| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| This includes alterations in AMPK , ACC , and MCD activity in the diabetic rat heart . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| ACC is in turn controlled by AMP activated protein kinase ( AMPK ) , which acts as a fuel gauge in the heart . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Evidence has been presented by others to indicate that a 5 ' AMP activated protein kinase ( AMPK ) is likely the major regulatory kinase active on ACC . ^^^ In the present study , we have examined , in Fao hepatoma cells , the effects of insulin on ACC and AMPK activity , the latter measured with a synthetic peptide corresponding to one of the phosphorylation sites on ACC for AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Regulation of acetyl CoA carboxylase ( ACC ) by ATP depletion in developing oligodendrocytes mimics the action of AMP activated protein kinase ( AMPK ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| A 5 ' AMP activated protein kinase ( AMPK ) has been identified as the major regulatory kinase active on ACC . ^^^ Employing dual digitonin pulse perfusion , the effect of varying nutrition on periportal and perivenous zonation of ACC and AMPK activity within the liver has been characterized . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Since AMPK can phosphorylate and inactivate acetyl CoA carboxylase ( ACC ) in other tissues , and heart ACC has an important role in regulating fatty acid oxidation , we measured ACC activity in hearts reperfused post ischemia . ^^^ A significant negative correlation ( r= 0 . 78 ) was observed between AMPK activity and ACC activity measured in aerobic and reperfused ischemic hearts . ^^^ AMPK then phosphorylates and inactivates ACC . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The activity of AMP dependent protein kinase ( AMPK ) , which phosphorylates and inactivates ACC , was also not significantly different in the dobutamine hearts compared to the saline hearts ( 322 + / 26 vs . 338 + / 39 pmol . min 1 . mg protein 1 , respectively ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| This study was designed to compare functional effects of phosphorylation of muscle acetyl CoA carboxylase ( ACC ) by adenosine 3 ' , 5 ' cyclic monophosphate dependent protein kinase ( PKA ) and by AMP activated protein kinase ( AMPK ) . ^^^ AMPK appears to be the more important regulator of muscle ACC . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In other tissues , 5 ' AMP activated protein kinase ( AMPK ) can phosphorylate and inhibit ACC activity . ^^^ In 1 day old hearts , the presence of insulin resulted in a significant decrease in AMPK activity , an increase in ACC activity , and a decrease in fatty acid oxidation rates . ^^^ In 7 day old hearts , AMPK activity was also decreased by insulin , although ACC activity remained low and fatty acid oxidation rates remained high . ^^^ Stimulation of AMPK in 7 day old hearts with 200 mumol / L 5 amino 4 imidazolecarboxamide ribotide resulted in a further decrease in ACC activity and an increase in fatty acid oxidation rates . ^^^ These data suggest that AMPK , ACC , and fatty acid oxidation are sensitive to insulin in 1 day old rabbit hearts and that the decrease in circulating insulin levels seen after birth leads to an increased activity of AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Muscle malonyl CoA decreases during exercise or electrical stimulation , the exercise induced decline being accompanied by changes in the kinetic properties [ maximal velocity ( Vmax ) , activation constant ( Ka ) , and citrate concentration required to produce 50 % Vmax ( K0 . 5 ) ] of acetyl CoAcarboxylase ( ACC ) and by an increase in the AMP activated protein kinase activity ( AMPK ) . ^^^ ACC and AMPK activities were quantitated in ammonium sulfate precipitates from homogenates prepared from the frozen muscles . ^^^ The Vmax and Ka of ACC for citrate decreased and increased , respectively , over the first 10 min of stimulation , but significantly increased AMPK activity was not observed until 10 to 20 min of stimulation ( P < 0 . 05 ) . ^^^ Thus exercise induced changes in functional properties of ACC appear to be contraction mediated and are accompanied by increased AMPK activity and an increase in the estimated free AMP . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The rapid decrease in ACC beta activity after the onset of contractions ( 50 % by 20 s ) and its slow restoration to initial values during recovery ( 60 90 min ) were paralleled temporally by reciprocal changes in the activity of the alpha 2 but not the alpha 1 isoform of 5 ' AMP activated protein kinase ( AMPK ) . ^^^ In conclusion , the results suggest that the decrease in ACC activity during muscle contraction is caused by an increase in its phosphorylation , most probably due , at least in part , to activation of the alpha 2 isoform of AMPK . ^^^ These alterations in ACC and AMPK activity , by diminishing the concentration of malonyl CoA , could be responsible for the increase in fatty acid oxidation observed in skeletal muscle during exercise . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Exercise induces a decline in skeletal muscle malonyl CoA , which is accompanied by inactivation of ACC and increased activity of AMP activated protein kinase ( AMPK ) . ^^^ This study was designed to determine the effect of exercise intensity on the enzyme kinetics of ACC , malonyl CoA levels , and AMPK activity in skeletal muscle . