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  • 93
    Thermo Fisher phospho erk 1 2
    Proteins extracted from PFPE tissues are suitable for ELISAs with antibodies directed against denatured proteins. Three human malignant (breast cancer metastasis, ovarian and prostate cancer) and three non-malignant (stomach, duodenum, uterus) tissue specimens were each divided into two samples and either cryopreserved (cryo) or fixed and stabilized in the PAXgene Tissue reagents and paraffin-embedded (PFPE). Proteins were extracted with respective protocols (See ELISA, Experimental Section) using denaturing or non-denaturing extraction buffer. Results are always depicted in duplicates for each lysate. ( A ) An ELISA for non-denatured Akt (n = 2 for stomach and duodenum samples. ( C ) An ELISA for denatured <t>Erk-1/2</t> (n = 2). ( E ) An ELISA for denatured phospho-Erk-1/2 (n = 3). Western blot analysis of ( B) 12.5 µg or ( D, F ) 25 µg protein of each lysate separated by SDS-PAGE and performed using indicated antibodies.
    Phospho Erk 1 2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore erk 1 kinase activity
    Proteins extracted from PFPE tissues are suitable for ELISAs with antibodies directed against denatured proteins. Three human malignant (breast cancer metastasis, ovarian and prostate cancer) and three non-malignant (stomach, duodenum, uterus) tissue specimens were each divided into two samples and either cryopreserved (cryo) or fixed and stabilized in the PAXgene Tissue reagents and paraffin-embedded (PFPE). Proteins were extracted with respective protocols (See ELISA, Experimental Section) using denaturing or non-denaturing extraction buffer. Results are always depicted in duplicates for each lysate. ( A ) An ELISA for non-denatured Akt (n = 2 for stomach and duodenum samples. ( C ) An ELISA for denatured <t>Erk-1/2</t> (n = 2). ( E ) An ELISA for denatured phospho-Erk-1/2 (n = 3). Western blot analysis of ( B) 12.5 µg or ( D, F ) 25 µg protein of each lysate separated by SDS-PAGE and performed using indicated antibodies.
    Erk 1 Kinase Activity, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam erk1 2
    <t>MEK1/2-ERK1/2</t> signaling pathway is essential for S1P-induced MMP-2 upregulation and invasion of HTR8/SVneo cells. (A) Cells were treated with 10 nM S1P for the indicated time. The level of phosphorylated MEK1/2, ERK1/2 were determined by western blot using phospho-specific antibodies (p-MEK1/2, pERK1/2 respectively). (B), Pretreatment of cells with 10 µM U0126, an inhibitor of MEK1/2, for 60 minutes resulted in significantly less of ERK1/2 phosphorylation (B), which downregulated level of MMP-2 (C). The invasion of MEK1/2 induced by S1P was also inhibited(D). N = 3 performed in triplicate and values were expressed as mean ±SEM with p
    Erk1 2, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 1120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher erk1 2
    Effect of baicalein on cisplatin-induced MAPKs activation. Immunoblot analyses showing expression levels of phospho-p38, p38, <t>phospho-ERK1/2,</t> ERK1/2, phospho-JNK and JNK (A). Immunoblots were representative of three independent experiments. β-actin was used as internal control. Bar diagram showing densitometric analysis for relative expression of (B) p-p38/p38, (C) p-ERK/ERK and (D) p-JNK/JNK. Values are the means ± SEM (n = 3). Where Control, group of animals treated with vehicle (2% gum acacia suspension, orally) daily for 15 consecutive days; Cisplatin, group of animals treated with 2% gum acacia suspension (orally) daily for 15 consecutive days and a single intraperitoneal (i.p) injection of cisplatin (20 mg/kg body weight, dissolved in normal saline) on 12 th day; Cis+Bai-50, group of animals treated with baicalein (50 mg/kg, orally) daily for 15 consecutive days and a single intraperitoneal (i.p) injection of cisplatin (20 mg/kg body weight, dissolved in normal saline) on 12 th day. # p
    Erk1 2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 515 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam anti erk1 2
    Lasp-1 and <t>ERK1/2</t> expression levels in tumors and adjacent normal colorectal mucosa tissues. The mRNA expression of (A) Lasp-1 and (B) ERK1/2 was examined in 20 pairs of colorectal cancer and adjacent normal tissues using the reverse transcription-quantitative polymerase chain reaction. ***P
    Anti Erk1 2, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 362 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam anti erk1 2 antibody
    The protein levels of extracellular signal-regulated kinase 1 and 2 <t>(ERK1/2),</t> phosphorylated extracellular signal-regulated kinase 1 and 2 (p-ERK1/2) and rat sarcoma (Ras) as measured by Western blot analysis in casein kinase 2 interacting protein 1 (CKIP-1) short hairpin RNA (shRNA) SGC7901 cells and CKIP-1 overexpression SGC7901 cells. Data presented as mean ± SD. * P
    Anti Erk1 2 Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore phosphorylated erk1 2
    <t>ERK1/2</t> pathway mediates cord formation by VHL knockdown HMVECs. A, top left , transfection of FGFR2 siRNA (siFGFR2) reduces expression of FGFR2 protein in both control and VHL knockdown HMVECs by ~ 3-fold. Bottom left and right , knockdown of FGFR2 (siFGFR2)
    Phosphorylated Erk1 2, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 158 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abcam p erk1 2
    Effects of AMOT overexpression on the intracellular signaling. The MCF-7 cells transfected with vector or AMOT-recombinant overexpression plasmid were exposed to vehicle or 2.0 μmol/L of Apatinib for 28 h. Then, the mRNA expressions of Cyclin D1 and LATS1/2 were detected with qRT-PCR (A), and the protein levels of Cyclin D1, LATS1/2, p-YAP, <t>ERK1/2</t> and p-ERK1/2 were determined with western blot (B). *P
    P Erk1 2, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 610 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Abcam phosphorylated p erk1 2
    Effects of AMOT overexpression on the intracellular signaling. The MCF-7 cells transfected with vector or AMOT-recombinant overexpression plasmid were exposed to vehicle or 2.0 μmol/L of Apatinib for 28 h. Then, the mRNA expressions of Cyclin D1 and LATS1/2 were detected with qRT-PCR (A), and the protein levels of Cyclin D1, LATS1/2, p-YAP, <t>ERK1/2</t> and p-ERK1/2 were determined with western blot (B). *P
    Phosphorylated P Erk1 2, supplied by Abcam, used in various techniques. Bioz Stars score: 98/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc total erk 1 2
