IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
Partial Inhibition of the Proteasome Enhances the Activity of the Myelin Basic Protein Promoter
Autor/es:
C.A. CALATAYUD C.I. GARCÍA P.M. PAEZ J.M. PASQUINI E.F. SOTO L.A. PASQUIN
Revista:
DEVELOPMENTAL NEUROSCIENCE
Editorial:
S. Karger AG, Basel
Referencias:
Año: 2008
ISSN:
0378-5866
Resumen:
We have previously shown that low concentrations of a specific
proteasome inhibitor accelerate exit from the cell cycle
and enhance oligodendroglial cell (OLGc) differentiation. To
elucidate the mechanisms involved in this process, OLGcs of
the N20.1 cell line, transfected with a reporter gene driven
by the MBP promoter, were treated with proteasome inhibitors
and/or inhibitors of different signaling pathways. Partial
proteasome inhibition resulted in enhanced activation of
the MBP promoter which involved the tyrosine kinase, P13-
Akt and PKC pathways, accompanied by an increase in the
levels of p21 Cip1 , p27 Kip1 and Sp1 and by a decrease in Nkx2.2.
Binding of Sp1 to DNA was also increased. These results were
not observed when the Sp1 binding site was mutated. We
conclude that the enhanced activation of the MBP promoter
induced by partial inhibition of the proteasome could be
due, at least in part, to the stabilization of p27 Kip1 and Sp1
Binding of Sp1 to DNA was also increased. These results were
not observed when the Sp1 binding site was mutated. We
conclude that the enhanced activation of the MBP promoter
induced by partial inhibition of the proteasome could be
due, at least in part, to the stabilization of p27 Kip1 and Sp1
Binding of Sp1 to DNA was also increased. These results were
not observed when the Sp1 binding site was mutated. We
conclude that the enhanced activation of the MBP promoter
induced by partial inhibition of the proteasome could be
due, at least in part, to the stabilization of p27 Kip1 and Sp1
Cip1 , p27 Kip1 and Sp1 and by a decrease in Nkx2.2.
Binding of Sp1 to DNA was also increased. These results were
not observed when the Sp1 binding site was mutated. We
conclude that the enhanced activation of the MBP promoter
induced by partial inhibition of the proteasome could be
due, at least in part, to the stabilization of p27 Kip1 and Sp1Kip1 and Sp1