phospho acc p acc  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho acc p acc
    Phospho Acc P Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho acc p acc  (Cell Signaling Technology Inc)


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    acetyl coa carboxylase acc  (Cell Signaling Technology Inc)


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    Acetyl Coa Carboxylase Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p acc ser79  (Cell Signaling Technology Inc)


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    phospho acetyl coa carboxylase phosphoacc 1  (Cell Signaling Technology Inc)


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    phospho acc ser79  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho acc ser79
    (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC <t>Ser79</t> levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.
    Phospho Acc Ser79, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Uncoupling of the LKB1-AMPKα Energy Sensor Pathway by Growth Factors and Oncogenic BRAF V600E"

    Article Title: Uncoupling of the LKB1-AMPKα Energy Sensor Pathway by Growth Factors and Oncogenic BRAF V600E

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0004771

    (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC Ser79 levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.
    Figure Legend Snippet: (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC Ser79 levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.

    Techniques Used: Mutagenesis, SDS Page, Western Blot, Activation Assay, Inhibition, Transfection

    total acc  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total acc
    Total Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    acetyl coa carboxylase acc ser79  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc acetyl coa carboxylase acc ser79
    Platycodi Radix activates AMPK and ACC phosphorylation in C2C12 myotubes. (a) Differentiated C2C12 myotubes were stimulated with various concentration (1, 10, 100, 400 μ g/mL) of PR for 1 hr. (b) Compound C (20 μ M) was pretreated for 30 min before stimulation of 10 μ g/mL PR. The cell lysates were analyzed by Western blotting for pAMPK (Thr172) and pACC <t>(Ser79).</t> The anti- β -actin blot was visualized as an internal control.
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    1) Product Images from "Long-Term Consumption of Platycodi Radix Ameliorates Obesity and Insulin Resistance via the Activation of AMPK Pathways"

    Article Title: Long-Term Consumption of Platycodi Radix Ameliorates Obesity and Insulin Resistance via the Activation of AMPK Pathways

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2012/759143

    Platycodi Radix activates AMPK and ACC phosphorylation in C2C12 myotubes. (a) Differentiated C2C12 myotubes were stimulated with various concentration (1, 10, 100, 400 μ g/mL) of PR for 1 hr. (b) Compound C (20 μ M) was pretreated for 30 min before stimulation of 10 μ g/mL PR. The cell lysates were analyzed by Western blotting for pAMPK (Thr172) and pACC (Ser79). The anti- β -actin blot was visualized as an internal control.
    Figure Legend Snippet: Platycodi Radix activates AMPK and ACC phosphorylation in C2C12 myotubes. (a) Differentiated C2C12 myotubes were stimulated with various concentration (1, 10, 100, 400 μ g/mL) of PR for 1 hr. (b) Compound C (20 μ M) was pretreated for 30 min before stimulation of 10 μ g/mL PR. The cell lysates were analyzed by Western blotting for pAMPK (Thr172) and pACC (Ser79). The anti- β -actin blot was visualized as an internal control.

    Techniques Used: Concentration Assay, Western Blot

    Administration of Platycodi Radix activates the ACC/AMPK phosphorylation in the muscle of obese mice. Mice were on 10% kCal ND, 60% kCal HFD, 0.1% and 1% PR in 60% kCal HFD for 10 weeks. Protein was extracted from individual frozen gastrocnemius muscles. (a) It is immunoblotted with pAMPK (Thr172) and pACC (Ser79) antibodies. The anti- β -actin blot was visualized as an internal control. (b) pAMPK and (c) pACC levels were quantitated by image densitometry and normalized by β -actin expression. # P < 0.05; ## P < 0.01 on HFD versus WBF PR-treated group.
    Figure Legend Snippet: Administration of Platycodi Radix activates the ACC/AMPK phosphorylation in the muscle of obese mice. Mice were on 10% kCal ND, 60% kCal HFD, 0.1% and 1% PR in 60% kCal HFD for 10 weeks. Protein was extracted from individual frozen gastrocnemius muscles. (a) It is immunoblotted with pAMPK (Thr172) and pACC (Ser79) antibodies. The anti- β -actin blot was visualized as an internal control. (b) pAMPK and (c) pACC levels were quantitated by image densitometry and normalized by β -actin expression. # P < 0.05; ## P < 0.01 on HFD versus WBF PR-treated group.

