The role of phospholipase D in Glut-4 translocation

2003 ◽  
Vol 19 (6) ◽  
pp. 456-463 ◽  
Author(s):  
Ping Huang ◽  
Michael A. Frohman
Keyword(s):  
Phospholipase D ◽  
Glut 4 ◽  
Glut 4 Translocation

scholarly journals Insulin-Like Growth Factor (IGF) Binding Protein-2, Independently of IGF-1, Induces GLUT-4 Translocation and Glucose Uptake in 3T3-L1 Adipocytes

2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
Biruhalem Assefa ◽  
Ayman M. Mahmoud ◽  
Andreas F. H. Pfeiffer ◽  
Andreas L. Birkenfeld ◽  
Joachim Spranger ◽  
...  
Keyword(s):  
Growth Factor ◽  
Glucose Uptake ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Glut 4 ◽  
Igf Binding ◽  
Glut 4 Translocation ◽  
Igf Binding Protein ◽  
The Impact

Insulin-like growth factor binding protein-2 (IGFBP-2) is the predominant IGF binding protein produced during adipogenesis and is known to increase the insulin-stimulated glucose uptake (GU) in myotubes. We investigated the IGFBP-2-induced changes in basal and insulin-stimulated GU in adipocytes and the underlying mechanisms. We further determined the role of insulin and IGF-1 receptors in mediating the IGFBP-2 and the impact of IGFBP-2 on the IGF-1-induced GU. Fully differentiated 3T3-L1 adipocytes were treated with IGFBP-2 in the presence and absence of insulin and IGF-1. Insulin, IGF-1, and IGFBP-2 induced a dose-dependent increase in GU. IGFBP-2 increased the insulin-induced GU after long-term incubation. The IGFBP-2-induced impact on GU was neither affected by insulin or IGF-1 receptor blockage nor by insulin receptor knockdown. IGFBP-2 significantly increased the phosphorylation of PI3K, Akt, AMPK, TBC1D1, and PKCζ/λand induced GLUT-4 translocation. Moreover, inhibition of PI3K and AMPK significantly reduced IGFBP-2-stimulated GU. In conclusion, IGFBP-2 stimulates GU in 3T3-L1 adipocytes through activation of PI3K/Akt, AMPK/TBC1D1, and PI3K/PKCζ/λ/GLUT-4 signaling. The stimulatory effect of IGFBP-2 on GU is independent of its binding to IGF-1 and is possibly not mediated through the insulin or IGF-1 receptor. This study highlights the potential role of IGFBP-2 in glucose metabolism.

Decreased insulin-stimulated GLUT-4 translocation in glycogen-supercompensated muscles of exercised rats

1999 ◽  
Vol 276 (5) ◽  
pp. E907-E912 ◽  
Author(s):  
Kentaro Kawanaka ◽  
Dong-Ho Han ◽  
Lorraine A. Nolte ◽  
Polly A. Hansen ◽  
Akira Nakatani ◽  
...  
Keyword(s):  
Cell Surface ◽  
Glucose Transport ◽  
Biosynthetic Pathway ◽  
Glycogen Content ◽  
Hexosamine Biosynthetic Pathway ◽  
Glut 4 ◽  
Glut 4 Translocation ◽  
Insulin Responsiveness ◽  
Exercise Induced

It was recently found that the effect of an exercise-induced increase in muscle GLUT-4 on insulin-stimulated glucose transport is masked by a decreased responsiveness to insulin in glycogen-supercompensated muscle. We evaluated the role of hexosamines in this decrease in insulin responsiveness and found that UDP- N-acetyl hexosamine concentrations were not higher in glycogen-supercompensated muscles than in control muscles with a low glycogen content. We determined whether the smaller increase in glucose transport is due to translocation of fewer GLUT-4 to the cell surface with the 2- N-4-(1-azi-2,2,2-trifluroethyl)-benzoyl-1,3-bis(d-mannose-4-yloxy)-2-propylamine (ATB-[2-3H]BMPA) photolabeling technique. The insulin-induced increase in GLUT-4 at the cell surface was no greater in glycogen-supercompensated exercised muscle than in muscles of sedentary controls and only 50% as great as in exercised muscles with a low glycogen content. We conclude that the decreased insulin responsiveness of glucose transport in glycogen-supercompensated muscle is not due to increased accumulation of hexosamine biosynthetic pathway end products and that the smaller increase in glucose transport is mediated by translocation of fewer GLUT-4 to the cell surface.

scholarly journals Role of PDE3B in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis in primary rat adipocytes

2006 ◽  
Vol 18 (3) ◽  
pp. 382-390 ◽  
Author(s):  
Emilia Zmuda-Trzebiatowska ◽  
Alina Oknianska ◽  
Vincent Manganiello ◽  
Eva Degerman
Keyword(s):  
Glucose Uptake ◽  
Rat Adipocytes ◽  
Glut 4 ◽  
Glut 4 Translocation

