PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35282369-19 2022 Further cell experiments confirmed that BAIBA increased AMPK phosphorylation and had a cardioprotective effect on downstream fatty acid uptake, oxidative efficiency, and mitochondrial function, which was prevented by the AMPK inhibitor Compound C. Conclusion: Exercise-generated BAIBA can reduce cardiomyocyte metabolic stress and apoptosis induced by mitochondrial dysfunction through the miR-208b/AMPK pathway. Fatty Acids 125-135 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 221-225 31199141-8 2019 Adiponectin was then significantly upregulated probably via the gut-brain axis and further activated the AMPK signaling pathway to improve lipid metabolism including the improvement of lipolysis and fatty acid oxidation and the suppression of lipogenesis. Fatty Acids 199-209 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 105-109 33755174-6 2021 Furthermore, ERRalpha/PGC-1beta and their target genes MCAD and CPT-1 were increased and regulated by AMPK, which coincided with increased fatty acid oxidation (FAO) and autophagy in TAM-resistant cells. Fatty Acids 139-149 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 102-106 32918993-8 2021 Concomitantly, there was an increase in the expression levels of fatty acid-oxidizing enzymes (AMPKalpha2, ACOX, MCAD, and VLCAD) in the liver and skeletal muscle after ALS-L1023 treatment. Fatty Acids 65-75 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 95-105 32786868-7 2020 The results showed that 2% fermented soy paste decreased serum triacylglycerol (TG) and alanine aminotransferase (ALT) and reduced lipid accumulation in the liver through induced fatty acid oxidation by activating the adenosine 5"-monophosphate -activated protein kinase (AMPK) pathway and increasing PGC1alpha and CPT1alpha protein expression. Fatty Acids 179-189 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 218-270 31948527-14 2020 CONCLUSIONS: Early EGCG intervention can down-regulate the de novo synthesis of fatty acids through the Ampk/Srebf1 signaling pathway and reduce hepatic lipid accumulation in IUGR rats by improving insulin resistance of hepatocytes. Fatty Acids 80-91 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 104-108 31400234-0 2019 SIRT1 Activation Promotes beta-Cell Regeneration by Activating Endocrine Progenitor Cells via AMPK Signaling-Mediated Fatty Acid Oxidation. Fatty Acids 118-128 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 94-98 31400234-8 2019 Upregulation of NGN3 by SIRT1 activation was through stimulating AMP-activated protein kinase (AMPK) signaling-mediated fatty acid oxidation (FAO) in human pancreatic progenitor cells; AMPK inhibition abolished these effects. Fatty Acids 120-130 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 65-93 31400234-8 2019 Upregulation of NGN3 by SIRT1 activation was through stimulating AMP-activated protein kinase (AMPK) signaling-mediated fatty acid oxidation (FAO) in human pancreatic progenitor cells; AMPK inhibition abolished these effects. Fatty Acids 120-130 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 95-99 30140413-0 2018 The effects of ginsenoside Rb1 on fatty acid beta-oxidation, mediated by AMPK, in the failing heart. Fatty Acids 34-44 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 73-77 30770790-0 2019 Autoantibody against beta1-adrenoceptor promotes the differentiation of natural regulatory T cells from activated CD4+ T cells by up-regulating AMPK-mediated fatty acid oxidation. Fatty Acids 158-168 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 144-148 27827305-2 2017 We examined, in isolated muscle and cardiac myocytes, whether leptin, via AMP-activated protein kinase (AMPK) activation, stimulated fatty acid translocase (FAT/CD36)-mediated fatty acid uptake to enhance fatty acid oxidation. Fatty Acids 133-143 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 104-108 27827305-3 2017 In both mouse skeletal muscle and rat cardiomyocytes, leptin increased fatty acid oxidation, an effect that was blocked when AMPK phosphorylation was inhibited by adenine 9-beta-d-arabinofuranoside or Compound C. In wild-type mice, leptin induced the translocation of FAT/CD36 to the plasma membrane and increased fatty acid uptake into giant sarcolemmal vesicles and into cardiomyocytes. Fatty Acids 314-324 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 125-129 27827305-7 2017 Our studies have revealed a novel mechanism of leptin-induced fatty acid oxidation in muscle tissue; namely, this process is dependent on the activation of AMPK to induce the translocation of FAT/CD36 to the plasma membrane, thereby stimulating fatty acid uptake. Fatty Acids 62-72 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 156-160 27827305-7 2017 Our studies have revealed a novel mechanism of leptin-induced fatty acid oxidation in muscle tissue; namely, this process is dependent on the activation of AMPK to induce the translocation of FAT/CD36 to the