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J. Biol. Chem., Vol. 266, Issue 16, 10122-10130, Jun, 1991
BM Clancy, SA Harrison, JM Buxton and MP Czech
In this study, we tested the hypothesis that hexose transport regulation
may involve proteins with relatively rapid turnover rates. 3T3-L1
adipocytes, which exhibit 10-fold increases in hexose transport rates
within 30 min of the addition of 100 nM insulin, were utilized. Exposure of
these cells to 300 microM anisomycin or 500 microM cycloheximide caused a
maximal, 7-fold increase in 2-deoxyglucose transport rate after 4-8 h. The
effects due to either insulin (0.5 h) or anisomycin (5 h) on the kinetics
of zero-trans 3-O- methyl[14C]glucose transport were similar, resulting in
2.5-3-fold increases in apparent Vmax values (control Vmax = 1.6 +/- 0.3 x
10(-7) mmol/s/10(6) cells) coupled with approximately 2-fold decreases in
apparent Km values (control Km = 23 +/- 3.3 mM). Insulin elicited the
expected increases in plasma membrane levels of HepG2/erythrocyte (GLUT1)
and muscle/adipocyte (GLUT4) transporters (1.6- and 2.8-fold, respectively)
as determined by protein immunoblotting. In contrast, neither total
cellular contents nor plasma membrane levels of these two transporter
isoforms were increased when 3T3-L1 adipocytes were treated with either
anisomycin or cycloheximide. 3-[125I]Iodo-4-
azidophenethylamido-7-O-succinyldeacetylforskoli n labeling of glucose
transporters in plasma membrane fractions of similarly treated cells was
also unaffected by these agents. Thus, a striking discrepancy was observed
between the marked increase in cellular hexose transport rates due to these
protein synthesis inhibitors and the unaltered amounts of glucose
transporter proteins in the plasma membrane fraction. These data indicate
that short-term protein synthesis inhibition in 3T3-L1 adipocytes leads to
large increases in the intrinsic catalytic activity of one or both of the
GLUT1 and GLUT4 transporter isoforms.
Protein synthesis inhibitors activate glucose transport without increasing plasma membrane glucose transporters in 3T3-L1 adipocytes
Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.
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