    Imatinib mesylate treatment blocks activation of the kinases Akt and Erk 1/2 in the heart
    Total Erk 1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 284 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc α erk 1 2
    Imatinib mesylate treatment blocks activation of the kinases Akt and Erk 1/2 in the heart
    α Erk 1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Cell Signaling Technology Inc phosphorylated erk 1
    Proposed molecular mechanisms for (a) the loss or (b) the preservation of liver weight by glycemic levels in the presence of insulin deficiency. In the liver of euglycemic rats with insulin deficiency, AMPK is activated and the activity of Akt, a major insulin signaling molecule, decreases (the decreased Akt activity is also influenced by PTEN activation), compared with those in hyperglycemic rats with insulin deficiency. The increased AMPK and decreased Akt activities, in turn, decrease the activity of mTOR. As a result, excessive autophagy is induced not only by the activated AMPK but also by the inhibition of protective role of mTOR against autophagy through <t>ERK-1</t> activation and caspase-3 inhibition. Then excessive autophagy leads to hepatic cell death, partially via apoptosis mediated by caspase-3 activation, resulting in the loss of liver weight in euglycemic rats with insulin deficiency. On the other hand, in the liver of hyperglycemic rats with insulin deficiency, AMPK is not activated while Akt and mTOR are activated, compared with those in euglycemic rats with insulin deficiency. Thus, excessive autophagy and hepatic cell death are prevented not only because of the protective role of mTOR against autophagy but also because of the low AMPK activity, resulting in the preservation of liver weight in hyperglycemic rats with insulin deficiency.
    Phosphorylated Erk 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Abcam phosphorylated erk 1 2
    Effect of  LNT  on  STZ ‐induced  JNK  and p38  MAPK  activation in  INS ‐1 cells. ( A ) Following pre‐incubation with  LNT  for 30 min., the cells were treated with the indicated concentrations of  LNT  and  STZ  (0.5 mM) for 24 hrs. Phospho (P‐ JNK ) and total (T‐ JNK ) form of  JNK  were analysed by Western blot assay. ( B ) Quantitative analysis of phosphorylation of  JNK  was detected as in  A . ( C )  INS ‐1 cells were treated as in  A , and the phosphorylation of p38  MAPK  (P‐P38) was determined by Western blot analysis. ( D ) Quantitative analysis of P‐P38 was detected as in  C . ( E )  INS ‐1 cells were treated as in  A , and the phosphorylation of  ERK 1/2 ( PERK 1/2) was determined by Western blot analysis. ( F ) Quantitative analysis of phosphorylation of  ERK 1/2 was detected as in  E . The data are presented as the means ±S.E.M. for three independent experiments. * P
    Phosphorylated Erk 1 2, supplied by Abcam, used in various techniques. Bioz Stars score: 89/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Abcam anti p erk1 2
    Effect of  LNT  on  STZ ‐induced  JNK  and p38  MAPK  activation in  INS ‐1 cells. ( A ) Following pre‐incubation with  LNT  for 30 min., the cells were treated with the indicated concentrations of  LNT  and  STZ  (0.5 mM) for 24 hrs. Phospho (P‐ JNK ) and total (T‐ JNK ) form of  JNK  were analysed by Western blot assay. ( B ) Quantitative analysis of phosphorylation of  JNK  was detected as in  A . ( C )  INS ‐1 cells were treated as in  A , and the phosphorylation of p38  MAPK  (P‐P38) was determined by Western blot analysis. ( D ) Quantitative analysis of P‐P38 was detected as in  C . ( E )  INS ‐1 cells were treated as in  A , and the phosphorylation of  ERK 1/2 ( PERK 1/2) was determined by Western blot analysis. ( F ) Quantitative analysis of phosphorylation of  ERK 1/2 was detected as in  E . The data are presented as the means ±S.E.M. for three independent experiments. * P
    Anti P Erk1 2, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 137 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Cell Signaling Technology Inc erk1 2 phospho erk 1 2
    Attenuation of cystitis-induced Akt and <t>ERK1/2</t> phosphorylation in the urinary bladder by NGF antibody. In the control IgG-treated animals, cystitis increased the phosphorylation levels of Akt ( A and B ) and ERK1/2 ( C and D ) in the inflamed bladder. Administration
    Erk1 2 Phospho Erk 1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam monoclonal rabbit anti erk 1
    Expression level of the apoptotic-related proteins in MCF-7 cells treated with EADs at different time point as determined by Western blot analysis. (A) Expression of p21, p53, Bax, Bcl-2, PARP and caspase-8 in MCF-7 cells treated with 25 and 50 μg/mL of EADs (B) Fold change of Bax to Bcl-2 ratio at 24 and 48 hours. (C) Expression of AKT-1, phosphor-AKT, JNK-1, phosphor-JNK, <t>ERK-1</t> and phosphor-ERK1 in MCF-7 cells treated with 25 and 50 μg/mL of EADs. The expression of proteins was normalized against beta actin and compared to the control. The data are represented as mean ± SD of at least three replicates from three independent tests. An asterisk a indicates statistically significantly different from the untreated control (P
    Monoclonal Rabbit Anti Erk 1, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc erk 1 2 antibodies
    ErbB2 small interfering (si)RNA inhibits the expression of ErbB2, Akt, and ERK <t>1/2.</t> A : cells were cultured after transfection with a specific ErbB2 siRNA or a control siRNA shortly after the time of plating. They were harvested at 48, 72, and 96 h after
    Erk 1 2 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Proteins extracted from PFPE tissues are suitable for ELISAs with antibodies directed against denatured proteins. Three human malignant (breast cancer metastasis, ovarian and prostate cancer) and three non-malignant (stomach, duodenum, uterus) tissue specimens were each divided into two samples and either cryopreserved (cryo) or fixed and stabilized in the PAXgene Tissue reagents and paraffin-embedded (PFPE). Proteins were extracted with respective protocols (See ELISA, Experimental Section) using denaturing or non-denaturing extraction buffer. Results are always depicted in duplicates for each lysate. ( A ) An ELISA for non-denatured Akt (n = 2 for stomach and duodenum samples. ( C ) An ELISA for denatured Erk-1/2 (n = 2). ( E ) An ELISA for denatured phospho-Erk-1/2 (n = 3). Western blot analysis of ( B) 12.5 µg or ( D, F ) 25 µg protein of each lysate separated by SDS-PAGE and performed using indicated antibodies.