plasma membrane, thereby stimulating fatty acid uptake. Fatty Acids 245-255 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 156-160 28142230-11 2018 CONCLUSIONS: CK improved glucose intolerance and hepatosteatosis in HFD-fed OLETF rats through AMPK activation, which has dual mode of action that involves decreasing the synthesis of fatty acids and increasing fatty acid oxidation. Fatty Acids 184-195 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 95-99 28142230-11 2018 CONCLUSIONS: CK improved glucose intolerance and hepatosteatosis in HFD-fed OLETF rats through AMPK activation, which has dual mode of action that involves decreasing the synthesis of fatty acids and increasing fatty acid oxidation. Fatty Acids 184-194 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 95-99 30453301-2 2018 AMP-activated protein kinase (AMPK), a key regulator of glucose and fatty acid metabolism, plays a major role in obesity and type 2 diabetes. Fatty Acids 68-78 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-28 30453301-2 2018 AMP-activated protein kinase (AMPK), a key regulator of glucose and fatty acid metabolism, plays a major role in obesity and type 2 diabetes. Fatty Acids 68-78 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 30-34 27827305-3 2017 In both mouse skeletal muscle and rat cardiomyocytes, leptin increased fatty acid oxidation, an effect that was blocked when AMPK phosphorylation was inhibited by adenine 9-beta-d-arabinofuranoside or Compound C. In wild-type mice, leptin induced the translocation of FAT/CD36 to the plasma membrane and increased fatty acid uptake into giant sarcolemmal vesicles and into cardiomyocytes. Fatty Acids 71-81 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 125-129 25535827-3 2015 Our data suggest that in pregnant rats, the hypothalamic fatty acid pathway shows an overall state that should lead to anorexia and elevated BAT thermogenesis: decreased activities of AMP-activated protein kinase (AMPK), FAS, and carnitine palmitoyltransferase 1, coupled with increased acetyl-CoA carboxylase function with subsequent elevation of malonyl-CoA levels. Fatty Acids 57-67 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 184-212 26007288-8 2015 The metabolic programming effects of GSPE that are related to the enhancement of fatty acid oxidation in skeletal muscle seem to be mediated, at least in part, by AMPK. Fatty Acids 81-91 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 163-167 26361764-6 2016 AMPK was induced in adipose tissue in rats that were treated with GT and likely restored insulin sensitivity, increased mRNA expression of GLUT4, reducing the concentrations of plasma and liver lipid content, also stimulating fatty acid oxidation in the same tissue. Fatty Acids 226-236 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-4 27602061-6 2016 It is hypothesized that fatty acid synthesis participates in autism through PI3K/Akt/FASN and AMPK/ACC pathways. Fatty Acids 24-34 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 94-98 25535827-3 2015 Our data suggest that in pregnant rats, the hypothalamic fatty acid pathway shows an overall state that should lead to anorexia and elevated BAT thermogenesis: decreased activities of AMP-activated protein kinase (AMPK), FAS, and carnitine palmitoyltransferase 1, coupled with increased acetyl-CoA carboxylase function with subsequent elevation of malonyl-CoA levels. Fatty Acids 57-67 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 214-218 21700905-1 2011 AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-alpha) are critical regulators of short-term and long-term fatty acid oxidation, respectively. Fatty Acids 154-164 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-28 25516653-6 2014 Accordingly, AMPK targets acetyl-CoA carboxylase and cyclic AMP response element binding protein are phosphorylated, with the concomitant carnitine palmitoyltransferase-1alpha (CPT-1alpha) activation and higher expression of peroxisome proliferator-activated receptor-gamma co-activator-1alpha and that of the fatty acid oxidation (FAO)-related enzymes CPT-1alpha, acyl-CoA oxidase 1, and acyl-CoA thioesterase 2. Fatty Acids 310-320 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 13-17 25127116-3 2014 Met has been shown to increase fatty acid oxidation, an effect mediated by AMP activated protein kinase (AMPK). Fatty Acids 31-41 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 75-103 25127116-3 2014 Met has been shown to increase fatty acid oxidation, an effect mediated by AMP activated protein kinase (AMPK). Fatty Acids 31-41 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 105-109 23626844-1 2013 BACKGROUND: Hypothalamic AMPK acts as a cell energy sensor and can modulate food intake, glucose homeostasis, and fatty acid biosynthesis. Fatty Acids 114-124 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 25-29 24665903-10 2014 In summary, ex229 efficiently activated skeletal muscle AMPK and elicited metabolic effects in muscle