    Techniques Used: Expressing

    p acc  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p acc
    Western blotting images of protein expression and protein phosphorylation related to the <t>leptin-AMPK-ACC</t> signaling pathway of different groups of type 2 diabetes rats. (a) Leptin and its receptor. (b) AMPK α 1/2 and p-AMPK α 1/2. (c) AMPK α 1 and p-AMPK α 1. (d) AMPK α 2 and p-AMPK α 2. (e) ACC <t>and</t> <t>p-ACC.</t> (f) GADPH as an internal standard.
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    1) Product Images from "Effects of Acute Exercise and Chronic Exercise on the Liver Leptin-AMPK-ACC Signaling Pathway in Rats with Type 2 Diabetes"

    Article Title: Effects of Acute Exercise and Chronic Exercise on the Liver Leptin-AMPK-ACC Signaling Pathway in Rats with Type 2 Diabetes

    Journal: Journal of Diabetes Research

    doi: 10.1155/2013/946432

    Western blotting images of protein expression and protein phosphorylation related to the leptin-AMPK-ACC signaling pathway of different groups of type 2 diabetes rats. (a) Leptin and its receptor. (b) AMPK α 1/2 and p-AMPK α 1/2. (c) AMPK α 1 and p-AMPK α 1. (d) AMPK α 2 and p-AMPK α 2. (e) ACC and p-ACC. (f) GADPH as an internal standard.
    Figure Legend Snippet: Western blotting images of protein expression and protein phosphorylation related to the leptin-AMPK-ACC signaling pathway of different groups of type 2 diabetes rats. (a) Leptin and its receptor. (b) AMPK α 1/2 and p-AMPK α 1/2. (c) AMPK α 1 and p-AMPK α 1. (d) AMPK α 2 and p-AMPK α 2. (e) ACC and p-ACC. (f) GADPH as an internal standard.

    Techniques Used: Western Blot, Expressing

    Histograph showing the effects of exercise on the leptin-AMPK-ACC pathway in type 2 diabetes rats. The relative levels of protein phosphorylation and protein expression related to the leptin-AMPK-ACC signaling pathway on different groups were shown. (a) Leptin and its receptor. (b) AMPK1/2 and p-AMPK1/2 (Thr 172 ). (c) AMPK α 1 and p-AMPK α 1 (Thr 172 ). (d) AMPK α 2 and p-AMPK α 2 (Thr 172 ). (e) ACC and p-ACC (Ser 79 ). Note: in comparison with the control group: ** P < 0.01, * P < 0.05; in comparison with the diabetes group: ## P < 0.01, # P < 0.05 ( n = 8).
    Figure Legend Snippet: Histograph showing the effects of exercise on the leptin-AMPK-ACC pathway in type 2 diabetes rats. The relative levels of protein phosphorylation and protein expression related to the leptin-AMPK-ACC signaling pathway on different groups were shown. (a) Leptin and its receptor. (b) AMPK1/2 and p-AMPK1/2 (Thr 172 ). (c) AMPK α 1 and p-AMPK α 1 (Thr 172 ). (d) AMPK α 2 and p-AMPK α 2 (Thr 172 ). (e) ACC and p-ACC (Ser 79 ). Note: in comparison with the control group: ** P < 0.01, * P < 0.05; in comparison with the diabetes group: ## P < 0.01, # P < 0.05 ( n = 8).

    Techniques Used: Expressing

    acetyl coa carboxylase acc  (Cell Signaling Technology Inc)


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    total acc  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total acc
    <t>P-AMPK</t> relative to t-AMPK in (A) red gastroenemius, (C) soleus and (E) white gastroenemius. <t>P-ACC</t> relative to total t-ACC in (B) red gastroenemius (D) soleus and (F) white gastroenemius. All data were expressed as the mean ± S.E.M of 4–8 mice/group. *p<0.05, **p<0.01 (compared with the HFDN group) # p<0.05 (compared with the DMN group)
    Total Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Nesfatin-1 Stimulates Fatty-Acid Oxidation by Activating AMP-Activated Protein Kinase in STZ-Induced Type 2 Diabetic Mice"

