Bmi1 deficient neural stem cells have increased Integrin dependent adhesion to self-secreted matrix

Neural cells deficient for Polycomb group (PcG) protein Bmi1 are impaired in the formation and differentiation of high grade glioma, an incurable cancer of the brain. It was shown that mechanisms involved in cell adhesion and migration were specifically affected in these tumors. Using biochemical an...

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Veröffentlicht in:	Biochimica et biophysica acta Jg. 1790; H. 5; S. 351 - 360
Hauptverfasser:	Bruggeman, Sophia W.M., Hulsman, Danielle, van Lohuizen, Maarten
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Netherlands Elsevier B.V 01.05.2009
Schlagworte:	Adhesion Animals Bmi1 Brain cancer Cell Adhesion Collagen - metabolism Cyclin-Dependent Kinase Inhibitor p16 - metabolism Extracellular Matrix - metabolism Gene Expression Regulation Integrins Integrins - metabolism Mice Neural stem cells Neurons - cytology Neurons - metabolism Nuclear Proteins - deficiency Nuclear Proteins - genetics Nuclear Proteins - metabolism Polycomb group Polycomb Repressive Complex 1 Proto-Oncogene Proteins - deficiency Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Receptors, Cell Surface - metabolism Repressor Proteins - genetics Repressor Proteins - metabolism Stem Cells - cytology Stem Cells - metabolism Neural stem cells Bmi1 Adhesion Polycomb group Brain cancer Integrins
ISSN:	0304-4165, 0006-3002, 1872-8006
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Zusammenfassung:	Neural cells deficient for Polycomb group (PcG) protein Bmi1 are impaired in the formation and differentiation of high grade glioma, an incurable cancer of the brain. It was shown that mechanisms involved in cell adhesion and migration were specifically affected in these tumors. Using biochemical and cell biological approaches, we investigated the adhesive capacities of Bmi1;Ink4a/Arf deficient primary neural stem cells (NSCs). Bmi1;Ink4a/Arf deficient NSCs have altered expression of Collagen-related genes, secrete increased amounts of extracellular matrix, and exhibit enhanced cell–matrix binding through the Beta-1 Integrin receptor. These traits are independent from the well described role of Bmi1 as repressor of the Ink4a/Arf tumor suppressor locus. In addition to proliferative processes, Bmi1 controls the adhesive capacities of primary NSCs by modulating extracellular matrix secretion. Since PcG protein Bmi1 is important for both normal development and tumorigenesis, it is vital to understand the complete network in which this protein acts. Whereas it is clear that control of Ink4a/Arf is a major Bmi1 function, there is evidence that other downstream mechanisms exist. Hence, our novel finding that Bmi1 also governs cell adhesion significantly contributes to our understanding of the PcG proteins.
Bibliographie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0304-4165 0006-3002 1872-8006
DOI:	10.1016/j.bbagen.2009.03.009