appropriate for treating Type 2 diabetes by stimulating glucose uptake and increasing fatty acid oxidation. Fatty Acids 188-198 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 56-60 23095119-2 2012 All three effects were blocked by the AMPK inhibitor Compound C, leading to the conclusion that in response to an increase in long-chain NEFA (non-esterified fatty acid) concentration AMPK mediated an enhancement of adipocyte glucose transport, thereby providing increased glycerol 3-phosphate for FA (fatty acid) esterification to TAG (triacylglycerol). Fatty Acids 158-168 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 38-42 23095119-2 2012 All three effects were blocked by the AMPK inhibitor Compound C, leading to the conclusion that in response to an increase in long-chain NEFA (non-esterified fatty acid) concentration AMPK mediated an enhancement of adipocyte glucose transport, thereby providing increased glycerol 3-phosphate for FA (fatty acid) esterification to TAG (triacylglycerol). Fatty Acids 158-168 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 184-188 23095119-2 2012 All three effects were blocked by the AMPK inhibitor Compound C, leading to the conclusion that in response to an increase in long-chain NEFA (non-esterified fatty acid) concentration AMPK mediated an enhancement of adipocyte glucose transport, thereby providing increased glycerol 3-phosphate for FA (fatty acid) esterification to TAG (triacylglycerol). Fatty Acids 302-312 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 38-42 23095119-2 2012 All three effects were blocked by the AMPK inhibitor Compound C, leading to the conclusion that in response to an increase in long-chain NEFA (non-esterified fatty acid) concentration AMPK mediated an enhancement of adipocyte glucose transport, thereby providing increased glycerol 3-phosphate for FA (fatty acid) esterification to TAG (triacylglycerol). Fatty Acids 302-312 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 184-188 21700905-14 2011 AMPK inhibition of PPAR-alpha and -gamma may allow for short-term processes to increase energy generation before the cells devote resources to increasing their capacity for fatty acid oxidation. Fatty Acids 173-183 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-4 21700905-1 2011 AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-alpha) are critical regulators of short-term and long-term fatty acid oxidation, respectively. Fatty Acids 154-164 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 30-34 19125418-1 2009 AMP-activated protein kinase (AMPK) is an intracellular fuel sensor that plays a key role in regulating fatty acid synthesis in liver. Fatty Acids 104-114 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-28 20227862-10 2011 CONCLUSION: Curcumin improves muscular insulin resistance by increasing oxidation of fatty acid and glucose, which is, at least in part, mediated through LKB1-AMPK pathway. Fatty Acids 85-95 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 159-163 19937189-2 2010 Sirtuin1 (SIRT1) and AMP-activated protein kinase (AMPK) are key metabolic regulators that reduce lipogenesis and increase fatty acid oxidation. Fatty Acids 123-133 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 21-49 19937189-2 2010 Sirtuin1 (SIRT1) and AMP-activated protein kinase (AMPK) are key metabolic regulators that reduce lipogenesis and increase fatty acid oxidation. Fatty Acids 123-133 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 51-55 19699196-5 2009 Treatment of TAC animals with 5-aminoimidazole 1 carboxamide ribonucleoside (AICAR, 0.5 mg/g body wt), a specific activator of AMPK, inhibited cardiac hypertrophy in TAC and reversed PPARalpha, CPT-I and MCAD expression and fatty acid oxidation. Fatty Acids 224-234 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 127-131 19236843-1 2009 BACKGROUND: AMP-dependent protein kinase (AMPK) and peroxisome proliferator-activated receptor (PPAR) alpha facilitate fatty acid oxidation. Fatty Acids 119-129 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 12-40 19236843-1 2009 BACKGROUND: AMP-dependent protein kinase (AMPK) and peroxisome proliferator-activated receptor (PPAR) alpha facilitate fatty acid oxidation. Fatty Acids 119-129 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 42-46 19125418-1 2009 AMP-activated protein kinase (AMPK) is an intracellular fuel sensor that plays a key role in regulating fatty acid synthesis in liver. Fatty Acids 104-114 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 30-34 18339363-5 2008 Activated AMPK phosphorylates and inhibits acetylCoA carboxylase (ACC), the first enzyme in fatty acid biosynthesis. Fatty Acids 92-102 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 10-14 18719073-9 2008 In summary, long-term moderate ethanol consumption reversed the adverse effect of saturated fatty acid on SLC2A4 expression in adipocytes, which was likely to be a result of PRKAA2 activation and subsequent up-regulation of MEF2 and SLC2A4 