    Article Title: Nesfatin-1 Stimulates Fatty-Acid Oxidation by Activating AMP-Activated Protein Kinase in STZ-Induced Type 2 Diabetic Mice

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0083397

    P-AMPK relative to t-AMPK in (A) red gastroenemius, (C) soleus and (E) white gastroenemius. P-ACC relative to total t-ACC in (B) red gastroenemius (D) soleus and (F) white gastroenemius. All data were expressed as the mean ± S.E.M of 4–8 mice/group. *p<0.05, **p<0.01 (compared with the HFDN group) # p<0.05 (compared with the DMN group)
    Figure Legend Snippet: P-AMPK relative to t-AMPK in (A) red gastroenemius, (C) soleus and (E) white gastroenemius. P-ACC relative to total t-ACC in (B) red gastroenemius (D) soleus and (F) white gastroenemius. All data were expressed as the mean ± S.E.M of 4–8 mice/group. *p<0.05, **p<0.01 (compared with the HFDN group) # p<0.05 (compared with the DMN group)

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    (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC <t>Ser79</t> levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.
    Phospho Acc Ser79, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC <t>Ser79</t> levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.
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    Platycodi Radix activates AMPK and ACC phosphorylation in C2C12 myotubes. (a) Differentiated C2C12 myotubes were stimulated with various concentration (1, 10, 100, 400 μ g/mL) of PR for 1 hr. (b) Compound C (20 μ M) was pretreated for 30 min before stimulation of 10 μ g/mL PR. The cell lysates were analyzed by Western blotting for pAMPK (Thr172) and pACC <t>(Ser79).</t> The anti- β -actin blot was visualized as an internal control.
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    Western blotting images of protein expression and protein phosphorylation related to the <t>leptin-AMPK-ACC</t> signaling pathway of different groups of type 2 diabetes rats. (a) Leptin and its receptor. (b) AMPK α 1/2 and p-AMPK α 1/2. (c) AMPK α 1 and p-AMPK α 1. (d) AMPK α 2 and p-AMPK α 2. (e) ACC <t>and</t> <t>p-ACC.</t> (f) GADPH as an internal standard.
    P Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC Ser79 levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.

    Journal: PLoS ONE

    Article Title: Uncoupling of the LKB1-AMPKα Energy Sensor Pathway by Growth Factors and Oncogenic BRAF V600E

    doi: 10.1371/journal.pone.0004771

    Figure Lengend Snippet: (A) BRAF mutant melanoma cells have a limited response to energy withdrawal that is restored by U0126 treatment. Fifty micrograms of total lysates from UACC903, A375, SKMel28 and 37-31E melanoma cells grown in serum free high glucose medium (H.G.), serum free low glucose medium (L.G.) or serum free low glucose medium (L.G.) plus 10 µM of U0126 for 4 hours were separated by SDS-PAGE. Western-Blot shows the activation status of proteins in the RAS and LKB1-AMPK-mTOR pathways. (B) U0126 inhibitor treatment does not activate AMPK. UACC903 A375 and SKMel28 melanoma cells were grown in high glucose medium with serum in the absence or presence of 1 µM, 5 µM or 10 µM of U0126. Total protein lysates were subjected to SDS-PAGE. Western-blot shows the phosphorylation state of AMPKα in the presence of different concentrations of U0126. (C) Inhibition of BRAF signaling increases cell response to AICAR. UACC903 and SKMel28 cells were grown in complete medium; cells were treated with AICAR (1 mM) for 4 h in the presence or absence of U0126 (10 µM) inhibitor. p-LKB1 Ser428 , p-AMPK Thr172 , p-Erk1/2 Thr202/Tyr204 , p-ACC Ser79 levels were checked by western blot. (D) Sorafenib treatment and siRNA BRAF knockdown restores the metabolic stress pathway in BRAF mutant melanoma cells. In the left panel, UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of U0126 (10 µM) Western blots show the levels of p-AMPKα T172 , p-LKB1 Ser431 p-Erk1/2 Thr202/Tyr204 and pCREB Ser133 proteins under the different conditions. In the right panel SKMel28 cells were transfected with either a scramble siRNA or BRAF siRNA. 72 hours after transfection, cells were starved either in high glucose (H.G.) or low glucose (L.G.) medium for six hours. Western-blots show the levels of p-AMPKα T172 , p-Erk1/2 Thr202/Tyr204 and BRAF proteins. (E) p90 Rsk inhibitor BI-D1870 (10 µM), does not restore the metabolic stress pathway. UACC903, A375 and SKMel28 melanoma cells were grown in low glucose serum free medium+/−EGF (50 ng/ml) for 4 h in the presence or absence of BI-D1870 (10 µM). Western blots show the levels of the indicated proteins under the different conditions.