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Under conditions of metabolic stress , 5 ' adenosine monophosphate activated protein kinase ( AMPK ) , which is highly expressed in cardiac muscle , can phosphorylate and decrease ACC activity . ^^^ In this study , we determined if fatty acid oxidation in the heart could be regulated by insulin , due to alterations in AMPK regulation of ACC activity . ^^^ Increasing insulin concentration resulted in a decrease in fatty acid oxidation rates ( P < . 05 ) , a decrease in AMPK activity ( P < . 05 ) , and an increase in ACC activity ( P < . 05 ) compared with the low insulin group . ^^^ A negative correlation was observed between AMPK and ACC activity ( r = . 76 ) . ^^^ We conclude that insulin , acting through inhibition of AMPK and stimulation of ACC , is capable of inhibiting myocardial fatty acid oxidation . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ Perfusion with medium containing AICAR was found to activate AMPK in skeletal muscle , inactivate ACC , and decrease malonyl CoA . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| As muscle goes from a resting state to exercise , the following sequence of events occurs ( Figure 5 . 5 ) : ( 1 ) The rise in AMP accompanying contraction allosterically activates AMPK and an AMPK kinase ; ( 2 ) The activated AMPK kinase phosphorylates and further activates AMPK ; ( 3 ) The activated AMPK phosphorylates and inactivates ACC ; and ( 4 ) The consequent decline in malonyl CoA ( product of ACC reaction ) relieves inhibition of CPT 1 and allows an increased rate of fatty acid oxidation when fatty acids become available . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Muscle malonyl CoA , a potent inhibitor of CPT 1 , decreases during muscle contraction as a consequence of phosphorylation and inactivation of acetyl CoA carboxylase ( ACC ) by AMP activated protein kinase ( AMPK ) . ^^^ When AMPK is artificially activated with AICA riboside , ACC is inactivated , malonyl CoA decreases , and fatty acid oxidation increases . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The purpose of these experiments was to determine whether this decrease in malonyl CoA is accompanied by an activation of AMP activated protein kinase ( AMPK ) and inactivation of acetyl CoA carboxylase ( ACC ) . ^^^ There was no significant difference in AMPK and ACC activities after 120 min of exercise , although a trend toward a decrease in ACC and an increase in AMPK was noted 15 min postexercise . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Our results demonstrate that 5 ' AMP activated protein kinase ( AMPK ) is able to phosphorylate both ACC 265 and ACC 280 , resulting in an almost complete loss of ACC activity . ^^^ ACC 280 and ACC 265 copurified under all experimental conditions , and purification of heart ACC also resulted in the specific copurification of the alpha 2 isoform of the catalytic subunit of AMPK . ^^^ Although both catalytic subunits of AMPK were expressed in crude heart homogenates , our results suggest that alpha 2 , and not alpha 1 , is the dominant isoform of AMPK catalytic subunit regulating ACC in the heart . ^^^ Immunoprecipitation studies demonstrated that specific antibodies for both ACC 265 and ACC 280 were able to coimmunoprecipitate the alternate isoform along with the alpha 2 isoform of AMPK . ^^^ Taken together , the immunoprecipitation and the purification studies suggest that the two isoforms of ACC in the heart exist in a heterodimeric structure , and that this structure is tightly associated with the alpha 2 subunit of AMPK . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : Shortly after birth , a rise in 5 ' adenosine monophosphate activated protein kinase ( AMPK ) activity results in the phosphorylation and inhibition of acetyl coenzyme A ( CoA ) carboxylase ( ACC ) , and a decline in myocardial malonyl CoA levels with increased fatty acid oxidation rates . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Here we report the presence of both AMPK and ACC in human umbilical vein endothelial cells ( HUVEC ) . ^^^ Incubation of HUVEC with 2 mM AICAR , an AMPK activator , caused a 5 fold activation of AMPK , which was accompanied by a 70 % decrease in ACC activity and a 2 fold increase in fatty acid oxidation . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| To determine if subcellular changes in the control of fatty acid oxidation contribute to these changes , we measured the activity of three enzymes involved in the control of fatty acid oxidation ; AMP activated protein kinase ( AMPK ) , acetyl CoA carboxylase ( ACC ) , and malonyl CoA decarboxylase ( MCD ) . ^^^ Although AMPK and ACC activity in control and diabetic hearts was not different , MCD activity and expression in all diabetic rat heart perfusion groups were significantly higher than that seen in corresponding control hearts . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Acetyl CoA carboxylase ( ACC ) activity , a target for AMPK , decreased in all three muscle types in response to AICAR injection but was lowest in the white quadriceps . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| During contraction decreases in muscle malonyl CoA concentration have been related to activation of AMP activated protein kinase ( AMPK ) , which phosphorylates and inhibits acetyl CoA carboxylase ( ACC ) , the rate limiting enzyme in malonyl CoA formation . ^^^ They also suggest a dual control of malonyl CoA concentration by ACC and MCD , via AMPK , during exercise . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In perfused fast twitch muscles , contractions induced significant increases in AMPK activity and glucose transport and decreases in acetyl CoA carboxylase ( ACC ) activity in both HG and LG groups . ^^^ Contraction induced glucose transport was nearly 2 fold ( P < 0 . 05 ) and AMPK activation was 3 fold ( P < 0 . 05 ) higher in the LG group compared with the HG group , whereas ACC deactivation was not different between groups . ^^^ In contracting slow twitch muscles with LG , the increase in AMPK activity ( 315 % ) and the decrease in ACC activity ( 54 vs . 34 % at 0 . 2 mmol / l citrate , LG vs . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMPK phosphorylates and inhibits acetyl coenzyme A ( CoA ) carboxylase ( ACC ) and enhances GLUT 4 translocation . ^^^ Here , we show that a 30 s bicycle sprint exercise increases the activity of the human skeletal muscle AMPK alpha 1 and alpha 2 isoforms approximately two to threefold and the phosphorylation of ACC at Ser ( 79 ) ( AMPK phosphorylation site ) approximately 8 . 5 fold . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The results indicate that the AMPK ACC malonyl CoA carnitine palmitoyl transferase 1 mechanism plays a key role in the physiological regulation of fatty acid oxidation in HUVECs . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| We tested the hypothesis that myocardial substrate supply regulates fatty acid oxidation independent of changes in acetyl CoA carboxylase ( ACC ) and 5 ' AMP activated protein kinase ( AMPK ) activities . ^^^ The increases in octanoate oxidation and malonyl CoA content were independent of changes in ACC and AMPK activity , except that ACC activity increased with very high acetyl CoA supply levels . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Here we report that metformin activates AMPK in hepatocytes ; as a result , acetyl CoA carboxylase ( ACC ) activity is reduced , fatty acid oxidation is induced , and expression of lipogenic enzymes is suppressed . ^^^ In metformin treated rats , hepatic expression of SREBP 1 ( and other lipogenic ) mRNAs and protein is reduced ; activity of the AMPK target , ACC , is also reduced . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Some of these effects are due to AMPK mediated regulation of cellular malonyl CoA content , ascribed to the ability of AMPK to phosphorylate and inactivate acetyl CoA carboxylase ( ACC ) , reducing malonyl CoA formation . ^^^ Although all muscle treatments resulted in activation of AMPK and phosphorylation of ACC , no stimulus had any effect on MCD activity . ^^^ We conclude that MCD is not a substrate for AMPK in fast twitch muscle or the 832 / 13 INS 1 islet cell line and that the principal mechanism by which AMPK regulates malonyl CoA content is through its regulation of ACC . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The 5 ' AMP activated protein kinase ( AMPK ) potently stimulates fatty acid oxidation in muscle by inhibiting the activity of acetyl coenzyme A carboxylase ( ACC ) . ^^^ In parallel with its activation of AMPK , leptin suppresses the activity of ACC , thereby stimulating the oxidation of fatty acids in muscle . ^^^ Blocking AMPK activation inhibits the phosphorylation of ACC stimulated by leptin . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| This was an excellent substrate that was phosphorylated with similar kinetic parameters to ACC 1 by both native AMPK and the bacterially expressed kinase domain . ^^^ The results reveal that AMPK and ACC 1 interact over a much wider region than previously realized ( > 20 residues ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| We also determined the potential role of 5 ' AMP activated protein kinase ( AMPK ) in this process , since it can phosphorylate and inhibit ACC activity in both liver and muscle . ^^^ TG content , ACC , and AMPK were examined in the liver and skeletal muscle of insulin resistant JCR : LA cp rats during the time frame when insulin resistance develops . ^^^ Hepatic ACC activity was significantly elevated in 12 week old JCR : LA cp rats compared with lean age matched controls ( 8 . 75 + / 0 . 53 vs . 3 . 30 + / 0 . 18 nmol . min ( 1 ) . mg ( 1 ) , respectively ) , even though AMPK activity was also increased . ^^^ There were no significant differences in ACC activity , ACC protein expression , or AMPK activity in the skeletal muscle of the 12 week JCR : LA cp rats . ^^^ Treatment of 12 week JCR : LA cp rats with MEDICA 16 ( an ATP citrate lyase inhibitor ) resulted in a decrease in hepatic ACC and AMPK activities , but had no effect on skeletal muscle ACC and AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In these experiments using a phosphoserine antibody to ACC and a phosphothreonine antibody to AMPK , evidence was obtained for phosphorylation and activation of ACC in vitro , in gastrocnemius muscle electrically stimulated at different frequencies , and in muscle from rats running on the treadmill . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMP activated protein kinase ( AMPK ) plays a major role in the regulation of cardiac fatty acid oxidation by inhibiting acetyl CoA carboxylase ( ACC ) and reducing malonyl CoA levels . ^^^ However , we demonstrate that leptin had no significant effect on AMPK activity , AMPK phosphorylation state , ACC activity , or malonyl CoA levels . ^^^ We also show that the effects of leptin in the heart are independent of changes in the AMPK ACC malonyl CoA axis . