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Department of Internal Medicine, University of South Florida College of Medicine; and James A. Haley Veterans Administration Medical Center, Tampa, Florida 33612
Considerable evidence suggests that
atypical protein kinase C isoforms (aPKCs), serving downstream of
insulin receptor substrates and phosphatidylinositol (PI) 3-kinase, are
required for insulin-stimulated glucose transport in skeletal muscle
and adipocytes. More recent findings further suggest that aPKCs are
activated and required for glucose transport responses while serving
downstream of 1) proline-rich tyrosine kinase-2,
extracellular signal-regulated kinase, and phospholipase D, as during
the actions of high concentrations of carbohydrates (glucose, sorbitol)
and agents that activate 5'-AMP-activated protein kinase (exercise,
5-amino-imidazole-4-carboxamide-1-
-D-riboside, dinitrophenol), and 2) Cbl-dependent PI 3-kinase, as during
the action of insulin-sensitizing thiazolidinediones. It therefore seems reasonable to postulate that, regardless of the initial mechanism, aPKCs may serve as terminal molecular switches for activating glucose transport responses. This postulation is of critical
importance, as it now appears that insulin-stimulated aPKC activation
is compromised in various states of insulin resistance.
glucose transport; insulin signaling; protein kinase C-
; protein
kinase C-
; insulin receptor substrate-1; phosphatidylinositol
3-kinase; skeletal muscle; adipocytes; exercise; 5-amino-imidazole-4-carboxamide-1--D-riboside; thiazolidinediones; glucose; sorbitol; insulin resistance; type 2 diabetes mellitus; obesity; embryonic stem cells
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