    Journal: PLoS ONE

    Article Title: The PAXgene® Tissue System Preserves Phosphoproteins in Human Tissue Specimens and Enables Comprehensive Protein Biomarker Research

    doi: 10.1371/journal.pone.0060638

    Figure Lengend Snippet: Proteins extracted from PFPE tissues are suitable for ELISAs with antibodies directed against denatured proteins. Three human malignant (breast cancer metastasis, ovarian and prostate cancer) and three non-malignant (stomach, duodenum, uterus) tissue specimens were each divided into two samples and either cryopreserved (cryo) or fixed and stabilized in the PAXgene Tissue reagents and paraffin-embedded (PFPE). Proteins were extracted with respective protocols (See ELISA, Experimental Section) using denaturing or non-denaturing extraction buffer. Results are always depicted in duplicates for each lysate. ( A ) An ELISA for non-denatured Akt (n = 2 for stomach and duodenum samples. ( C ) An ELISA for denatured Erk-1/2 (n = 2). ( E ) An ELISA for denatured phospho-Erk-1/2 (n = 3). Western blot analysis of ( B) 12.5 µg or ( D, F ) 25 µg protein of each lysate separated by SDS-PAGE and performed using indicated antibodies.

    Article Snippet: For the Erk-1/2 (total) and phospho-Erk-1/2 [pTpY185/187] Human ELISA Kits (Invitrogen Corp., CA, USA), proteins were extracted with the Denaturing Cell Extraction Buffer (DCEB, Invitrogen Corp., CA, USA) supplemented with protease inhibitors.

    Techniques: Enzyme-linked Immunosorbent Assay, Western Blot, SDS Page

    MEK1/2-ERK1/2 signaling pathway is essential for S1P-induced MMP-2 upregulation and invasion of HTR8/SVneo cells. (A) Cells were treated with 10 nM S1P for the indicated time. The level of phosphorylated MEK1/2, ERK1/2 were determined by western blot using phospho-specific antibodies (p-MEK1/2, pERK1/2 respectively). (B), Pretreatment of cells with 10 µM U0126, an inhibitor of MEK1/2, for 60 minutes resulted in significantly less of ERK1/2 phosphorylation (B), which downregulated level of MMP-2 (C). The invasion of MEK1/2 induced by S1P was also inhibited(D). N = 3 performed in triplicate and values were expressed as mean ±SEM with p

    Journal: PLoS ONE

    Article Title: Sphingosine-1-Phosphate Promotes Extravillous Trophoblast Cell Invasion by Activating MEK/ERK/MMP-2 Signaling Pathways via S1P/S1PR1 Axis Activation

    doi: 10.1371/journal.pone.0106725

    Figure Lengend Snippet: MEK1/2-ERK1/2 signaling pathway is essential for S1P-induced MMP-2 upregulation and invasion of HTR8/SVneo cells. (A) Cells were treated with 10 nM S1P for the indicated time. The level of phosphorylated MEK1/2, ERK1/2 were determined by western blot using phospho-specific antibodies (p-MEK1/2, pERK1/2 respectively). (B), Pretreatment of cells with 10 µM U0126, an inhibitor of MEK1/2, for 60 minutes resulted in significantly less of ERK1/2 phosphorylation (B), which downregulated level of MMP-2 (C). The invasion of MEK1/2 induced by S1P was also inhibited(D). N = 3 performed in triplicate and values were expressed as mean ±SEM with p

    Article Snippet: The activation of MEK1/2, ERK1/2 was reduced by knockdown of S1PR1 ( ).

    Techniques: Western Blot

    S1P-induced MMP-2 upregulation and signaling pathways is mediated through S1PR1 receptor. (A) HTR8/SVneo cells were pretreated for 30 minutes with the S1PR1 and S1PR3 receptor antagonist VPC23019 (1 µM) before stimulation with S1P (10 nM). (B) HTR8/SVneo were pretreated for 30 minutes with the selective S1PR3 receptor antagonist CAY10444 (1 µM) before stimulation with S1P. (C) HTR8/SVneo were pretreated for 30 minutes with VPC23019 (1 µM) before stimulation with the selective S1PR1 receptor agonist SEW2871 (1 µM). (D) Cells were transfected with control siRNA or siRNAs targeting S1PR1 (50 pmol). Knockdown of S1P1 was confirmed by Real-time PCR. (E) Induction of MMP-2 by S1P was disrupted in siRNA transfected cells. (F) The levels of activated MEK1/2, ERK1/2 were determined by western blot using phospho-specific antibodies (p-MEK1/2, p-ERK1/2, respectively). N = 3 performed in triplicate and values were expressed as mean ±SEM with p

    Journal: PLoS ONE

    Article Title: Sphingosine-1-Phosphate Promotes Extravillous Trophoblast Cell Invasion by Activating MEK/ERK/MMP-2 Signaling Pathways via S1P/S1PR1 Axis Activation

    doi: 10.1371/journal.pone.0106725

    Figure Lengend Snippet: S1P-induced MMP-2 upregulation and signaling pathways is mediated through S1PR1 receptor. (A) HTR8/SVneo cells were pretreated for 30 minutes with the S1PR1 and S1PR3 receptor antagonist VPC23019 (1 µM) before stimulation with S1P (10 nM). (B) HTR8/SVneo were pretreated for 30 minutes with the selective S1PR3 receptor antagonist CAY10444 (1 µM) before stimulation with S1P. (C) HTR8/SVneo were pretreated for 30 minutes with VPC23019 (1 µM) before stimulation with the selective S1PR1 receptor agonist SEW2871 (1 µM). (D) Cells were transfected with control siRNA or siRNAs targeting S1PR1 (50 pmol). Knockdown of S1P1 was confirmed by Real-time PCR. (E) Induction of MMP-2 by S1P was disrupted in siRNA transfected cells. (F) The levels of activated MEK1/2, ERK1/2 were determined by western blot using phospho-specific antibodies (p-MEK1/2, p-ERK1/2, respectively). N = 3 performed in triplicate and values were expressed as mean ±SEM with p

    Article Snippet: The activation of MEK1/2, ERK1/2 was reduced by knockdown of S1PR1 ( ).