expressions. Fatty Acids 82-102 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 174-180 17173081-4 2006 RESULTS: Glucose and fatty acid at different concentrations inhibited the phosphorylation of AMPK and ACC at the end of 60 min, but AICAR increased the phosphorylation of AMPK and ACC significantly, while 2.5 mg/L globular adiponectin increased the phosphorylation of AMPK and ACC by 23% (P<0.05) and 50% (P<0.05) respectively, at baseline. Fatty Acids 21-31 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 93-97 18255222-1 2008 Leptin stimulates fatty acid oxidation via the phosphorylation of AMPK (AMP-activated protein kinase) and ACC (acetyl-CoA carboxylase). Fatty Acids 18-28 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 66-70 18255222-1 2008 Leptin stimulates fatty acid oxidation via the phosphorylation of AMPK (AMP-activated protein kinase) and ACC (acetyl-CoA carboxylase). Fatty Acids 18-28 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 72-100 17997005-0 2008 Ethanol consumption impairs regulation of fatty acid metabolism by decreasing the activity of AMP-activated protein kinase in rat liver. Fatty Acids 42-52 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 94-122 17997005-8 2008 These effects are consistent with the impairment of AMPK-mediated regulation of fatty acid metabolism after ethanol consumption, that will facilitate triacylglycerol accumulation. Fatty Acids 80-90 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 52-56 16835401-2 2006 The purpose of this study was to determine whether activation of AMPK and/or ERK1/2 contributes to the regulation of muscle fatty acid (FA) uptake and oxidation in contracting muscle. Fatty Acids 124-134 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 65-69 17942824-2 2008 Our objective was to determine the mechanisms by which AMP-activated protein kinase (AMPK) augments cardiac lipoprotein lipase (LPL), the enzyme that provides the heart with the majority of its fatty acid. Fatty Acids 194-204 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 55-83 17942824-2 2008 Our objective was to determine the mechanisms by which AMP-activated protein kinase (AMPK) augments cardiac lipoprotein lipase (LPL), the enzyme that provides the heart with the majority of its fatty acid. Fatty Acids 194-204 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 85-89 17942824-11 2008 CONCLUSIONS: We propose that AMPK recruitment of LPL to the cardiomyocyte surface (which embraces p38 MAPK activation and actin cytoskeleton polymerization) represents an immediate compensatory response by the heart to guarantee fatty acid supply when glucose utilization is compromised. Fatty Acids 229-239 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 29-33 17188707-0 2007 AMPK control of myocardial fatty acid metabolism fluctuates with the intensity of insulin-deficient diabetes. Fatty Acids 27-37 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-4 17118340-10 2007 In beta cells, an increase in AMPK activity may be required for fatty acid-induced fatty acid oxidation and prevention of lipotoxicity. Fatty Acids 64-74 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 30-34 17118340-10 2007 In beta cells, an increase in AMPK activity may be required for fatty acid-induced fatty acid oxidation and prevention of lipotoxicity. Fatty Acids 83-93 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 30-34 16920812-2 2007 Therefore, we tested the hypothesis that enhanced fatty acid oxidation improves energy status and normalizes AMPK activity and glycolysis in hypertrophied hearts. Fatty Acids 50-60 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 109-113 16816404-0 2006 5-Aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside-induced AMP-activated protein kinase phosphorylation inhibits basal and insulin-stimulated glucose uptake, lipid synthesis, and fatty acid oxidation in isolated rat adipocytes. Fatty Acids 183-193 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 63-91 16816404-1 2006 The objective of this study was to investigate the effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR)-induced AMP-activated protein kinase (AMPK) activation on basal and insulin-stimulated glucose and fatty acid metabolism in isolated rat adipocytes. Fatty Acids 224-234 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 133-161 16816404-1 2006 The objective of this study was to investigate the effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR)-induced AMP-activated protein kinase (AMPK) activation on basal and insulin-stimulated glucose and fatty acid metabolism in isolated rat adipocytes. Fatty Acids 224-234 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 163-167 16816404-6 2006 In contrast to skeletal muscle in which AMPK stimulates fatty acid oxidation to provide ATP as a fuel, we propose that AMPK activation inhibits lipogenesis and fatty acid oxidation in adipocytes. Fatty Acids 56-66 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 40-44 16816404-6 