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  Protein kinase C-lambda knockout in embryonic stem cells and adipocytes impairs insulin-stimulated glucose transport

Bandyopadhyay, G., Standaert, M. L., Sajan, M. P., Kanoh, Y., Miura, A., Braun, U., et al. (2004). Protein kinase C-lambda knockout in embryonic stem cells and adipocytes impairs insulin-stimulated glucose transport. Molecular Endocrinology, 18(2), 373-383. Retrieved from http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14615604.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-EE65-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E541-E
Genre: Journal Article

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 Creators:
Bandyopadhyay, G., Author
Standaert, M. L., Author
Sajan, M. P., Author
Kanoh, Y., Author
Miura, A., Author
Braun, U., Author
Kruse, F., Author
Leitges, M.1, Author              
Farese, R. V., Author
Affiliations:
1Department of Genes and Behavior, MPI for biophysical chemistry, Max Planck Society, ou_persistent34              

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Free keywords: 1-Phosphatidylinositol 3-Kinase/metabolism ; Adipocytes/drug effects/*metabolism ; Animals ; Biological Transport/drug effects ; Cell Differentiation/drug effects/physiology ; Cells, Cultured ; Deoxyglucose/pharmacokinetics ; Embryo/cytology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Glucose/*metabolism ; Insulin/*metabolism/pharmacology ; Mice ; Mice, Knockout ; Mitogen-Activated Protein Kinases/metabolism ; Monosaccharide Transport Proteins/metabolism ; Phospholipase D/antagonists & inhibitors/metabolism ; Protein Kinase C/*genetics/metabolism ; Protein-Tyrosine Kinase/drug effects/metabolism ; Receptor, Insulin/metabolism ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Signal Transduction ; Stem Cells/drug effects/*metabolism
 Abstract: Atypical protein kinase C (aPKC) isoforms have been suggested to mediate insulin effects on glucose transport in adipocytes and other cells. To more rigorously test this hypothesis, we generated mouse embryonic stem (ES) cells and ES-derived adipocytes in which both aPKC-lambda alleles were knocked out by recombinant methods. Insulin activated PKC-lambda and stimulated glucose transport in wild-type (WT) PKC-lambda(+/+), but not in knockout PKC-lambda(-/-), ES cells. However, insulin-stimulated glucose transport was rescued by expression of WT PKC-lambda in PKC-lambda(-/-) ES cells. Surprisingly, insulin-induced increases in both PKC-lambda activity and glucose transport were dependent on activation of proline-rich tyrosine protein kinase 2, the ERK pathway, and phospholipase D (PLD) but were independent of phosphatidylinositol 3-kinase (PI3K) in PKC-lambda(+/+) ES cells. Interestingly, this dependency was completely reversed after differentiation of ES cells to adipocytes, i.e. insulin effects on PKC-lambda and glucose transport were dependent on PI3K, rather than proline-rich tyrosine protein kinase 2/ERK/PLD. As in ES cells, insulin effects on glucose transport were absent in PKC-lambda(-/-) adipocytes but were rescued by expression of WT PKC-lambda in these adipocytes. Our findings suggest that insulin activates aPKCs and glucose transport in ES cells by a newly recognized PI3K-independent ERK/PLD-dependent pathway and provide a compelling line of evidence suggesting that aPKCs are required for insulin-stimulated glucose transport, regardless of whether aPKCs are activated by PI3K-dependent or PI3K-independent mechanisms.

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Language(s): eng - English
 Dates: 2004-02
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Molecular Endocrinology
Source Genre: Journal
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Pages: - Volume / Issue: 18 (2) Sequence Number: - Start / End Page: 373 - 383 Identifier: -