    Article Snippet: Anti-DYKDDDDK (Flag), phospho-Erk1/2 (Thr202/Tyr204), Erk1/2, phospho-ACC (Ser79), p-90 RSK (Thr359/Ser363), AMPKα, p-AMPK (Thr172), phospho-S6 ribosomal protein (Ser235/236); phosho-Bad (Ser112), anti-Bad and Bim were purchased from Cell Signaling.

    Techniques: Mutagenesis, SDS Page, Western Blot, Activation Assay, Inhibition, Transfection

    Platycodi Radix activates AMPK and ACC phosphorylation in C2C12 myotubes. (a) Differentiated C2C12 myotubes were stimulated with various concentration (1, 10, 100, 400 μ g/mL) of PR for 1 hr. (b) Compound C (20 μ M) was pretreated for 30 min before stimulation of 10 μ g/mL PR. The cell lysates were analyzed by Western blotting for pAMPK (Thr172) and pACC (Ser79). The anti- β -actin blot was visualized as an internal control.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Long-Term Consumption of Platycodi Radix Ameliorates Obesity and Insulin Resistance via the Activation of AMPK Pathways

    doi: 10.1155/2012/759143

    Figure Lengend Snippet: Platycodi Radix activates AMPK and ACC phosphorylation in C2C12 myotubes. (a) Differentiated C2C12 myotubes were stimulated with various concentration (1, 10, 100, 400 μ g/mL) of PR for 1 hr. (b) Compound C (20 μ M) was pretreated for 30 min before stimulation of 10 μ g/mL PR. The cell lysates were analyzed by Western blotting for pAMPK (Thr172) and pACC (Ser79). The anti- β -actin blot was visualized as an internal control.

    Article Snippet: Antibodies that recognize phosphorylated AMPK Thr172 and acetyl-CoA carboxylase (ACC) Ser79 were purchased from Cell Signaling Technology (Beverly, MA) and β -actin was purchased from BETHYL Laboratories (Montgomery, TX).

    Techniques: Concentration Assay, Western Blot

    Administration of Platycodi Radix activates the ACC/AMPK phosphorylation in the muscle of obese mice. Mice were on 10% kCal ND, 60% kCal HFD, 0.1% and 1% PR in 60% kCal HFD for 10 weeks. Protein was extracted from individual frozen gastrocnemius muscles. (a) It is immunoblotted with pAMPK (Thr172) and pACC (Ser79) antibodies. The anti- β -actin blot was visualized as an internal control. (b) pAMPK and (c) pACC levels were quantitated by image densitometry and normalized by β -actin expression. # P < 0.05; ## P < 0.01 on HFD versus WBF PR-treated group.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Long-Term Consumption of Platycodi Radix Ameliorates Obesity and Insulin Resistance via the Activation of AMPK Pathways

    doi: 10.1155/2012/759143

    Figure Lengend Snippet: Administration of Platycodi Radix activates the ACC/AMPK phosphorylation in the muscle of obese mice. Mice were on 10% kCal ND, 60% kCal HFD, 0.1% and 1% PR in 60% kCal HFD for 10 weeks. Protein was extracted from individual frozen gastrocnemius muscles. (a) It is immunoblotted with pAMPK (Thr172) and pACC (Ser79) antibodies. The anti- β -actin blot was visualized as an internal control. (b) pAMPK and (c) pACC levels were quantitated by image densitometry and normalized by β -actin expression. # P < 0.05; ## P < 0.01 on HFD versus WBF PR-treated group.