    Techniques: Transfection, Real-time Polymerase Chain Reaction, Western Blot

    Effect of baicalein on cisplatin-induced MAPKs activation. Immunoblot analyses showing expression levels of phospho-p38, p38, phospho-ERK1/2, ERK1/2, phospho-JNK and JNK (A). Immunoblots were representative of three independent experiments. β-actin was used as internal control. Bar diagram showing densitometric analysis for relative expression of (B) p-p38/p38, (C) p-ERK/ERK and (D) p-JNK/JNK. Values are the means ± SEM (n = 3). Where Control, group of animals treated with vehicle (2% gum acacia suspension, orally) daily for 15 consecutive days; Cisplatin, group of animals treated with 2% gum acacia suspension (orally) daily for 15 consecutive days and a single intraperitoneal (i.p) injection of cisplatin (20 mg/kg body weight, dissolved in normal saline) on 12 th day; Cis+Bai-50, group of animals treated with baicalein (50 mg/kg, orally) daily for 15 consecutive days and a single intraperitoneal (i.p) injection of cisplatin (20 mg/kg body weight, dissolved in normal saline) on 12 th day. # p

    Journal: PLoS ONE

    Article Title: Baicalein, a Bioflavonoid, Prevents Cisplatin-Induced Acute Kidney Injury by Up-Regulating Antioxidant Defenses and Down-Regulating the MAPKs and NF-κB Pathways

    doi: 10.1371/journal.pone.0134139

    Figure Lengend Snippet: Effect of baicalein on cisplatin-induced MAPKs activation. Immunoblot analyses showing expression levels of phospho-p38, p38, phospho-ERK1/2, ERK1/2, phospho-JNK and JNK (A). Immunoblots were representative of three independent experiments. β-actin was used as internal control. Bar diagram showing densitometric analysis for relative expression of (B) p-p38/p38, (C) p-ERK/ERK and (D) p-JNK/JNK. Values are the means ± SEM (n = 3). Where Control, group of animals treated with vehicle (2% gum acacia suspension, orally) daily for 15 consecutive days; Cisplatin, group of animals treated with 2% gum acacia suspension (orally) daily for 15 consecutive days and a single intraperitoneal (i.p) injection of cisplatin (20 mg/kg body weight, dissolved in normal saline) on 12 th day; Cis+Bai-50, group of animals treated with baicalein (50 mg/kg, orally) daily for 15 consecutive days and a single intraperitoneal (i.p) injection of cisplatin (20 mg/kg body weight, dissolved in normal saline) on 12 th day. # p

    Article Snippet: In total protein extract, expressions of Bax (rabbit, monoclonal, Cell Signaling Technology; 1:1000), Bcl-2 (rabbit, monoclonal, Cell Signaling Technology; 1:1000), cleaved caspase-3 (rabbit, monoclonal, Cell Signaling Technology; 1:1000), cleaved caspase-9 (mouse, monoclonal, Cell Signaling Technology; 1:1000), cleaved PARP (rabbit, monoclonal, Cell Signaling Technology; 1:1000), p53 (mouse, monoclonal, Cell Signaling Technology; 1:1000), iNOS (rabbit, monoclonal, Sigma-Aldrich; 1:500), Nrf2 (rabbit, monoclonal, Cell Signaling Technology; 1:500), HO-1 (rabbit, monoclonal, Cell Signaling Technology; 1:1000), ERK1/2 (rabbit, monoclonal, Pierce Biotechnology, 1:1000), phospho-ERK1/2 (rabbit, monoclonal, Pierce Biotechnology, 1:1000), p38 (rabbit, monoclonal, Pierce Biotechnology, 1:1000), phospho-p38 (rabbit, monoclonal, Pierce Biotechnology, 1:1000), JNK (rabbit, monoclonal, Pierce Biotechnology, 1:1000), phospho-JNK (rabbit, monoclonal, Pierce Biotechnology, 1:1000); in mitochondrial and cytosolic fractions, expression of cytochrome c (rabbit, monoclonal, Cell Signaling Technology; 1:1000); in nuclear fractions, expression of Nrf2 (rabbit, monoclonal, Cell Signaling Technology; 1:500) and NF-κB (p65) (rabbit, monoclonal, Cell Signaling Technology; 1:500) and in cytoplasmic fraction, the expressions of Nrf2 (rabbit, monoclonal, Cell Signaling Technology; 1:500), NF-κB (p65) (rabbit, monoclonal, Cell Signaling Technology; 1:500), phospho-IKKα/β (rabbit, monoclonal, Cell Signaling Technology; 1:500), phospho-IκBα (rabbit, monoclonal, Cell Signaling Technology; 1:1000) and IκBα (mouse, monoclonal, Cell Signaling Technology; 1:1000) were estimated.

    Techniques: Activation Assay, Expressing, Western Blot, Injection

    Lasp-1 and ERK1/2 expression levels in tumors and adjacent normal colorectal mucosa tissues. The mRNA expression of (A) Lasp-1 and (B) ERK1/2 was examined in 20 pairs of colorectal cancer and adjacent normal tissues using the reverse transcription-quantitative polymerase chain reaction. ***P

    Journal: Oncology Letters

    Article Title: LIM and SH3 protein 1 knockdown suppresses proliferation and metastasis of colorectal carcinoma cells via inhibition of the mitogen-activated protein kinase signaling pathway

    doi: 10.3892/ol.2018.8222

    Figure Lengend Snippet: Lasp-1 and ERK1/2 expression levels in tumors and adjacent normal colorectal mucosa tissues. The mRNA expression of (A) Lasp-1 and (B) ERK1/2 was examined in 20 pairs of colorectal cancer and adjacent normal tissues using the reverse transcription-quantitative polymerase chain reaction. ***P

    Article Snippet: Membranes were blocked by 5% BSA for 1 h at room temperature and incubated overnight at 4°C with anti-Lasp-1 (1:20,000; cat. no. ab156872), anti-ERK1/2 (1:1,000; cat. no. ab17942), anti-phospho (p-)ERK1/2 (1:500; cat. no. ab214362), anti-GAPDH (1:2,000; cat. no. ab8245) primary antibodies (Abcam, Cambridge, UK) followed by incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies (1:5,000; cat. no., ab181658, goat anti-HRP) at room temperature for 1 h (Abcam).