2006 In contrast to skeletal muscle in which AMPK stimulates fatty acid oxidation to provide ATP as a fuel, we propose that AMPK activation inhibits lipogenesis and fatty acid oxidation in adipocytes. Fatty Acids 160-170 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 119-123 16020477-1 2005 The AMP-activated protein kinase (AMPK) is a major regulator of energy metabolism involved in fatty acid and cholesterol synthesis. Fatty Acids 94-104 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 4-32 16304351-4 2006 A 2-fold increase in both AMPK and ACC phosphorylation was observed in the presence of palmitate concentrations as low as 10 microM, which was also accompanied by a significant increase in fatty acid oxidation. Fatty Acids 189-199 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 26-30 16020477-1 2005 The AMP-activated protein kinase (AMPK) is a major regulator of energy metabolism involved in fatty acid and cholesterol synthesis. Fatty Acids 94-104 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 34-38 15547141-1 2005 To determine the role of AMP-activated protein kinase (AMPK) activation on the regulation of fatty acid (FA) uptake and oxidation, we perfused rat hindquarters with 6 mM glucose, 10 microU/ml insulin, 550 microM palmitate, and [14C]palmitate during rest (R) or electrical stimulation (ES), inducing low-intensity (0.1 Hz) muscle contraction either with or without 2 mM 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR). Fatty Acids 93-103 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 25-53 15913551-8 2005 Adenovirus-mediated administration of dominant negative AMPK into skeletal muscle prevented the ALA-induced increases in fatty acid oxidation and insulin-stimulated glucose uptake. Fatty Acids 121-131 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 56-60 15774530-1 2005 5-Amino-4-imidazolecarboxamide riboside (AICAR), a pharmacological activator of AMP-activated protein kinase (AMPK), acutely stimulates glucose uptake and fatty acid (FA) oxidation in skeletal muscle. Fatty Acids 155-165 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 80-108 15774530-1 2005 5-Amino-4-imidazolecarboxamide riboside (AICAR), a pharmacological activator of AMP-activated protein kinase (AMPK), acutely stimulates glucose uptake and fatty acid (FA) oxidation in skeletal muscle. Fatty Acids 155-165 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 110-114 15547141-1 2005 To determine the role of AMP-activated protein kinase (AMPK) activation on the regulation of fatty acid (FA) uptake and oxidation, we perfused rat hindquarters with 6 mM glucose, 10 microU/ml insulin, 550 microM palmitate, and [14C]palmitate during rest (R) or electrical stimulation (ES), inducing low-intensity (0.1 Hz) muscle contraction either with or without 2 mM 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR). Fatty Acids 93-103 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 55-59 15607747-6 2005 The results indicate that dietary PUFA enhance hepatic AMPK activity in vivo, and implicate AMPK as a component of the nutrient-sensing mechanism through which dietary fatty acids and especially PUFA influence the regulation of hepatic lipid metabolism and gene expression. Fatty Acids 168-179 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 55-59 15607747-6 2005 The results indicate that dietary PUFA enhance hepatic AMPK activity in vivo, and implicate AMPK as a component of the nutrient-sensing mechanism through which dietary fatty acids and especially PUFA influence the regulation of hepatic lipid metabolism and gene expression. Fatty Acids 168-179 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 92-96 15578517-11 2004 CONCLUSIONS: Taken together, our findings suggest that AMPK may play a key role in regulating the effects of ethanol on SREBP-1 activation, fatty acid metabolism, and development of alcoholic fatty liver. Fatty Acids 140-150 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 55-59 12015362-2 2002 Once activated, AMPK has been proposed to phosphorylate a number of targets, resulting in increases in glucose transport, fatty acid oxidation, and gene transcription. Fatty Acids 122-132 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 16-20 14985344-2 2004 AMPK has recently emerged as an attractive novel target for the treatment of obesity and type 2 diabetes because its activation increases fatty acid oxidation and improves glucose homeostasis. Fatty Acids 138-148 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-4 12864749-1 2003 UNLABELLED: An increasing body of evidence has revealed that activation of adenosine monophosphate (AMP)-activated protein kinase (AMPK)-activated protein kinase increases fatty acid oxidation by lowering the concentration of malonyl coenzyme A (CoA), an inhibitor of carnitine palmitoyl transferase 1. Fatty Acids 172-182 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 131-135 9435525-2 1997 This study was designed to determine whether AICAR can