Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10765111 | Biochemical and Biophysical Research Communications | 2009 | 6 Pages |
Abstract
Functional adipocyte glucose disposal is a key component of global glucose homeostasis. PKCβII is involved in rat skeletal muscle cell ISGT. Western blot analysis and real-time PCR revealed 3T3-L1 cells developmentally regulated PKCβ splicing such that PKCβI was downregulated and PKCβII was upregulated during the course of differentiation. An initial glucose uptake screen using PKC inhibitor LY379196 pointed to a PKC isozyme other than PKCζ mediating 3T3-L1 adipocyte ISGT. Subsequent use of PKCβII inhibitor CGP53353 pointed to a role for PKCβII in ISGT. Western blot analysis showed that CGP53353 specifically inhibited phosphorylation of PKCβII Serine 660. Subcellular fractionation and immunofluorescence demonstrated that PKCβII regulates GLUT4 translocation. Further Western blot, immunofluorescence and co-immunoprecipitation analysis reveal that PKCβII inhibition does not affect mTORC2 activity yet abrogates phosphorylation of Akt Serine 473. PKCβII regulates GLUT4 translocation by regulating Akt phosphorylation and thus activity.
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Authors
E. Kleiman, G. Carter, T. Ghansah, N.A. Patel, D.R. Cooper,