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    Lasp-1 and p-ERK1/2 protein expression following Lasp-1 knockdown. (A) Lasp-1 protein expression detected using immunofluorescence. The Merge panels are superimposed images of Lasp-1 staining in red and nuclei staining in blue (using DAPI). Magnification, ×400. (B) p-ERK1/2 protein expression detected using immunofluorescence. The Merge panels are superimposed images of p-ERK1/2 staining in green and nuclei staining in blue (using DAPI). Magnification, ×400. Lasp-1, LIM and SH3 protein 1; ERK, extracellular-signal-regulated kinase; p-, phospho-; NC, negative control; siRNA, small interfering RNA.

    Journal: Oncology Letters

    Article Title: LIM and SH3 protein 1 knockdown suppresses proliferation and metastasis of colorectal carcinoma cells via inhibition of the mitogen-activated protein kinase signaling pathway

    doi: 10.3892/ol.2018.8222

    Figure Lengend Snippet: Lasp-1 and p-ERK1/2 protein expression following Lasp-1 knockdown. (A) Lasp-1 protein expression detected using immunofluorescence. The Merge panels are superimposed images of Lasp-1 staining in red and nuclei staining in blue (using DAPI). Magnification, ×400. (B) p-ERK1/2 protein expression detected using immunofluorescence. The Merge panels are superimposed images of p-ERK1/2 staining in green and nuclei staining in blue (using DAPI). Magnification, ×400. Lasp-1, LIM and SH3 protein 1; ERK, extracellular-signal-regulated kinase; p-, phospho-; NC, negative control; siRNA, small interfering RNA.

    Article Snippet: Membranes were blocked by 5% BSA for 1 h at room temperature and incubated overnight at 4°C with anti-Lasp-1 (1:20,000; cat. no. ab156872), anti-ERK1/2 (1:1,000; cat. no. ab17942), anti-phospho (p-)ERK1/2 (1:500; cat. no. ab214362), anti-GAPDH (1:2,000; cat. no. ab8245) primary antibodies (Abcam, Cambridge, UK) followed by incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies (1:5,000; cat. no., ab181658, goat anti-HRP) at room temperature for 1 h (Abcam).

    Techniques: Expressing, Immunofluorescence, Staining, Negative Control, Small Interfering RNA

    Lasp-1 and ERK1/2 expression in SW480 cells following Lasp-1 knockdown. (A) Lasp-1 and ERK1/2 mRNA expression determined using reverse transcription-quantitative polymerase chain reaction (n=3; *P

    Journal: Oncology Letters

    Article Title: LIM and SH3 protein 1 knockdown suppresses proliferation and metastasis of colorectal carcinoma cells via inhibition of the mitogen-activated protein kinase signaling pathway

    doi: 10.3892/ol.2018.8222

    Figure Lengend Snippet: Lasp-1 and ERK1/2 expression in SW480 cells following Lasp-1 knockdown. (A) Lasp-1 and ERK1/2 mRNA expression determined using reverse transcription-quantitative polymerase chain reaction (n=3; *P

    Article Snippet: Membranes were blocked by 5% BSA for 1 h at room temperature and incubated overnight at 4°C with anti-Lasp-1 (1:20,000; cat. no. ab156872), anti-ERK1/2 (1:1,000; cat. no. ab17942), anti-phospho (p-)ERK1/2 (1:500; cat. no. ab214362), anti-GAPDH (1:2,000; cat. no. ab8245) primary antibodies (Abcam, Cambridge, UK) followed by incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies (1:5,000; cat. no., ab181658, goat anti-HRP) at room temperature for 1 h (Abcam).

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    LR blocks mitogen-associated protein kinase and NF-κB pathways in LPS-induced mice with ALI. (A) Phosphorylated p38, phosphorylated ERK1/2 and phosphorylated JNK levels were examined by use of western blot analysis. (B) IKK-α, IκBα and NF-κB phosphorylation were tested through western blot analysis. Data are represented as mean ± standard error of the mean of three independent experiments (n=6). ++ P

    Journal: International Journal of Molecular Medicine

    Article Title: Linarin prevents LPS-induced acute lung injury by suppressing oxidative stress and inflammation via inhibition of TXNIP/NLRP3 and NF-κB pathways

    doi: 10.3892/ijmm.2018.3710

    Figure Lengend Snippet: LR blocks mitogen-associated protein kinase and NF-κB pathways in LPS-induced mice with ALI. (A) Phosphorylated p38, phosphorylated ERK1/2 and phosphorylated JNK levels were examined by use of western blot analysis. (B) IKK-α, IκBα and NF-κB phosphorylation were tested through western blot analysis. Data are represented as mean ± standard error of the mean of three independent experiments (n=6). ++ P

    Article Snippet: The primary antibodies: Rabbit anti-NLRP3 (1:1,000, cat. no. 15101), rabbit anti-ASC (1:1,000, cat. no. 67824) (both from Cell Signaling Technology, Inc., Danvers, MA, USA), rabbit anti-caspase-1 (1:1,000, ab1872), rabbit anti-Nrf2 (1:1,000, ab31163) (both from Abcam), rabbit anti-HO-1 (1:1,000, cat. no. 70081), rabbit anti-p-ERK1/2 (1:1,000, cat. no. 4370; Cell Signaling Technology, Inc.), rabbit anti-ERK1/2 (1:1,000, ab17942; Abcam), rabbit anti-p-JNK (1:1,000, cat. no. 9255), rabbit anti-JNK (1:1,000, #9252) (both from Cell Signaling Technology, Inc.), rabbit anti-XO (1:1,000, ab109235), rabbit anti-TXNIP (1:1,000, ab188865) (both from Abcam), rabbit anti-p-p38 (1:1,000, cat. no. 9211), rabbit anti-p38 (1:1,000, cat. no. 8690), rabbit anti-p-IKKα (1:1,000, cat. no. 2697), rabbit anti-IKKα (1:1,000, cat. no. 2682) (all from Cell Signaling Technology, Inc.), anti-NF-κB (1:1,000, ab19870), rabbit anti-p-NF-κB (1:1,000, ab86299), rabbit anti-IκBα (1:1,000, ab32518), rabbit anti-p-IκBα (1:1,000, ab24783) (all from Abcam), rabbit and anti-GAPDH (1:500, sc-293335, Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Mouse Assay, Western Blot

