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localization
Garvan Institute of Medical Research, Sydney, New South Wales 2010, Australia
Muscle insulin
resistance in the chronic high-fat-fed rat is associated with increased
membrane translocation and activation of the novel, lipid-responsive,
protein kinase C (nPKC) isozymes PKC-
and -
. Surprisingly,
fat-induced insulin resistance can be readily reversed by one
high-glucose low-fat meal, but the underlying mechanism is unclear.
Here, we have used this model to determine whether changes in the
translocation of PKC- and - are associated with the acute
reversal of insulin resistance. We measured cytosol and particulate
PKC-
and nPKC- and - in muscle in control chow-fed Wistar rats
(C) and 3-wk high-fat-fed rats with (HF-G) or without (HF-F) a single
high-glucose meal. PKC- and - were translocated to the membrane
in muscle of insulin-resistant HF-F rats. However, only membrane
PKC- was reduced to the level of chow-fed controls when insulin
resistance was reversed in HF-G rats [% PKC- at membrane,
23.0 ± 4.4% (C); 39.7 ± 3.4% (HF-F, P < 0.01 vs. C); 22.5 ± 2.7% (HF-G, P < 0.01 vs.
HF-F), by ANOVA]. We conclude that, although muscle localization of
both PKC- and PKC- are influenced by chronic dietary lipid
oversupply, PKC- and PKC- localization are differentially
influenced by acute withdrawal of dietary lipid. These results provide
further support for an association between PKC- muscle cellular
localization and lipid-induced muscle insulin resistance and stress the
labile nature of high-fat diet-induced insulin resistance in the rat.
high-fat-fed rat; glucose; long-chain acyl-coenzyme A
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