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and Noninvolvement of Diacylglycerol-Sensitive PKCs in Insulin-Stimulated Glucose Transport in L6 Myotubes1
J. A. Haley Veterans Hospital and the Departments of Internal Medicine and Biochemistry/Molecular Biology (G.B., M.L.S., L.G., R.V.F.), University of South Florida College of Medicine, Tampa, Florida 33612; and Centro de Biologia Molecular "Severo Ochoa" (J.M.), Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain
Address all correspondence and requests for reprints to: Robert V. Farese, M.D., Research Service (VAR 151), J. A. Haley Veterans Hospital, 13000 Bruce Downs Boulevard, Tampa, Florida 33612.
We examined the question of whether insulin activates protein kinase C
(PKC)-
in L6 myotubes, and the dependence of this activation on
phosphatidylinositol (PI) 3-kinase. We also evaluated a number of
issues that are relevant to the question of whether diacylglycerol
(DAG)-dependent PKCs or DAG-insensitive PKCs, such as PKC-, are more
likely to play a role in insulin-stimulated glucose transport in L6
myotubes and other insulin-sensitive cell types. We found that insulin
increased the enzyme activity of immunoprecipitable PKC- in L6
myotubes, and this effect was blocked by PI 3-kinase inhibitors,
wortmannin and LY294002; this suggested that PKC- operates
downstream of PI 3-kinase during insulin action. We also found that
treatment of L6 myotubes with 5 µM tetradecanoyl
phorbol-13-acetate (TPA) for 24 h led to 80–100% losses of all
DAG-dependent PKCs (
, ß1, ß2, 
, 
)
and TPA-stimulated glucose transport (2-deoxyglucose uptake); in
contrast, there was full retention of PKC-, as well as
insulin-stimulated glucose transport and translocation of GLUT4 and
GLUT1 to the plasma membrane. Unlike what has been reported in BC3H-1
myocytes, TPA treatment did not elicit increases in PKCß2 messenger
RNA or protein in L6 myotubes, and selective retention of this PKC
isoform could not explain the retention of insulin effects on glucose
transport after prolonged TPA treatment. Of further interest, TPA
acutely activated membrane-associated PI 3-kinase in L6 myotubes, and
acute effects of TPA on glucose transport were inhibited, not only by
the PKC inhibitor, LY379196, but also by both wortmannin and LY294002;
this suggested that DAG-sensitive PKCs activate glucose transport
through cross-talk with phosphatidylinositol (PI) 3-kinase, rather than
directly through PKC. Also, the cell-permeable, myristoylated PKC-
pseudosubstrate inhibited insulin-stimulated glucose transport both in
non-down-regulated and PKC-depleted (TPA-treated) L6 myotubes; thus,
the PKC- pseudosubstrate appeared to inhibit a protein kinase that
is required for insulin-stimulated glucose transport but is distinct
from DAG-sensitive PKCs. In keeping with the latter dissociation of
DAG-sensitive PKCs and insulin-stimulated glucose transport, LY379196,
which inhibits PKC-ß (preferentially) and other DAG-sensitive PKCs at
relatively low concentrations, inhibited insulin-stimulated glucose
transport only at much higher concentrations, not only in L6 myotubes,
but also in rat adipocytes, BC3H-1 myocytes, 3T3/L1 adipocytes and rat
soleus muscles. Finally, stable and transient expression of a
kinase-inactive PKC- inhibited basal and insulin-stimulated glucose
transport in L6 myotubes. Collectively, our findings suggest that,
whereas PKC- is a reasonable candidate to participate in insulin
stimulation of glucose transport, DAG-sensitive PKCs are unlikely
participants.
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 L. M. NERI, A. M. MARTELLI, P. BORGATTI, M. L. COLAMUSSI, M. MARCHISIO, and S. CAPITANI Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-{zeta} translocation to the nucleus of NGF-treated PC12 cells FASEB J, December 1, 1999; 13(15): 2299 - 2310. [Abstract] [Full Text]
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M. P. Sajan, M. L. Standaert, G. Bandyopadhyay, M. J. Quon, T. R. Burke Jr., and R. V. Farese Protein Kinase C-zeta and Phosphoinositide-dependent Protein Kinase-1 Are Required for Insulin-induced Activation of ERK in Rat Adipocytes J. Biol. Chem., October 22, 1999; 274(43): 30495 - 30500. [Abstract] [Full Text] [PDF]
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