    LR reduces oxidative stress through suppressing the TXNIP/NLRP3 pathway in LPS-treated cells. The lung epithelia cells of BEAS-2B were pretreated with different concentrations of LR (0, 20, 40 and 80 µ M) for 24 h, followed by LPS exposure for 1 h. Then, all cells were harvested for the following research. (A) 2′-7′-Dichlorofluorescein (DCF) analysis was used to calculate ROS generation, and the representative images were displayed. The scale bar is 50 µ m. (B) The quantification of ROS production was exhibited. (C) Western blot analysis of XO, TXNIP, LPRP3, apoptosis-associated speck-like protein containing a C-terminal caspase recruitment domain (ASC) and caspase-1 in LPS-treated cells in the presence or absence of LR. (D) p-p38, p-ERK1/2 and p-JNK levels were measured through western blot analysis. Data are represented as mean ± standard error of the mean of three independent experiments (n=6). +++P

    Journal: International Journal of Molecular Medicine

    Article Title: Linarin prevents LPS-induced acute lung injury by suppressing oxidative stress and inflammation via inhibition of TXNIP/NLRP3 and NF-κB pathways

    doi: 10.3892/ijmm.2018.3710

    Figure Lengend Snippet: LR reduces oxidative stress through suppressing the TXNIP/NLRP3 pathway in LPS-treated cells. The lung epithelia cells of BEAS-2B were pretreated with different concentrations of LR (0, 20, 40 and 80 µ M) for 24 h, followed by LPS exposure for 1 h. Then, all cells were harvested for the following research. (A) 2′-7′-Dichlorofluorescein (DCF) analysis was used to calculate ROS generation, and the representative images were displayed. The scale bar is 50 µ m. (B) The quantification of ROS production was exhibited. (C) Western blot analysis of XO, TXNIP, LPRP3, apoptosis-associated speck-like protein containing a C-terminal caspase recruitment domain (ASC) and caspase-1 in LPS-treated cells in the presence or absence of LR. (D) p-p38, p-ERK1/2 and p-JNK levels were measured through western blot analysis. Data are represented as mean ± standard error of the mean of three independent experiments (n=6). +++P

    Article Snippet: The primary antibodies: Rabbit anti-NLRP3 (1:1,000, cat. no. 15101), rabbit anti-ASC (1:1,000, cat. no. 67824) (both from Cell Signaling Technology, Inc., Danvers, MA, USA), rabbit anti-caspase-1 (1:1,000, ab1872), rabbit anti-Nrf2 (1:1,000, ab31163) (both from Abcam), rabbit anti-HO-1 (1:1,000, cat. no. 70081), rabbit anti-p-ERK1/2 (1:1,000, cat. no. 4370; Cell Signaling Technology, Inc.), rabbit anti-ERK1/2 (1:1,000, ab17942; Abcam), rabbit anti-p-JNK (1:1,000, cat. no. 9255), rabbit anti-JNK (1:1,000, #9252) (both from Cell Signaling Technology, Inc.), rabbit anti-XO (1:1,000, ab109235), rabbit anti-TXNIP (1:1,000, ab188865) (both from Abcam), rabbit anti-p-p38 (1:1,000, cat. no. 9211), rabbit anti-p38 (1:1,000, cat. no. 8690), rabbit anti-p-IKKα (1:1,000, cat. no. 2697), rabbit anti-IKKα (1:1,000, cat. no. 2682) (all from Cell Signaling Technology, Inc.), anti-NF-κB (1:1,000, ab19870), rabbit anti-p-NF-κB (1:1,000, ab86299), rabbit anti-IκBα (1:1,000, ab32518), rabbit anti-p-IκBα (1:1,000, ab24783) (all from Abcam), rabbit and anti-GAPDH (1:500, sc-293335, Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Western Blot

    ROS production is involved in LR-reduced oxidative stress and inflammation in LPS-treated cells. (A) The lung epithelia cells of BEAS-2B were pretreated with LR (80 µ M) for 24 h, followed by LPS exposure for another 1 h, and then for addition of 10 mM N-acetylcysteine (NAC) or 5 mM ATP for 0–60 min as indicated. Then, reactive oxygen species production was measured as the relative fluorescence intensity. The lung epithelia cells of BEAS-2B were pretreated with different concentrations of LR (0, 20, 40 and 80 µ M) for 24 h, followed by LPS exposure for another 1 h, and then for addition of 5 mM ATP for 60 min. Finally, all cells were harvested for further experiments. (B) XO, TXNIP, p-p38, p-ERK1/2 and p-JNK protein levels were measured using western blot analysis. (C) Western blot analysis of p-IKK-α, p-IκBα and p-NF-κB were exhibited. (D) TNF-α, IL-1β, IL-6, MCP-5, MIP-1α, IL-10, iNOS and COX2 gene levels were evaluated using reverse transcription-quantitative polymerase chain reaction assays. Data are represented as mean ± standard error of the mean of three independent experiments (n=6). +++ P

    Journal: International Journal of Molecular Medicine

    Article Title: Linarin prevents LPS-induced acute lung injury by suppressing oxidative stress and inflammation via inhibition of TXNIP/NLRP3 and NF-κB pathways

    doi: 10.3892/ijmm.2018.3710

    Figure Lengend Snippet: ROS production is involved in LR-reduced oxidative stress and inflammation in LPS-treated cells. (A) The lung epithelia cells of BEAS-2B were pretreated with LR (80 µ M) for 24 h, followed by LPS exposure for another 1 h, and then for addition of 10 mM N-acetylcysteine (NAC) or 5 mM ATP for 0–60 min as indicated. Then, reactive oxygen species production was measured as the relative fluorescence intensity. The lung epithelia cells of BEAS-2B were pretreated with different concentrations of LR (0, 20, 40 and 80 µ M) for 24 h, followed by LPS exposure for another 1 h, and then for addition of 5 mM ATP for 60 min. Finally, all cells were harvested for further experiments. (B) XO, TXNIP, p-p38, p-ERK1/2 and p-JNK protein levels were measured using western blot analysis. (C) Western blot analysis of p-IKK-α, p-IκBα and p-NF-κB were exhibited. (D) TNF-α, IL-1β, IL-6, MCP-5, MIP-1α, IL-10, iNOS and COX2 gene levels were evaluated using reverse transcription-quantitative polymerase chain reaction assays. Data are represented as mean ± standard error of the mean of three independent experiments (n=6). +++ P