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In addition , the activity of sn glycerol 3 phosphate acyltransferase ( GPAT ) , which like MCD and ACC can be regulated by AMP activated protein kinase ( AMPK ) , was assayed . ^^^ These events appeared to be mediated via activation of AMPK since : 1 ) AMPK activity was concurrently increased by exercise in both tissues ; 2 ) similar findings were observed after the injection of 5 amino 4 imidazole carboxamide , an AMPK activator ; 3 ) changes in the activity of GPAT and ACC paralleled that of MCD ; and 4 ) the increase in MCD activity in muscle was reversed in vitro by incubating immunoprecipitated enzyme from the exercised muscle with protein phosphatase 2A , and it was reproduced by incubating immunopurified MCD from resting muscle with purified AMPK . ^^^ An unexpected finding was that exercise caused similar changes in the activities of ACC , MCD , GPAT , and AMPK and the concentration of malonyl CoA in adipose tissue . ^^^ In conclusion : MCD , GPAT , and ACC are coordinately regulated by AMPK in liver and adipose tissue in response to exercise , and except for GPAT , also in muscle . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The effects of endurance training on the response of muscle AMP activated protein kinase ( AMPK ) and acetyl CoA carboxylase ( ACC ) to moderate treadmill exercise were examined . ^^^ In red quadriceps , there was a large activation of alpha 2 AMPK and inactivation of ACC in response to exercise . ^^^ In white quadriceps , there were no effects of exercise on AMPK or ACC , but alpha 2 activity was higher after training because of increased phosphorylation of Thr ( 172 ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In this paper , we studied the effect of AMPK activation and of protein phosphatase inhibitors , on the amino acid induced activation of p70S6K and ACC in hepatocytes in suspension . ^^^ It also activated ACC by a phosphatase dependent mechanism but did not modify AMPK activation . ^^^ Conversely , the amino acid induced activation of both ACC and p70S6K was blocked or reversed when AMPK was activated . ^^^ This AMPK activation increased Ser 79 phosphorylation in ACC but decreased Thr 389 phosphorylation in p70S6K . ^^^ It is concluded that ( a ) AMPK blocks amino acid induced activation of ACC and p70S6K , directly by phosphorylating Ser 79 in ACC , and indirectly by inhibiting p70S6K phosphorylation , and ( b ) both activation and inhibition of protein phosphatases are involved in the activation of p70S6K by amino acids . p70S6K adds to an increasing list of targets of AMPK in agreement with the inhibition of energy consuming biosynthetic pathways . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In parallel with its activation of AMPK , Ad stimulates phosphorylation of acetyl coenzyme A carboxylase ( ACC ) , fatty acid oxidation , glucose uptake and lactate production in myocytes , phosphorylation of ACC and reduction of molecules involved in gluconeogenesis in the liver , and reduction of glucose levels in vivo . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| This study was designed to determine the role of thyroid hormones in controlling expression levels of these AMPK subunits and of one downstream target , acetyl CoA carboxylase ( ACC ) , in muscle . ^^^ AMPK subunit and ACC levels were determined by Western blots in control rats , in rats given 0 . 01 % propylthiouracil ( PTU ) in drinking water for 3 wk , and in rats given 3 mg of thyroxine and 1 mg of triiodothyronine per kilogram chow for 1 or 3 wk . ^^^ These data provide evidence that skeletal muscle AMPK subunit and ACC expression is partially under the control of thyroid hormones . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Activation of AMPK by cellular stress or exercise therefore switches on fatty acid oxidation ( via phosphorylation of ACC 2 ) while switching off fatty acid synthesis ( via phosphorylation of ACC 1 ) . ^^^ The Drosophila melanogaster genome contains single genes encoding homologues of the alpha , beta and gamma subunits of AMPK ( DmAMPK ) and of ACC ( DmACC ) . ^^^ Studies in a Drosophila embryonal cell line show that DmAMPK is activated by stresses that cause ATP depletion ( oligomycin , hypoxia or glucose deprivation ) and that this is associated with phosphorylation of the site on DmACC equivalent to the AMPK sites on mammalian ACC 1 and ACC 2 . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| However , taken as a whole , our data support recent evidence in rodent muscle that leptin stimulates FA oxidation through stimulation of AMPK and a subsequent downregulation of ACC activity . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Incubation of rat extensor digitorum longus ( EDL ) , a predominantly fast twitch muscle , with gACRP 30 ( 2 . 5 micro g / ml ) for 30 min led to 2 fold increases in AMPK activity and phosphorylation of both AMPK on Thr 172 and acetyl CoA carboxylase ( ACC ) on Ser 79 . ^^^ Similar changes in malonyl CoA and ACC were observed in soleus muscle incubated with gACRP 30 ( 2 . 5 micro g / ml ) , although no significant changes in AMPK activity or 2 deoxyglucose uptake were detected . ^^^ When EDL was incubated with full length hexameric ACRP 30 ( 10 micro g / ml ) , AMPK activity and ACC phosphorylation were not altered . ^^^ Administration of gACRP 30 ( 75 micro g ) to C 57 BL6J mice in vivo led to increased AMPK activity and ACC phosphorylation and decreased malonyl CoA concentration in gastrocnemius muscle within 15 30 min . ^^^ Both in vivo and in vitro , activation of AMPK was the first effect of gACRP 30 and was transient , whereas alterations in malonyl CoA and ACC occurred later and were more sustained . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| When activated , AMPK increases fatty acid oxidation by inhibiting acetyl CoA carboxylase ( ACC ) and reducing malonyl CoA levels , and it decreases TG content by inhibiting glycerol 3 phosphate acyltransferase ( GPAT ) , the rate limiting step in TG synthesis . ^^^ We also found no significant difference in various established downstream targets of AMPK : ACC activity , malonyl CoA levels , carnitine palmitoyltransferase 1 activity , or GPAT activity . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Extracellular regulated kinase ( ERK1 / 2 ) , p 38 MAPK , histone H 3 , AMPK and acetyl CoA carboxylase ( ACC ) phosphorylation was determined by immunoblot analysis using phosphospecific antibodies . ^^^ In conclusion , intense cycling exercise in subjects with a prolonged history of endurance training increases MAPK signalling to the downstream targets MSK 1 and histone H 3 and isoform specific AMPK signalling to ACC . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Three enzymes , namely AMP activated protein kinase ( AMPK ) , acetyl CoA carboxylase ( ACC ) and malonyl CoA decarboxylase ( MCD ) , appear to be extremely important in this process . ^^^ AMPK causes phosphorylation and inhibition of ACC , which reduces the production of malonyl CoA . ^^^ In ischaemia , AMPK is rapidly activated and inhibits ACC , subsequently decreasing malonyl CoA levels and increasing fatty acid oxidation rates . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The changes in AMPK activity during exercise were associated with physiological AMPK effects ( GLUT 4 translocation to the sarcolemma and ACC phosphorylation ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Exposure of bovine aortic endothelial cells ( BAEC ) to chemically synthesized ONOO acutely and significantly increased phosphorylation of c Src , PDK 1 , AMPK , and its downstream target , acetyl CoA carboxylase ( ACC ) , without affecting cellular AMP . ^^^ Exposure of BAEC to hypoxia reoxygenation ( H / R ) caused a biphasic increase in AMPK and ACC phosphorylation , which was prevented by adenoviral overexpression of superoxide dismutase ( SOD ) or inhibition of nitric oxide synthase ( NOS ) implicating a role of ONOO formed during H / R . ^^^ Taken together , our results indicate a novel pathway by which H / R via ONOO activates AMPK in a c Src mediated , PI 3 kinase dependent manner , and suggest that ONOO induced activation of AMPK might thereby regulate metabolic enzymes , such as ACC . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Studies carried out primarily in skeletal muscle suggest that AMPK modulates the concentration of malonyl CoA by concurrently phosphorylating and inhibiting acetyl CoA carboxylase ( ACC ) , the rate limiting enzyme in malonyl CoA synthesis , and phosphorylating and activating malonyl CoA decarboxylase ( MCD ) , an enzyme involved in its degradation . ^^^ We have recently observed that AMPK and MCD activities are increased and ACC activity diminished in skeletal muscle , liver and , surprisingly , in adipose tissue 30 min following exercise ( treadmill run ) in normal rats . ^^^ In liver and adipose tissue these changes were associated with a decrease in the activity of glycerol 3 phosphate acyltransferase ( GPAT ) , which catalyses the first committed reaction in glycerolipid synthesis and , which like ACC , is phosphorylated and inhibited by AMPK . ^^^ Similar changes in ACC , MCD and GPAT were observed following the administration of 5 aminoimidazole 4 carboxamide riboside ( AICAR ) , further indicating that the exercise induced alterations in these enzymes were AMPK mediated . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| These results indicate that ACC beta phosphorylation is especially sensitive to exercise and tightly coupled to AMPK signaling and that AMPK activation does not depend on AMPK kinase activation during exercise . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In the absence of high affinity and selective antiphospho Ser / Thr antibodies for AMPK substrates , we have developed two homogeneous AMPK assays with the commercially available antibody Anti pS ( 133 ) CREB and an engineered peptide ACC CREBp . ^^^ ACC CREBp showed increased suitability as a substrate for AMPK , eliminated phosphorylation by PKA , and preserved antibody binding . ^^^ The homogeneous time resolved fluorescence and AlphaScreen AMPK assays were developed using both Anti pS ( 133 ) CREB antibody and ACC CREBp that are either labeled with a fluorescent probe or linked to a photoactivated bead , respectively . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In contrast , exercise lowers the concentration of malonyl CoA , by activating an AMP activated protein kinase ( AMPK ) , which phosphorylates and inhibits ACC . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| To assess these questions , we examined the effects of pioglitazone , administered orally to intact rats , on AMPK phosphorylation ( AMPK P ) ( a measure of its activation ) and acetyl CoA carboxylase ( ACC ) activity and malonyl CoA concentration in rat liver and adipose tissue . ^^^ Treatment with pioglitazone ( 20mg / kg bw / day for 3 weeks ) did not significantly increase either P AMPK or P ACC ( which varies inversely with ACC activity ) in control rats . ^^^ However , in the Dahl S rats values for AMPK P and ACC P were 50 % lower than in control rats and were doubled by pioglitazone treatment . ^^^ Under basal conditions ( no manipulation of the animals ) , pioglitazone increased AMPK phosphorylation by twofold and decreased ACC activity and the concentration of malonyl CoA by 50 % in liver . ^^^ Following a euglycemic hyperinsulinemic clamp ( 6h ) , 50 % decreases in AMPK and ACC phosphorylation ( indicating an increase in its activity ) and comparable increases in malonyl CoA concentration were observed in liver and adipose tissue . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The `` dual inhibitor ' ' activity of ESP 55016 was unlikely attributable to the activation of the AMP activated protein kinase ( AMPK ) pathway because AMPK and acetyl CoA carboxylase ( ACC ) phosphorylation states as well as ACC activity were not altered by ESP 55016 . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AICAR or LPS did not alter the AMPK activity as well as the phosphorylations of AMPK alpha ( Thr 172 ) and ACC ( Ser 79 ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Some cells were then collected for immunoblot analysis to assess phosphorylation of AMPK ( pAMPK ) and its substrate acetyl CoA carboxylase ( ACC ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| We report here that incubation with IL 6 ( 30 120 ng / ml ) increases the phosphorylation of AMPK ( an indicator of its activation ) and that of its target molecule , acetyl CoA carboxylase ( ACC ) , in both extensor digitorum longus muscle and cultured F422a adipocytes . ^^^ In agreement with previous studies in the rat , in control mice P AMPK and P ACC abundance was increased by 30 150 % in the three tissues in response to exercise with the greatest increases in skeletal muscle . ^^^ In contrast , in IL 6 ( / ) mice , we found that the abundance of both P AMPK and P ACC was lower ( 60 90 % ) in muscle and adipose tissue at rest . ^^^ In liver , decreases in P AMPK and P ACC in the IL 6 ( / ) mice were more modest and the increases in their abundance caused by exercise were indistinguishable from those of control mice . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMPK signaling is intact , because 5 aminoimidazole 4 carboxamide 1 beta D ribonucleoside ( AICAR ) increased AMPK and acetyl CoA carboxylase ( ACC ) phosphorylation to a similar extent in Type 2 diabetic and nondiabetic subjects . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| To better understand the role of AMPK in the regulation of hepatic lipids , we studied the effect of metformin on AMPK and its downstream effector , acetyl CoA carboxylase ( ACC ) , as well as on lipid content in cultured human hepatoma HepG 2 cells . ^^^ Under these conditions , the phosphorylation of AMPK and ACC was also decreased , and the level of hepatocellular triacylglycerols increased . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AICAR treatment significantly increased total FA oxidation ( P < 0 . 05 ) during both R ( 0 . 38 + / 0 . 11 vs . 0 . 89 + / 0 . 1 nmol 10 min ( 1 ) 10 g ( 1 ) ) and ES ( 0 . 73 + / 0 . 11 vs . 2 . 01 + / 0 . 1 nmol 10 min ( 1 ) 10 g ( 1 ) ) , which was paralleled in both conditions by a significant increase and significant decrease in AMPK and acetyl CoA carboxylase ( ACC ) activity , respectively ( P < 0 . 05 ) . ^^^ Low intensity muscle contraction increased glucose uptake , FA uptake , and total FA oxidation ( P < 0 . 05 ) despite no change in AMPK ( 950 . 5 + / 35 . 9 vs . 1 , 067 . 7 + / 58 . 8 nmol 10 min ( 1 ) 10 g ( 1 ) ) or ACC ( 51 . 2 + / 6 . 7 vs . 55 . 7 + / 2 . 0 nmol 10 min ( 1 ) 10 g ( 1 ) ) activity from R to ES ( P > 0 . 05 ) . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| A non specific effect of the MEK inhibitors on AICAR accessibility to the oocyte was discounted by showing that they failed to suppress either nucleoside uptake or AICAR stimulated phosphorylation of acetyl CoA carboxylase ( ACC ) , a substrate of AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| METHODS : The effects of ethanol on AMPK , acetyl CoA carboxylase ( ACC ) , and SREBP 1 were assessed in rat hepatic cells and in the livers of ethanol fed mice . ^^^ Finally , feeding mice a low fat diet with ethanol resulted in significantly reduced hepatic AMPK activity , increased ACC activity , and enhanced malonyl CoA content . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMP activated protein kinase ( AMPK ) has previously been demonstrated to phosphorylate and inactivate skeletal muscle acetyl CoA carboxylase ( ACC ) , the enzyme responsible for synthesis of malonyl CoA , an inhibitor of carnitine palmitoyltransferase 1 and fatty acid oxidation . ^^^ Contraction induced activation of AMPK with subsequent phosphorylation / inactivation of ACC has been postulated to be responsible in part for the increase in fatty acid oxidation that occurs in muscle during exercise . ^^^ These studies were designed to answer the question : Does phosphorylation of ACC by AMPK make palmitoyl CoA a more effective inhibitor of ACC . ^^^ Purified rat muscle ACC was subjected to phosphorylation by AMPK . ^^^ Skeletal muscle ACC is more potently inhibited by palmitoyl CoA after having been phosphorylated by AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Recently , two adiponectin receptors ( AdipoR ) have been isolated and adenosine monophosphate kinase ( AMPK ) , as well as acetyl coenzyme A carboxylase ( ACC ) , appear to be critical downstream mediators for various effects of this adipokine . