Open Access. Powered by Scholars. Published by Universities.®
Translational Medical Research Commons™
Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 5 of 5
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 …
Lack Of Effect Of Leptin On Glucose Transport, Lipoprotein Lipase, And Insulin Action In Adipose And Muscle Cells, Subramanian Ranganathan, Theodore P. Ciaraldi, Robert R. Henry, Sunder Mudaliar, Philip A. Kern
Lack Of Effect Of Leptin On Glucose Transport, Lipoprotein Lipase, And Insulin Action In Adipose And Muscle Cells, Subramanian Ranganathan, Theodore P. Ciaraldi, Robert R. Henry, Sunder Mudaliar, Philip A. Kern
Clinical and Translational Science Faculty Publications
The effect of leptin on glucose transport, lipogenesis, and lipoprotein lipase activity was studied in cultured rat adipocytes and 3T3-L1 adipocytes. Leptin had no effect on basal and insulin stimulated glucose transport in isolated adipocytes from the rat and the genetically obese mouse. The incorporation of glucose into lipids was also unaffected. Lipoprotein lipase (LPL) activity remained unchanged in response to leptin in these cells, as well as in minced adipose tissue. Leptin also had no effect on both basal and insulin-stimulated glucose transport in cultured rat and human skeletal muscle cells. These studies showed that leptin had no effect …
1,25-Dihydroxyvitamin D Induces Lipoprotein Lipase Expression In 3t3-L1 Cells In Association With Adipocyte Differentiation, Diane Vu, John M. Ong, Thomas L. Clemens, Philip A. Kern
1,25-Dihydroxyvitamin D Induces Lipoprotein Lipase Expression In 3t3-L1 Cells In Association With Adipocyte Differentiation, Diane Vu, John M. Ong, Thomas L. Clemens, Philip A. Kern
Clinical and Translational Science Faculty Publications
1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] is known to modulate the development of hone and other mesenchymal cell types. Since osteoblasts and adipocytes are thought to arise in bone marrow from a common progenitor, this work examined the effects of 1,25-(OH)2D3 on adipocyte development, and in particular on the expression of lipoprotein lipase (LPL), which is an early marker for the differentiated adipocyte. 3T3-L1 preadipocytes were cultured in the presence of 1.25-(OH)2D3 (10-9 to 10-7 M) for up to 7 days. LPL activity was measured in the medium and cell …
Tissue-Specific Expression Of Human Lipoprotein Lipase: Effect Of The 3′-Untranslated Region On Translation, Gouri Ranganathan, John M. Ong, Ada Yukht, Mehrnoosh Saghizadeh, Rosa B. Simsolo, Andrea Pauer, Philip A. Kern
Tissue-Specific Expression Of Human Lipoprotein Lipase: Effect Of The 3′-Untranslated Region On Translation, Gouri Ranganathan, John M. Ong, Ada Yukht, Mehrnoosh Saghizadeh, Rosa B. Simsolo, Andrea Pauer, Philip A. Kern
Clinical and Translational Science Faculty Publications
Lipoprotein lipase (LPL) is a central enzyme in lipoprotein metabolism and is expressed predominantly in adipose tissue and muscle. In these tissues, the regulation of LPL is complex and often opposite in response to the same physiologic stimulus. In addition, much regulation of LPL occurs post-transcriptionally. The human LPL cDNA is characterized by a long 3′-untranslated region, which has two polyadenylation signals. In this report, human adipose tissue expressed two LPL mRNA species (3.2 and 3.6 kb) due to an apparent random choice of sites for mRNA polyadenylation, whereas human skeletal and heart muscle expressed predominantly the longer 3.6-kb mRNA …