    Article Snippet: The primary antibodies: Rabbit anti-NLRP3 (1:1,000, cat. no. 15101), rabbit anti-ASC (1:1,000, cat. no. 67824) (both from Cell Signaling Technology, Inc., Danvers, MA, USA), rabbit anti-caspase-1 (1:1,000, ab1872), rabbit anti-Nrf2 (1:1,000, ab31163) (both from Abcam), rabbit anti-HO-1 (1:1,000, cat. no. 70081), rabbit anti-p-ERK1/2 (1:1,000, cat. no. 4370; Cell Signaling Technology, Inc.), rabbit anti-ERK1/2 (1:1,000, ab17942; Abcam), rabbit anti-p-JNK (1:1,000, cat. no. 9255), rabbit anti-JNK (1:1,000, #9252) (both from Cell Signaling Technology, Inc.), rabbit anti-XO (1:1,000, ab109235), rabbit anti-TXNIP (1:1,000, ab188865) (both from Abcam), rabbit anti-p-p38 (1:1,000, cat. no. 9211), rabbit anti-p38 (1:1,000, cat. no. 8690), rabbit anti-p-IKKα (1:1,000, cat. no. 2697), rabbit anti-IKKα (1:1,000, cat. no. 2682) (all from Cell Signaling Technology, Inc.), anti-NF-κB (1:1,000, ab19870), rabbit anti-p-NF-κB (1:1,000, ab86299), rabbit anti-IκBα (1:1,000, ab32518), rabbit anti-p-IκBα (1:1,000, ab24783) (all from Abcam), rabbit and anti-GAPDH (1:500, sc-293335, Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Fluorescence, Western Blot, Real-time Polymerase Chain Reaction

    The protein levels of extracellular signal-regulated kinase 1 and 2 (ERK1/2), phosphorylated extracellular signal-regulated kinase 1 and 2 (p-ERK1/2) and rat sarcoma (Ras) as measured by Western blot analysis in casein kinase 2 interacting protein 1 (CKIP-1) short hairpin RNA (shRNA) SGC7901 cells and CKIP-1 overexpression SGC7901 cells. Data presented as mean ± SD. * P

    Journal: The Journal of International Medical Research

    Article Title: High expression of the CKIP-1 gene might promote apoptosis through downregulation of the Ras/ERK signalling pathway in the intestinal type of gastric cancer

    doi: 10.1177/0300060520909025

    Figure Lengend Snippet: The protein levels of extracellular signal-regulated kinase 1 and 2 (ERK1/2), phosphorylated extracellular signal-regulated kinase 1 and 2 (p-ERK1/2) and rat sarcoma (Ras) as measured by Western blot analysis in casein kinase 2 interacting protein 1 (CKIP-1) short hairpin RNA (shRNA) SGC7901 cells and CKIP-1 overexpression SGC7901 cells. Data presented as mean ± SD. * P

    Article Snippet: After blocking with 5% dry milk for 1 h at room temperature, the PVDF membranes were incubated with anti-CKIP-1 antibody, anti-Bcl-2 antibody, anti-Bax antibody, anti-cleaved caspase-3 antibody, anti-cleaved caspase-9 antibody, anti-Ras antibody, anti-ERK1/2 antibody and anti-p-ERK1/2 antibody (all 1:2000 dilution; Abcam) or anti-GAPDH antibody (1:20000 dilution; Sigma-Aldrich, St Louis, MO, USA) for 2 h at room temperature.

    Techniques: Western Blot, shRNA, Over Expression

    Myricitrin suppresses PDGFRβ, Akt and Erk1/2 signaling pathways activated by PDGF-BB in VSMCs. A. The proteins PDGFRβ, Akt, Erk1/2, p-Akt and p-Erk1/2 were determined using western blotting with corresponding antibodies. β-actin was used as an internal control. B-D. Data are expressed as mean ± SD; *P

    Journal: International Journal of Clinical and Experimental Medicine

    Article Title: Myricitrin inhibits PDGF-BB-stimulated vascular smooth muscle cell proliferation and migration through suppressing PDGFRβ/Akt/Erk signaling

    doi:

    Figure Lengend Snippet: Myricitrin suppresses PDGFRβ, Akt and Erk1/2 signaling pathways activated by PDGF-BB in VSMCs. A. The proteins PDGFRβ, Akt, Erk1/2, p-Akt and p-Erk1/2 were determined using western blotting with corresponding antibodies. β-actin was used as an internal control. B-D. Data are expressed as mean ± SD; *P

    Article Snippet: Mouse anti-Erk1/2 monoclonal antibody, mouse anti-Akt monoclonal antibody, mouse anti-PDGF-Rβ monoclonal antibody, mouse anti-p-Erk1/2 monoclonal antibody, mouse anti-p-Akt monoclonal antibody, mouse anti-cyclin-dependent kinases (CDK) 2 monoclonal antibody, mouse anti-CDK4 monoclonal antibody, mouse anti-cyclin D1 monoclonal antibody, mouse anti-cyclin E monoclonal antibody and mouse anti-β-actin monoclonal antibody were obtained from Abcam (Cambridge, MA).