GLUT-4 translocation in skeletal muscle studied with a cell-free assay: involvement of phospholipase D

2001 ◽  
Vol 281 (3) ◽  
pp. E608-E618 ◽  
Author(s):  
Søren Kristiansen ◽  
Jakob N. Nielsen ◽  
Sylvain Bourgoin ◽  
Amira Klip ◽  
Michel Franco ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ammonium Sulfate ◽  
Phospholipase D ◽  
Membrane Structures ◽  
Receptor Proteins ◽  
Glut 4 ◽  
Unstimulated Control ◽  
A Cell ◽  
Glut 4 Translocation

GLUT-4-containing membranes immunoprecipitated from insulin-stimulated rat skeletal muscle produce the phospholipase D (PLD) product phosphatidic acid. In vitro stimulation of PLD in crude membrane with ammonium sulfate (5 mM) resulted in transfer of GLUT-4 (3.0-fold vs. control) as well as transferrin receptor proteins from large to small membrane structures. The in vitro GLUT-4 transfer could be blocked by neomycin (a PLD inhibitor), and neomycin also reduced insulin-stimulated glucose transport in intact incubated soleus muscles. Furthermore, protein kinase Bβ (PKBβ) was found to associate with the GLUT-4 protein and was transferred to small vesicles in response to ammonium sulfate in vitro. Finally, addition of cytosolic proteins, prepared from basal skeletal muscle, and GTP nucleotides to an enriched GLUT-4 membrane fraction resulted in in vitro transfer of GLUT-4 to small membranes (6.8-fold vs. unstimulated control). The cytosol and nucleotide-induced GLUT-4 transfer could be blocked by neomycin and N-ethylmaleimide. In conclusion, we have developed a cell-free assay that demonstrates in vitro GLUT-4 transfer. This transfer may suggest release of GLUT-4-containing vesicles from donor GLUT-4 membranes involving PLD activity and binding of PKBβ to GLUT-4.

scholarly journals Redox regulation of ischemic preconditioning is mediated by the differential activation of caveolins and their association with eNOS and GLUT-4

2007 ◽  
Vol 292 (5) ◽  
pp. H2060-H2072 ◽  
Author(s):  
Srikanth Koneru ◽  
Suresh Varma Penumathsa ◽  
Mahesh Thirunavukkarasu ◽  
Samson Mathews Samuel ◽  
Lijun Zhan ◽  
...  
Keyword(s):  
Ischemic Preconditioning ◽  
Redox Regulation ◽  
Ischemia Reperfusion ◽  
Free Radical Scavenger ◽  
Radical Scavenger ◽  
Glut 4 ◽  
Glut 4 Translocation ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Reactive oxygen species (ROS) generated during ischemia-reperfusion (I/R) enhance myocardial injury, but brief periods of myocardial ischemia followed by reperfusion [ischemic preconditioning (IP)] induce cardioprotection. Ischemia is reported to stimulate glucose uptake through the translocation of GLUT-4 from the intracellular vesicles to the sarcolemma. In the present study we demonstrated involvement of ROS in IP-mediated GLUT-4 translocation along with increased expression of caveolin (Cav)-3, phospho (p)-endothelial nitric oxide synthase (eNOS), p-Akt, and decreased expression of Cav-1. The rats were divided into the following groups: 1) control sham, 2) N-acetyl-l-cysteine (NAC, free radical scavenger) sham (NS), 3) I/R, 4) IP + I/R (IP), and 5) NAC + IP (IPN). IP was performed by four cycles of 4 min of ischemia and 4 min of reperfusion followed by 30 min of ischemia and 3, 24, 48 h of reperfusion, depending on the protocol. Increased mRNA expression of GLUT-4 and Cav-3 was observed after 3 h of reperfusion in the IP group compared with other groups. IP increased expression of GLUT-4, Cav-3, and p-AKT and p-eNOS compared with I/R. Coimmunoprecipitation demonstrated decreased association of Cav-1/eNOS in the IP group compared with the I/R group. Significant GLUT-4 and Cav-3 association was also observed in the IP group. This association was disrupted when NAC was used in conjunction with IP. It clearly documents a significant role of ROS signaling in Akt/eNOS/Cav-3-mediated GLUT-4 translocation and association in IP myocardium. In conclusion, we demonstrated a novel redox mechanism in IP-induced eNOS and GLUT-4 translocation and the role of caveolar paradox in making the heart euglycemic during the process of ischemia, leading to myocardial protection in a clinically relevant rat ischemic model.

scholarly journals Potential Role of Protein Kinase B in Glucose Transporter 4 Translocation in Adipocytes*

Endocrinology ◽  
1997 ◽  
Vol 138 (5) ◽  
pp. 2005-2010 ◽  
Author(s):  
Jean-François Tanti ◽  
Sophie Grillo ◽  
Thierry Grémeaux ◽  
Paul J. Coffer ◽  
Emmanuel Van Obberghen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Okadaic Acid ◽  
Potential Role ◽  
Glucose Transporter ◽  
Protein Kinase B ◽  
Glucose Transporter 4 ◽  
Glut 4 ◽  
Glut 4 Translocation

