeur Emile Jeanbrau, 34090, Montpellier, France. norbert.bakalara@enstbb.fr.

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Classifications MeSH