Stimulation of AMP-activated protein kinase and enhancement of basal glucose uptake in muscle cells by quercetin and quercetin glycosides, active principles of the antidiabetic medicinal plant Vaccinium vitis-idaea

2010 ◽  
Vol 54 (7) ◽  
pp. 991-1003 ◽  
Author(s):  
Hoda M. Eid ◽  
Louis C. Martineau ◽  
Ammar Saleem ◽  
Asim Muhammad ◽  
Diane Vallerand ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Medicinal Plant ◽  
Glucose Uptake ◽  
Muscle Cells ◽  
Quercetin Glycosides ◽  
Amp Activated Protein Kinase ◽  
Basal Glucose Uptake ◽  
Stimulation Of

Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells

2002 ◽  
Vol 363 (1) ◽  
pp. 167-174 ◽  
Author(s):  
Lee G.D. FRYER ◽  
Fabienne FOUFELLE ◽  
Kay BARNES ◽  
Stephen A. BALDWIN ◽  
Angela WOODS ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Glucose Transport ◽  
Phorbol Ester ◽  
Hyperosmotic Stress ◽  
Amp Activated Protein Kinase ◽  
Stimulation Of ◽  
Constitutively Active

Stimulation of AMP-activated protein kinase (AMPK) in skeletal muscle has been correlated with an increase in glucose transport. Here, we demonstrate that adenoviral-mediated expression of a constitutively active mutant of AMPKα leads to activation of glucose transport in a skeletal-muscle cell line, similar to that seen following treatment with 5-amino-imidazolecarboxamide (AICA) riboside, hyperosmotic stress or insulin. In contrast, expression of a dominant-negative form of AMPK blocked the stimulation of glucose transport by both AICA riboside and hyperosmotic stress, but was without effect on either insulin or phorbol-ester-stimulated transport. These results demonstrate that activation of AMPK is sufficient for stimulation of glucose uptake into muscle cells, and is a necessary component of the AICA riboside- and hyperosmotic-stress-induced pathway leading to increased glucose uptake. On the other hand, AMPK is not required in the insulin- or phorbol-ester-mediated pathways. Long-term (5 days) expression of the constitutively active AMPK mutant increased protein expression of GLUT1, GLUT4 and hexokinase II, consistent with previous reports on the chronic treatment of rats with AICA riboside. Expression of constitutively active AMPK had no detectable effect on p38 mitogen-activated protein kinase levels, although interestingly the level of protein kinase B was decreased. These results demonstrate that long-term activation of AMPK is sufficient to cause increased expression of specific proteins in muscle. Our results add further support to the hypothesis that long-term activation of AMPK is involved in the adaptive response of muscle to exercise training.

Rapid stimulation of glucose transport by mitochondrial uncoupling depends in part on cytosolic Ca2+ and cPKC

1998 ◽  
Vol 275 (6) ◽  
pp. C1487-C1497 ◽  
Author(s):  
Zayna A. Khayat ◽  
Theodoros Tsakiridis ◽  
Atsunori Ueyama ◽  
Romel Somwar ◽  
Yousuke Ebina ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Glucose Transport ◽  
Energy Demand ◽  
Plasma Membranes ◽  
Muscle Cells ◽  
Atp Production ◽  
Pkc Β ◽  
Stimulation Of

2,4-Dinitrophenol (DNP) uncouples the mitochondrial oxidative chain from ATP production, preventing oxidative metabolism. The consequent increase in energy demand is, however, contested by cells increasing glucose uptake to produce ATP via glycolysis. In L6 skeletal muscle cells, DNP rapidly doubles glucose transport, reminiscent of the effect of insulin. However, glucose transport stimulation by DNP does not require insulin receptor substrate-1 phosphorylation and is wortmannin insensitive. We report here that, unlike insulin, DNP does not activate phosphatidylinositol 3-kinase, protein kinase B/Akt, or p70 S6 kinase. However, chelation of intra- and extracellular Ca2+ with 1,2-bis(2-aminophenoxy)ethane- N, N, N′, N′-tetraacetic acid-AM in conjunction with EGTA inhibited DNP-stimulated glucose uptake by 78.9 ± 3.5%. Because Ca2+-sensitive, conventional protein kinase C (cPKC) can activate glucose transport in L6 muscle cells, we examined whether cPKC may be translocated and activated in response to DNP in L6 myotubes. Acute DNP treatment led to translocation of cPKCs to plasma membrane. cPKC immunoprecipitated from plasma membranes exhibited a twofold increase in kinase activity in response to DNP. Overnight treatment with 4-phorbol 12-myristate 13-acetate downregulated cPKC isoforms α, β, and γ and partially inhibited (45.0 ± 3.6%) DNP- but not insulin-stimulated glucose uptake. Consistent with this, the PKC inhibitor bisindolylmaleimide I blocked PKC enzyme activity at the plasma membrane (100%) and inhibited DNP-stimulated 2-[3H]deoxyglucose uptake (61.2 ± 2.4%) with no effect on the stimulation of glucose transport by insulin. Finally, the selective PKC-β inhibitor LY-379196 partially inhibited DNP effects on glucose uptake (66.7 ± 1.6%). The results suggest interfering with mitochondrial ATP production acts on a signal transduction pathway independent from that of insulin and partly mediated by Ca2+ and cPKCs, of which PKC-β likely plays a significant role.

Osthole Enhances Glucose Uptake through Activation of AMP-Activated Protein Kinase in Skeletal Muscle Cells

2011 ◽  
Vol 59 (24) ◽  
pp. 12874-12881 ◽  
Author(s):  
Wei-Hwa Lee ◽  
Ren-Jye Lin ◽  
Shyr-Yi Lin ◽  
Yu-Chien Chen ◽  
Hsiu-Ming Lin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Amp Activated Protein Kinase
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