    Article Snippet: Antibodies that recognize phosphorylated AMPK Thr172 and acetyl-CoA carboxylase (ACC) Ser79 were purchased from Cell Signaling Technology (Beverly, MA) and β -actin was purchased from BETHYL Laboratories (Montgomery, TX).

    Techniques: Expressing

    Western blotting images of protein expression and protein phosphorylation related to the leptin-AMPK-ACC signaling pathway of different groups of type 2 diabetes rats. (a) Leptin and its receptor. (b) AMPK α 1/2 and p-AMPK α 1/2. (c) AMPK α 1 and p-AMPK α 1. (d) AMPK α 2 and p-AMPK α 2. (e) ACC and p-ACC. (f) GADPH as an internal standard.

    Journal: Journal of Diabetes Research

    Article Title: Effects of Acute Exercise and Chronic Exercise on the Liver Leptin-AMPK-ACC Signaling Pathway in Rats with Type 2 Diabetes

    doi: 10.1155/2013/946432

    Figure Lengend Snippet: Western blotting images of protein expression and protein phosphorylation related to the leptin-AMPK-ACC signaling pathway of different groups of type 2 diabetes rats. (a) Leptin and its receptor. (b) AMPK α 1/2 and p-AMPK α 1/2. (c) AMPK α 1 and p-AMPK α 1. (d) AMPK α 2 and p-AMPK α 2. (e) ACC and p-ACC. (f) GADPH as an internal standard.

    Article Snippet: The used antibodies include leptin, leptin receptors, phosphorylated (p)-AMPK α 1 (Thr 172 ), AMPK α 1, p-AMPK α 2 (Thr 172 ), AMPK α 2, p-AMPK α 1/2 (Thr 172 ), AMPK α 1/2, acetyl-CoA carboxylase (ACC), and p-ACC (Ser 79 ) (Cell Signaling Technology, Beverly, MA, USA; 1 : 1 000 dilution).

    Techniques: Western Blot, Expressing

    Histograph showing the effects of exercise on the leptin-AMPK-ACC pathway in type 2 diabetes rats. The relative levels of protein phosphorylation and protein expression related to the leptin-AMPK-ACC signaling pathway on different groups were shown. (a) Leptin and its receptor. (b) AMPK1/2 and p-AMPK1/2 (Thr 172 ). (c) AMPK α 1 and p-AMPK α 1 (Thr 172 ). (d) AMPK α 2 and p-AMPK α 2 (Thr 172 ). (e) ACC and p-ACC (Ser 79 ). Note: in comparison with the control group: ** P < 0.01, * P < 0.05; in comparison with the diabetes group: ## P < 0.01, # P < 0.05 ( n = 8).

    Journal: Journal of Diabetes Research

    Article Title: Effects of Acute Exercise and Chronic Exercise on the Liver Leptin-AMPK-ACC Signaling Pathway in Rats with Type 2 Diabetes

    doi: 10.1155/2013/946432

    Figure Lengend Snippet: Histograph showing the effects of exercise on the leptin-AMPK-ACC pathway in type 2 diabetes rats. The relative levels of protein phosphorylation and protein expression related to the leptin-AMPK-ACC signaling pathway on different groups were shown. (a) Leptin and its receptor. (b) AMPK1/2 and p-AMPK1/2 (Thr 172 ). (c) AMPK α 1 and p-AMPK α 1 (Thr 172 ). (d) AMPK α 2 and p-AMPK α 2 (Thr 172 ). (e) ACC and p-ACC (Ser 79 ). Note: in comparison with the control group: ** P < 0.01, * P < 0.05; in comparison with the diabetes group: ## P < 0.01, # P < 0.05 ( n = 8).

    Article Snippet: The used antibodies include leptin, leptin receptors, phosphorylated (p)-AMPK α 1 (Thr 172 ), AMPK α 1, p-AMPK α 2 (Thr 172 ), AMPK α 2, p-AMPK α 1/2 (Thr 172 ), AMPK α 1/2, acetyl-CoA carboxylase (ACC), and p-ACC (Ser 79 ) (Cell Signaling Technology, Beverly, MA, USA; 1 : 1 000 dilution).

    Techniques: Expressing