activate AMP-activated protein kinase (AMPK) in skeletal muscle with consequent phosphorylation of acetyl-CoA carboxylase (ACC), decrease in malonyl-CoA, and increase in fatty acid oxidation. Fatty Acids 225-235 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 64-92 11724780-0 2002 Mechanism for fatty acid "sparing" effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase. Fatty Acids 14-24 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 141-169 11724780-10 2002 Similarly to the fatty acids, 5-amino-4-imidazolecarboxamide ribotide, a specific activator of AMP-activated protein kinase (AMPK) also inhibited the l-PK transcription activity in ChREBP-overexpressed hepatocytes. Fatty Acids 17-28 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 95-123 11724780-10 2002 Similarly to the fatty acids, 5-amino-4-imidazolecarboxamide ribotide, a specific activator of AMP-activated protein kinase (AMPK) also inhibited the l-PK transcription activity in ChREBP-overexpressed hepatocytes. Fatty Acids 17-28 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 125-129 11724780-14 2002 These results strongly suggested that the fatty acid inhibition of glucose-induced l-PK transcription resulted from AMPK phosphorylation of ChREBP at Ser(568), which inactivated the DNA binding activity. Fatty Acids 42-52 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 116-120 10025949-2 1999 Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Fatty Acids 117-128 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 23-27 11724780-15 2002 AMPK was activated by the increased AMP that was generated by the fatty acid activation. Fatty Acids 66-76 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 0-4 11090599-2 2000 This study was designed to determine whether activation of AMP-activated protein kinase (AMPK) will prevent inhibitory effects of insulin and glucose on the rate of fatty acid oxidation. Fatty Acids 165-175 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 59-87 11090599-2 2000 This study was designed to determine whether activation of AMP-activated protein kinase (AMPK) will prevent inhibitory effects of insulin and glucose on the rate of fatty acid oxidation. Fatty Acids 165-175 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 89-93 9435525-2 1997 This study was designed to determine whether AICAR can activate AMP-activated protein kinase (AMPK) in skeletal muscle with consequent phosphorylation of acetyl-CoA carboxylase (ACC), decrease in malonyl-CoA, and increase in fatty acid oxidation. Fatty Acids 225-235 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 94-98 34836374-8 2021 In conclusion, EGCG activated AMPK and insulin pathways, thereby promoting glycolysis, glycogen, and protein synthesis and inhibiting fatty acid (FA) and cholesterol synthesis. Fatty Acids 134-144 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 30-34 7959015-12 1994 An interesting aspect of AMPK is that its expression, unlike in rat liver, could not be detected in human liver, and thus the purported role of the gene in controlling fatty-acid synthesis in the human liver remains to be determined. Fatty Acids 168-178 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 25-29 7744080-7 1995 Incubation of hepatocytes with AICAR activates AMPK due to increased phosphorylation, causes phosphorylation and inactivation of a known target for AMPK (3-hydroxy-3-methylglutaryl-CoA reductase), and almost total cessation of two of the known target pathways, i.e. fatty acid and sterol synthesis. Fatty Acids 266-276 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 47-51 7744080-7 1995 Incubation of hepatocytes with AICAR activates AMPK due to increased phosphorylation, causes phosphorylation and inactivation of a known target for AMPK (3-hydroxy-3-methylglutaryl-CoA reductase), and almost total cessation of two of the known target pathways, i.e. fatty acid and sterol synthesis. Fatty Acids 266-276 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 148-152 34593005-4 2021 And the differentiate of effector CD8+ T cell (CD8+ Teff) into central memory CD8+ T cell (CD8+ TCM) depends on fatty acid oxidation (FAO) to meet their metabolic requirements, which is regulated by adenosine monophosphate activated protein kinase (AMPK). Fatty Acids 112-122 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 199-247 34593005-4 2021 And the differentiate of effector CD8+ T cell (CD8+ Teff) into central memory CD8+ T cell (CD8+ TCM) depends on fatty acid oxidation (FAO) to meet their metabolic requirements, which is regulated by adenosine monophosphate activated protein kinase (AMPK). Fatty Acids 112-122 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 249-253 35488997-7 2022 Further, bodyweight management effect of TCP was observed to target AMPK signalling pathway as the mediator of lipogenesis, sterol biosynthesis, lipolysis, and beta-oxidation of fatty acids. Fatty Acids 178-189 protein kinase AMP-activated catalytic subunit alpha 2 Rattus norvegicus 68-72