Abstract Phosphatidylinositol 3-kinase (PI 3-kinase) activation promotes glucose transporter 4 (Glut 4) translocation in adipocytes. In this study, we demonstrate that protein kinase B, a serine/threonine kinase stimulated by PI 3-kinase, is activated by both insulin and okadaic acid in isolated adipocytes, in parallel with their effects on Glut 4 translocation. In 3T3-L1 adipocytes, platelet-derived growth factor activated PI 3-kinase as efficiently as insulin but was only half as potent as insulin in promoting protein kinase B (PKB) activation. To look for a potential role of PKB in Glut 4 translocation, adipocytes were transfected with a constitutively active PKB (Gag-PKB) together with an epitope tagged transporter (Glut 4 myc). Gag-PKB was associated with all membrane fractions, whereas the endogenous PKB was mostly cytosolic. Expression of Gag-PKB led to an increase in Glut 4 myc amount at the cell surface. Our results suggest that PKB could play a role in promoting Glut 4 appearance at the cell surface following exposure of adipocytes to insulin and okadaic acid stimulation.

scholarly journals Specificity of Loxosceles α Clade Phospholipase D Enzymes for Choline-Containing Lipids: Role of a Conserved Aromatic Cage

2021 ◽  
Vol 120 (3) ◽  
pp. 234a
Author(s):  
Emmanuel E. Moutoussamy ◽  
Qaiser Waheed ◽  
Greta Binford ◽  
Matthew Cordes ◽  
Hanif Muhammad Khan ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Aromatic Cage

Role of Phospholipase D Activation in Nervous System Physiology and Pathophysiology

2002 ◽  
Vol 65 (4) ◽  
pp. 1445-1455 ◽  
Author(s):  
Jochen Klein ◽  
Vered Chalifa ◽  
Mordechai Liscovitch ◽  
Konrad Löffelholz
Keyword(s):  
Nervous System ◽  
Phospholipase D ◽  
System Physiology

scholarly journals Targeting of Protein Kinase C-ϵ during Fcγ Receptor-dependent Phagocytosis Requires the ϵC1B Domain and Phospholipase C-γ1

2006 ◽  
Vol 17 (2) ◽  
pp. 799-813 ◽  
Author(s):  
Keylon L. Cheeseman ◽  
Takehiko Ueyama ◽  
Tanya M. Michaud ◽  
Kaori Kashiwagi ◽  
Demin Wang ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Phospholipase D ◽  
Fluorescent Protein ◽  
Wild Type ◽  
Fcγ Receptor ◽  
Kinase C ◽  
Green Fluorescent

Protein kinase C-ϵ (PKC-ϵ) translocates to phagosomes and promotes uptake of IgG-opsonized targets. To identify the regions responsible for this concentration, green fluorescent protein (GFP)-protein kinase C-ϵ mutants were tracked during phagocytosis and in response to exogenous lipids. Deletion of the diacylglycerol (DAG)-binding ϵC1 and ϵC1B domains, or the ϵC1B point mutant ϵC259G, decreased accumulation at phagosomes and membrane translocation in response to exogenous DAG. Quantitation of GFP revealed that ϵC259G, ϵC1, and ϵC1B accumulation at phagosomes was significantly less than that of intact PKC-ϵ. Also, the DAG antagonist 1-hexadecyl-2-acetyl glycerol (EI-150) blocked PKC-ϵ translocation. Thus, DAG binding to ϵC1B is necessary for PKC-ϵ translocation. The role of phospholipase D (PLD), phosphatidylinositol-specific phospholipase C (PI-PLC)-γ1, and PI-PLC-γ2 in PKC-ϵ accumulation was assessed. Although GFP-PLD2 localized to phagosomes and enhanced phagocytosis, PLD inhibition did not alter target ingestion or PKC-ϵ localization. In contrast, the PI-PLC inhibitor U73122 decreased both phagocytosis and PKC-ϵ accumulation. Although expression of PI-PLC-γ2 is higher than that of PI-PLC-γ1, PI-PLC-γ1 but not PI-PLC-γ2 consistently concentrated at phagosomes. Macrophages from PI-PLC-γ2-/-mice were similar to wild-type macrophages in their rate and extent of phagocytosis, their accumulation of PKC-ϵ at the phagosome, and their sensitivity to U73122. This implicates PI-PLC-γ1 as the enzyme that supports PKC-ϵ localization and phagocytosis. That PI-PLC-γ1 was transiently tyrosine phosphorylated in nascent phagosomes is consistent with this conclusion. Together, these results support a model in which PI-PLC-γ1 provides DAG that binds to ϵC1B, facilitating PKC-ϵ localization to phagosomes for efficient IgG-mediated phagocytosis.

Sign in / Sign up

Export Citation Format

Share Document