TAILIEUCHUNG - Báo cáo khoa học: Use of lithium and SB-415286 to explore the role of glycogen synthase kinase-3 in the regulation of glucose transport and glycogen synthase

Glycogen synthase kinase 3 (GSK3) is inactivated by insulin and lithium and, like insulin, Li also activates glycogen synthase (GS)viainhibition of GSK3. Li also mimics insu-lin’s ability to stimulate glucose transport (GT), an obser-vation that has led to the suggestion that GSK3 may coordinate hormonal increases in GT and glycogen synthe-sis. Here we have used Li and SB-415286, a selective GSK3 inhibitor, to establish the importance of GSK3 in the hor-monal activation of GT in terms of its effect on GS in L6 myotubes and3T3-L1adipocytes. . | Eur. J. Biochem. 270 3829-3838 2003 FEBS 2003 doi Use of lithium and SB-415286 to explore the role of glycogen synthase kinase-3 in the regulation of glucose transport and glycogen synthase Katrina MacAulay1 Eric Hajduch1 Anne S. Blair1 Matthew P. Coghlan2 Stephen A. Smith2 and Harinder S. Hundal1 1 Division of Molecular Physiology Faculty of Life Sciences MSI WTB Complex University of Dundee UK 2GlaxoSmithKline Harlow UK Glycogen synthase kinase 3 GSK3 is inactivated by insulin and lithium and like insulin Li also activates glycogen synthase GS via inhibition of GSK3. Li also mimics insulin s ability to stimulate glucose transport GT an observation that has led to the suggestion that GSK3 may coordinate hormonal increases in GT and glycogen synthesis. Here we have used Li and SB-415286 a selective GSK3 inhibitor to establish the importance of GSK3 in the hormonal activation of GT in terms of its effect on GS in L6 myotubes and 3T3-L1 adipocytes. Insulin Li and SB-415286 all induced a significant inhibition of GSK3 which was associated with a marked dephosphorylation and activation of GS. In L6 myotubes SB-415286 induced a much greater activation of GS compared to that elicited by insulin or Li 4-fold . In adipocytes insulin Li and SB-415286 all caused a comparable activation of GS despite a substantial differentiation-linked reduction in GSK3 expression w 85 indicating that GSK3 remains an important determinant of GS activation in fat cells. Whilst Li and SB-415286 both inhibit GSK3 in muscle and fat cells only Li stimulated GT. This increase in GT was not sensitive to inhibitors of PI3-kinase MAP kinase or mTOR but was suppressed by the p38 MAP kinase inhibitor SB-203580. Consistent with this phosphorylation of p38 MAP kinase induced by Li correlated with its stimulatory effect on GT. Our findings support a crucial role for GSK3 in the regulation of GS but based on the differential effects of Li and SB-415286 it

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