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| There were no differences among groups in activity of ACC or AMP activated protein kinase ( AMPK ) , which physiologically inhibits ACC . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Running increased alpha 1 AMPK kinase activity , phosphorylation ( P ) of AMPK , and acetyl CoA carboxylase ( ACC ) beta in alpha 2 WT and alpha 2 KO muscles and increased alpha 2 AMPK kinase activity in alpha 2 WT . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Culture with physiological concentrations ( 2 . 5 microg / ml ) of globular adiponectin was found to increase the phosphorylation of both AMPK and acetylcoA carboxylase ( ACC ) in these cell types . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In addition , we examine how changes in the activity of ACC , MCD , and other enzymes that govern fatty acid and glycerolipid synthesis relate temporally to alterations in the activities of the fuel sensing enzyme AMP activated protein kinase ( AMPK ) . ^^^ At 1 h , the decrease in AMPK activity was associated with an eightfold increase in the activity of the alpha 1 isoform of ACC and a 30 % decrease in the activity of MCD , two enzymes thought to be regulated by AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMPK was first discovered as an activity that inhibited preparations of ACC 1 ( acetyl CoA carboxylase ) , a regulator of cellular fatty acid synthesis . ^^^ Manipulation of NM 23 H1 / NDPK A nucleotide transphosphorylation activity to generate ATP ( but not GTP ) enhances the activity of AMPK towards its specific peptide substrate in vitro and also regulates the phosphorylation of ACC 1 , an in vivo target for AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| To assess skeletal muscle AMPK activity in leptin sensitive and insensitive states , we examined phosphorylation of AMPK and its target , acetyl CoA carboxylase ( ACC ) , in muscles from LepTg under dietary modification . ^^^ Here we show that phosphorylation of AMPK and ACC are chronically augmented in LepTg soleus muscle , with a concomitant increase in the AMP to ATP ratio and a significant decrease in tissue triglyceride content . ^^^ In parallel , elevated soleus AMPK and ACC phosphorylation in regular diet fed LepTg is attenuated , and tissue triglyceride content is increased in those given HFD . ^^^ Of note , substitution of HFD with regular diet causes a robust recovery of soleus AMPK and ACC phosphorylation in LepTg , with a higher rate of body weight reduction and a regain of insulin sensitivity . ^^^ In conclusion , soleus AMPK and ACC phosphorylation in LepTg changes in parallel with its insulin sensitivity under dietary modification , suggesting a close association between skeletal muscle AMPK activity and sensitivity to leptin . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Decreased AMPK and ACC phosphorylation were observed in response to resistin while expression of ACC and AMPK isoforms was unaltered . ^^^ In summary , our results demonstrate that chronic incubation of skeletal muscle cells with resistin decreased fatty acid uptake and metabolism via a mechanism involving decreased cell surface CD 36 content , FATP 1 expression and a decrease in phosphorylation of AMPK and ACC . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Immunoblotting demonstrated that cold exposure per se is sufficient for inducing , on a time dependent basis , the molecular activation of the serine / threonine kinase AMP activated protein kinase ( AMPK ) and inactivation of the acetyl CoA carboxylase ( ACC ) . ^^^ These molecular phenomena were accompanied by resistance to nutrient induced inactivation of AMPK and activation of ACC . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Significant ( P < 0 . 01 ) muscle and liver insulin resistance first appeared in red quadriceps and liver of the glucose infused group at 5 h and was associated with a twofold increase in DAG and malonyl CoA content and a 50 % decrease in AMPK and acetyl CoA carboxylase ( ACC ) phosphorylation and AMPK activity . ^^^ White quadriceps showed qualitatively similar changes but without decreases in AMPK or ACC phosphorylation . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Muscle stimulation increased the phosphorylation of acetyl CoA carboxylase ( ACC ) , a downstream target of AMPK , and the rate of 3 O methyl d glucose transport . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The purpose of this study was to investigate the effects of long chain fatty acids ( LCFAs ) on AMP activated protein kinase ( AMPK ) and acetyl coenzyme A carboxylase ( ACC ) phosphorylation and beta oxidation in skeletal muscle . ^^^ Subsequently , ACC and AMPK phosphorylation and fatty acid oxidation were measured . ^^^ 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 . ^^^ The effect of palmitate on AMPK and ACC phosphorylation was dose dependent , reaching maximum increases of 3 . 5 and 4 . 5 fold , respectively . ^^^ Interestingly , ACC phosphorylation was coupled with AMPK activation at palmitate concentrations ranging from 10 to 100 microM ; however , at concentrations > 200 microM , ACC phosphorylation and fatty acid oxidation remained high even after AMPK phosphorylation was completely prevented by the use of a selective AMPK inhibitor . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The ability of gAd to increase GLUT 4 myc translocation , glucose uptake , fatty acid uptake and oxidation , as well as AMP activated protein kinase ( AMPK ) and acetyl CoA carboxylase ( ACC ) phosphorylation , was decreased by both hyperglycemia and hyperinsulinemia . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| We compared AMPK and ACC phosphorylation and the protein content of the upstream AMPK kinase LKB 1 and the AMPK regulated transcriptional coactivator PPARgamma coactivator 1 ( PGC 1 ) in gastrocnemius of sedentary obese Zucker rats and sedentary lean Zucker rats . ^^^ In obese rats , phosphorylation of ACC and protein expression of PGC 1alpha , two AMPK regulated proteins , tended to be reduced by 50 ( P = 0 . 07 ) and 35 % ( P = 0 . 1 ) , respectively . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| The role of the various lipid binding proteins in transmembrane and cytosolic transport of lipids is considered as well as regulation of lipid entry into the mitochondria , focusing on the putative role of AMP activated protein kinase ( AMPK ) , acetyl CoA carboxylase ( ACC ) , and carnitine during exercise . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Acetyl CoA carboxylase ( ACC ) is phosphorylated at Ser 218 by AMPK , and alpha 1 but not beta adrenoceptor stimulation results in phosphorylation of ACC at this residue . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Extracellular adenosine is equally able to activate AMPK and promote ACC phosphorylation in liver parenchymal cell models in a manner that is also inhibited by 5 ' ITU . ^^^ In summary , this study shows that adenosine , when added at physiological concentrations , activates AMPK and promotes ACC phosphorylation . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMP activated protein kinase ( AMPK ) activation is known to promote FA oxidation through its control of acetyl CoA carboxylase ( ACC ) . ^^^ Acute Dex promoted ACC phosphorylation , and increased cardiac palmitate oxidation , likely through its effects in increasing AMPK phosphorylation and total AMPK protein and gene expression . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Recent data strongly implicate the AMPK acetyl CoA carboxylase ( ACC ) malonyl CoA pathway in the hypothalamus in the regulation of food intake , body weight and hepatic glucose production . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Acetyl coenzyme A carboxylase ( ACC ) is a well known downstream target of AMPK . ^^^ The ACC contains serine residues that are phosphorylated by AMPK . ^^^ The present study was undertaken to determine whether long term exercise of medium intensity ( 60 % of Vo2max for 12 weeks ) may influence AMPK enzyme activity , gene / protein expression , and subsequent ACC phosphorylation in rat adipose tissue ( visceral and subcutaneous ) and liver . ^^^ We initially demonstrated that long term exercise induced a significant increase in phosphorylation of Thr 172 in the AMPK alpha 1 subunit and of Ser 79 in ACC in visceral adipose tissue rather than subcutaneous tissue . ^^^ In addition to adipose tissue , we demonstrated that long term exercise induced an increase in both AMPK / ACC phosphorylation and alpha 1 , alpha 2 subunit mRNA / protein expression in the liver . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| AMPK was first discovered as an activity that inhibited preparations of acetyl coenzyme A carboxylase 1 ( ACC 1 ) , a regulator of cellular fatty acid synthesis . ^^^ We report the cellular effects of the S 122 mutation on ACC 1 phosphorylation and demonstrate that the presence of E 124 ( absent in NDPK B ) is necessary and sufficient to permit both AMPK alpha 1 binding and substrate channeling . . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| In HepG 2 hepatocytes , polyphenols , including resveratrol ( a major polyphenol in red wine ) , apigenin , and S 17834 ( a synthetic polyphenol ) , increased phosphorylation of AMPK and its downstream target , acetyl CoA carboxylase ( ACC ) , and they increased activity of AMPK with 200 times the potency of metformin . ^^^ Furthermore , treatment of DMLDLR ( / ) mice with S 17834 prevented the decrease in AMPK and ACC phosphorylation and the lipid accumulation in the liver , and it also inhibited hyperlipidemia and the acceleration of aortic lesion development . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| To characterize the nature of the defects in lipid metabolism and to evaluate the effects of thiazolidinedione treatment , we analyzed the levels of triacylglycerol , long chain fatty acyl coA , malonyl CoA , fatty acid oxidation , AMP activated protein kinase ( AMPK ) , acetyl CoA carboxylase ( ACC ) , malonyl CoA decarboxylase , and fatty acid transport proteins in muscle biopsies from nondiabetic lean , obese , and type 2 subjects before and after an euglycemic hyperinsulinemic clamp as well as pre and post 3 month rosiglitazone treatment . ^^^ We observed that low AMPK and high ACC activities resulted in elevation of malonyl CoA levels and lower fatty acid oxidation rates . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| Thrombin stimulation led to phosphorylation of acetyl coenzyme A carboxylase ( ACC ) and endothelial nitric oxide synthase ( eNOS ) , two downstream targets of AMPK . ^^^ Inhibition or downregulation of CaMKKbeta or AMPK abolished phosphorylation of ACC in response to thrombin but had no effect on eNOS phosphorylation , indicating that thrombin stimulated phosphorylation of eNOS is not mediated by AMPK . ^^^ |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13131 and Q13085 |
Pubmed |
SVM Score :0.0 |
| NA |
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