Caffeine acutely activates 5′adenosine monophosphate–activated protein kinase and increases insulin-independent glucose transport in rat skeletal muscles

Egawa, Tatsuro; Hamada, Taku; Kameda, Naoko; Karaike, Kouhei; Ma, Xiao; Masuda, Shinji; Iwanaka, Nobumasa; Hayashi, Tatsuya

doi:10.1016/j.metabol.2009.05.013

Cited by 75 publications

(90 citation statements)

References 40 publications

(75 reference statements)

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“…It has been shown by us and others that caffeine-induced increases in Ca 2ϩ signaling regulate substrate metabolism, possibly via AMPK activation (1,6,22,35). Indeed, we have shown that when CaMKII or CaMKK was inhibited during caffeine stimulation, there were subsequent decreases in AMPK␣ 2 activity along with decreases in the rates of FA uptake, glucose uptake, and FA oxidation (1,35).…”

Section: Discussionmentioning

confidence: 57%

AMPKα₂deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

Abbott

Bogachus²,

Turcotte

2011

Journal of Applied Physiology

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Abbott MJ, Bogachus LD, Turcotte LP. AMPK␣2 deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle. J Appl Physiol 111: 125-134, 2011. First published May 5, 2011 doi:10.1152/japplphysiol.00807.2010.-AMP-activated protein kinase (AMPK) is a fuel sensor in skeletal muscle with multiple downstream signaling targets that may be triggered by increases in intracellular Ca 2ϩ concentration ([Ca 2ϩ ]). The purpose of this study was to determine whether increases in intracellular [Ca 2ϩ ] induced by caffeine act solely via AMPK␣ 2 and whether AMPK␣2 is essential to increase glucose uptake, fatty acid (FA) uptake, and FA oxidation in contracting skeletal muscle. Hindlimbs from wild-type (WT) or AMPK␣ 2 dominant-negative (DN) transgene mice were perfused during rest (n ϭ 11), treatment with 3 mM caffeine (n ϭ 10), or muscle contraction (n ϭ 11). Time-dependent effects on glucose and FA uptake were uncovered throughout the 20-min muscle contraction perfusion period (P Ͻ 0.05). Glucose uptake rates did not increase in DN mice during muscle contraction until the last 5 min of the protocol (P Ͻ 0.05). FA uptake rates were elevated at the onset of muscle contraction and diminished by the end of the protocol in DN mice (P Ͻ 0.05). FA oxidation rates were abolished in the DN mice during muscle contraction (P Ͻ 0.05). The DN transgene had no effect on caffeine-induced FA uptake and oxidation (P Ͼ 0.05). Glucose uptake rates were blunted in caffeine-treated DN mice (P Ͻ 0.05). The DN transgene resulted in a greater use of intramuscular triglycerides as a fuel source during muscle contraction. The DN transgene did not alter caffeine-or contraction-mediated changes in the phosphorylation of Ca 2ϩ /calmodulin-dependent protein kinase I or ERK1/2 (P Ͼ 0.05). These data suggest that AMPK␣ 2 is involved in the regulation of substrate uptake in a time-dependent manner in contracting muscle but is not necessary for regulation of FA uptake and oxidation during caffeine treatment. ERK1/2; muscle contraction; caffeine; calcium/calmodulin-dependent protein kinase kinase; acetyl-CoA carboxylase EVIDENCE SUGGESTS THAT MULTIPLE cellular signals regulate the changes in substrate metabolism with muscle contraction, including the AMP-activated protein kinase (AMPK) signaling cascade (2, 34, 35, 52). During states of low energy, such as muscle contraction or exercise, it is widely accepted that liver kinase B1 (LKB1) acts as an upstream AMPK kinase that phosphorylates and activates AMPK and initiates a multitude of signaling events to maintain energy homeostasis (39 -41). Although strong evidence indicates that the LKB1-AMPK cascade is a key signaling pathway that regulates changes in glucose uptake, fatty acid (FA) uptake, and FA oxidation in contracting skeletal muscle (16,25,54,56), data also show that AMPK may not be the sole signal mediating contractioninduced changes in glucose uptake, FA uptake, and FA oxidation (35,36,56).Along with AMPK, mounting data suggest that increas...

