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Full-Text Articles in Translational Medical Research
The Translational Regulation Of Lipoprotein Lipase By Epinephrine Involves An Rna Binding Complex Including The Catalytic Subunit Of Protein Kinase A, Gouri Ranganathan, Dan Phan, Irina D. Pokrovskaya, Joan E. Mcewen, Chunling Li, Philip A. Kern
The Translational Regulation Of Lipoprotein Lipase By Epinephrine Involves An Rna Binding Complex Including The Catalytic Subunit Of Protein Kinase A, Gouri Ranganathan, Dan Phan, Irina D. Pokrovskaya, Joan E. Mcewen, Chunling Li, Philip A. Kern
Clinical and Translational Science Faculty Publications
The balance of lipid flux in adipocytes is controlled by the opposing actions of lipolysis and lipogenesis, which are controlled primarily by hormone-sensitive lipase and lipoprotein lipase (LPL), respectively. Catecholamines stimulate adipocyte lipolysis through reversible phosphorylation of hormone-sensitive lipase, and simultaneously inhibit LPL activity. However, LPL regulation is complex and previous studies have described translational regulation of LPL in response to catecholamines because of an RNA-binding protein that interacts with the 3′-untranslated region of LPL mRNA. In this study, we identified several protein components of an LPL RNA binding complex. Using an LPL RNA affinity column, we identified two of …
Regulation Of Lipoprotein Lipase By Protein Kinase Cα In 3t3-F442a Adipocytes, Gouri Ranganathan, Wei Song, Nicholas Dean, Brett Monia, Steven W. Barger, Philip A. Kern
Regulation Of Lipoprotein Lipase By Protein Kinase Cα In 3t3-F442a Adipocytes, Gouri Ranganathan, Wei Song, Nicholas Dean, Brett Monia, Steven W. Barger, Philip A. Kern
Clinical and Translational Science Faculty Publications
Lipoprotein lipase (LPL) is an important enzyme in adipocyte and lipid metabolism with complex cellular regulation. Previous studies demonstrated an inhibition of LPL activity and synthesis following depletion of protein kinase C (PKC) isoforms with long term treatment of 3T3-F442A adipocytes with 12-O-tetradecanoylphorbol-13-acetate. To identify the specific PKC isoforms involved, we treated cells with antisense oligonucleotides that block expression of specific PKC isoforms. An antisense oligonucleotide to PKCα inhibited LPL activity by 78 ± 8%, whereas antisense oligonucleotides directed against PKCδ or PKCε had no effect on LPL activity. The change in LPL activity was maximal at 72 …