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(Received for publication, August 5, 1996, and in revised form, January 15, 1997)
From the Klinisches Institut für Herzinfarktforschung an der
Medizinischen Universitätsklinik Heidelberg, Bergheimerstraße
58, Heidelberg 69115, Germany
Human fat cells possess a multireceptor-linked
H2O2-generating system that is activated
by insulin. Previous studies revealed that manganese was the sole
cofactor required for a hormonal regulation of
NADPH-dependent H2O2 generation
in vitro. In this report it is shown that the synergistic
activation of NADPH-dependent H2O2 generation by Mn2+ and insulin was blocked by GDP Consistently, manganese could be replaced by micromolar concentrations
of GTP The insulin receptor and Gi were co-adsorbed on
anti-G
Volume 272, Number 15,
Issue of April 11, 1997
pp. 10135-10143
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
i2
S
(guanosine 5
-O-(2-thiodiphosphate)), pertussis toxin and
COOH-terminal anti-G
i1-2 or the corresponding peptide.
S (guanosine 5-O-(3-thiotriphosphate)), which increased NADPH-dependent H2O2
generation by 20-40%. Insulin shifted the dose response curve for
GTPS to the left (>10-fold) and increased the maximal response. In
the presence of 10 µM GTPS, the hormone was active at
picomolar concentrations, indicating that insulin acted via its cognate
receptor.
i and anti-insulin receptor -subunit
(anti-IR) affinity columns. Partially purified insulin receptor
preparations contained Gs, Gi2, and
G (but no Gi1 or Gi3). The
functional nature of the insulin receptor-Gi2 complex was
made evident by insulin's ability to modulate labeling of
Gi by bacterial toxins. Insulin action was mimicked by
activated Gi, but not by Go or G,
indicating that insulin's signal was transduced via
Gi2. Thus, NADPH oxidase is the first example of an
effector system that is coupled to the insulin receptor via a
heterotrimeric G protein.
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