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Section: Discussionmentioning

confidence: 57%

AMPKα₂deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

Abbott

Bogachus²,

Turcotte

2011

Journal of Applied Physiology

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“…Our results suggest that caffeine administration restored Glut4 expression in the elderly group, but it was not able to increase Glut4 expression above a maximal level in the 12 M group. The mechanism by which caffeine increases Glut4 expression is still unclear, but the effect appears to be extant to several cell types: rat skeletal muscle primary cultures (Egawa et al 2009) and myoblasts (Mukwevho et al 2008), although contrasting results have been obtained in adipose tissue cells where caffeine suppressed insulininduced Glut4 translocation (Akiba et al 2004). …”

Section: Discussionmentioning

confidence: 99%

“…AMPK also decreases hepatic glucose production and increases glucose uptake in skeletal muscle, playing an important role in glucose homeostasis, and AMPK activation in the pancreatic beta cell decreases insulin secretion (Long and Zierath 2006). Recently, it has been shown that caffeine can increase Glut4 mRNA in skeletal muscle cells and insulinindependent glucose transport through an AMPKmediated process (Egawa et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Chronic caffeine intake reverses age-induced insulin resistance in the rat: effect on skeletal muscle Glut4 transporters and AMPK activity

Ribeiro¹,

Sacramento²,

Conde³

2012

AGE

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The role of caffeine consumption on insulin action is still under debate. The hypothesis that chronic caffeine intake reverses aging-induced insulin resistance in the rat was tested in this work. The mechanism by which caffeine restores insulin sensitivity was also investigated. Six groups of rats were used: 3 months old (3 M), 3 months old caffeine-treated (3MCaf), 12 months old (12 M), 12 months old caffeine-treated (12MCaf), 24 months old (24 M), and 24 months old caffeinetreated (24MCaf). Caffeine was administered in drinking water (1 g/l) during 15 days. Insulin sensitivity was assessed by means of the insulin tolerance test. Blood pressure, body weight, visceral and total fat, fasting glycemia and insulinemia, plasma nonesterified fatty acids (NEFA), total antioxidant capacity (TAC), cortisol, nitric oxide, and catecholamines were monitored. Skeletal muscle Glut4 and 5′-AMP activated protein kinase (AMPK) protein expression and activity were also assessed. Aged rats exhibited diminished insulin sensitivity accompanied by hyperinsulinemia and normoglycemia, increased visceral and total fat, decreased TAC and plasma catecholamines, and also decreased skeletal muscle Glut4 and AMPK protein expression. Chronic caffeine intake restored insulin sensitivity and regularized circulating insulin and NEFA in both aging models. Caffeine neither modified skeletal muscle AMPK expression nor activity in aged rats; however, it decreased visceral and total fat in 12 M rats and it restored skeletal muscle Glut4 expression to control values in 24 M rats. We concluded that chronic caffeine intake reverses aging-induced insulin resistance in rats by decreasing NEFA production and also by increasing Glut4 expression in skeletal muscle.

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“…In ex vivo skeletal muscle incubation, some groups reported that caffeine decreased insulin sensitivity and glucose transport by inhibiting insulin signaling (16)(17)(18) (17). At present, there has been no report that caffeine has a positive effect on insulin signaling.…”

Section: Discussionmentioning

confidence: 99%

Coffee Improves Insulin-Stimulated Akt Phosphorylation in Liver and Skeletal Muscle in Diabetic KK-Ay Mice

Kobayashi

Matsuda

Iwai

et al. 2012

J Nutr Sci Vitaminol

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Caffeine acutely activates 5′adenosine monophosphate–activated protein kinase and increases insulin-independent glucose transport in rat skeletal muscles

Cited by 75 publications

References 40 publications

AMPKα₂deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

AMPKα₂deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

Chronic caffeine intake reverses age-induced insulin resistance in the rat: effect on skeletal muscle Glut4 transporters and AMPK activity

Coffee Improves Insulin-Stimulated Akt Phosphorylation in Liver and Skeletal Muscle in Diabetic KK-Ay Mice

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Caffeine acutely activates 5′adenosine monophosphate–activated protein kinase and increases insulin-independent glucose transport in rat skeletal muscles

Cited by 75 publications

References 40 publications

AMPKα2deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

AMPKα2deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

Chronic caffeine intake reverses age-induced insulin resistance in the rat: effect on skeletal muscle Glut4 transporters and AMPK activity

Coffee Improves Insulin-Stimulated Akt Phosphorylation in Liver and Skeletal Muscle in Diabetic KK-Ay Mice

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AMPKα₂deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle

AMPKα₂deficiency uncovers time dependency in the regulation of contraction-induced palmitate and glucose uptake in mouse muscle