    Techniques: Western Blot

    E2 enhances Schwann cell differentiation via ERβ-ERK1/2 signaling. (A) Immunohistochemistry with anti-ERα (green) and anti-ERβ (red) of Schwann cells. Scale bar, 50 μm. (B) ERα and ERβ expression in the cultured pure Schwann cells and DRG neurons s, as shown by western blotting. (C) Western blotting compared the MAG expression in differentiated SCs treated with E2 alone or with E2 plus ICI182780 or MPP (antagonist of ERα) or PHTPP (antagonist of ERβ) for 3 days. (D) Western blotting compared the MAG and P0 expression in differentiated SCs treated with E2 alone or with E2 plus PHTPP or PD98059 (antagonist of MEK1/2) or LY294002 (antagonist of PI3K) for 3 days, and vehicle as control, β-actin served as an internal standard. (E,F) Showed the phosphorylation of AKT (E) and ERK 1/2 (F) in differentiated SCs after treatments with E2 alone or with E2 plus ICI182780 or MPP or PHTPP for 3 days. ∗∗ p

    Journal: Frontiers in Pharmacology

    Article Title: 17β-Estradiol Enhances Schwann Cell Differentiation via the ERβ-ERK1/2 Signaling Pathway and Promotes Remyelination in Injured Sciatic Nerves

    doi: 10.3389/fphar.2018.01026

    Figure Lengend Snippet: E2 enhances Schwann cell differentiation via ERβ-ERK1/2 signaling. (A) Immunohistochemistry with anti-ERα (green) and anti-ERβ (red) of Schwann cells. Scale bar, 50 μm. (B) ERα and ERβ expression in the cultured pure Schwann cells and DRG neurons s, as shown by western blotting. (C) Western blotting compared the MAG expression in differentiated SCs treated with E2 alone or with E2 plus ICI182780 or MPP (antagonist of ERα) or PHTPP (antagonist of ERβ) for 3 days. (D) Western blotting compared the MAG and P0 expression in differentiated SCs treated with E2 alone or with E2 plus PHTPP or PD98059 (antagonist of MEK1/2) or LY294002 (antagonist of PI3K) for 3 days, and vehicle as control, β-actin served as an internal standard. (E,F) Showed the phosphorylation of AKT (E) and ERK 1/2 (F) in differentiated SCs after treatments with E2 alone or with E2 plus ICI182780 or MPP or PHTPP for 3 days. ∗∗ p

    Article Snippet: Antibodies: Chicken anti-myelin protein zero (P0), rabbit anti-phospho-AKT, anti-AKT, anti-phospho-PI3 Kinase, anti-PI3 Kinase, anti-ERK1/2 (ERK), anti-phospho-ERK1/2 were from Abcam, Rabbit anti-myelin associated glycoprotein (MAG), Mouse anti-neurofilament 200 (NF200), anti-β-actin, anti-S100β were from Sigma, and Rabbit anti-ERα and goat anti-ERβ were from Santa Cruz Biotechnology.

    Techniques: Cell Differentiation, Immunohistochemistry, Expressing, Cell Culture, Western Blot

    miR-195 targets FGF-18 and regulates its downstream pathway. ( A ) FGF-18 3′UTR had a binding site containing seven bases for miR-195, as predicted by online prediction software TargetScan (Available online: http://www.targetscan.org) and RNAhybrid (Available online: https://bibiserv.cebitec.uni-bielefeld.de/rnahybrid ); ( B ) miR-195 expression after different intervention when normalized to the control group was detected by real-time PCR and GAPDH and was set as an internal control. ( C – F ) miR-195 could regulate FGF-18 expression ( C ), then affect the phosphorylation level of FGFR3 (FGFR3 p-Tyr724 ) ( D ), ERK1/2 (ERK1/2 p-Thr202/Tyr204 ) ( E ), and affect the expression level of SOX ( F ) as determined by western blot test method and real-time PCR. GAPDH was set as the internal control and all data were normalized to the control group, respectively. ** p

    Journal: International Journal of Molecular Sciences

    Article Title: Decrease of miR-195 Promotes Chondrocytes Proliferation and Maintenance of Chondrogenic Phenotype via Targeting FGF-18 Pathway

    doi: 10.3390/ijms18050975

    Figure Lengend Snippet: miR-195 targets FGF-18 and regulates its downstream pathway. ( A ) FGF-18 3′UTR had a binding site containing seven bases for miR-195, as predicted by online prediction software TargetScan (Available online: http://www.targetscan.org) and RNAhybrid (Available online: https://bibiserv.cebitec.uni-bielefeld.de/rnahybrid ); ( B ) miR-195 expression after different intervention when normalized to the control group was detected by real-time PCR and GAPDH and was set as an internal control. ( C – F ) miR-195 could regulate FGF-18 expression ( C ), then affect the phosphorylation level of FGFR3 (FGFR3 p-Tyr724 ) ( D ), ERK1/2 (ERK1/2 p-Thr202/Tyr204 ) ( E ), and affect the expression level of SOX ( F ) as determined by western blot test method and real-time PCR. GAPDH was set as the internal control and all data were normalized to the control group, respectively. ** p

    Article Snippet: The following antibodies were used: mouse anti-FGF-18 antibody (Absci, Vancouver, WA, USA; dilution rates of 1:1000), mouse anti-FGFR3 antibody (Abcam, Cambridge, UK; dilution rates of 1:1000), mouse anti anti-phospho-FGFR3 antibody (Abcam; dilution rates of 1:1000), mouse anti-ERK1/2 antibody (Abcam, dilution rates of 1:1000), mouse anti-phospho-ERK1/2 (Cell Signaling Technologies, Danvers, MA, USA; dilution rates of 1:1000), and mouse anti-GAPDH antibody (Abcam, concentration of 0.5 µg/mL).

    Techniques: Binding Assay, Software, Expressing, Real-time Polymerase Chain Reaction, Western Blot

    ERK1/2 pathway mediates cord formation by VHL knockdown HMVECs. A, top left , transfection of FGFR2 siRNA (siFGFR2) reduces expression of FGFR2 protein in both control and VHL knockdown HMVECs by ~ 3-fold. Bottom left and right , knockdown of FGFR2 (siFGFR2)

    Journal: Cancer research

    Article Title: Endothelial Function of von Hippel-Lindau Tumor Suppressor Gene: Control of Fibroblast Growth Factor Receptor Signaling

    doi: 10.1158/0008-5472.CAN-07-6003

    Figure Lengend Snippet: ERK1/2 pathway mediates cord formation by VHL knockdown HMVECs. A, top left , transfection of FGFR2 siRNA (siFGFR2) reduces expression of FGFR2 protein in both control and VHL knockdown HMVECs by ~ 3-fold. Bottom left and right , knockdown of FGFR2 (siFGFR2)

    Article Snippet: Mouse monoclonal antibodies are doubly phosphorylated ERK1/2 (dp-ERK; Sigma), β-actin (Sigma), VHL (Neomarkers and Cell Signaling), HIF-1α (Novus Biologicals), phosphothreonine (Zymed), and phosphoserine (Zymed).

    Techniques: Transfection, Expressing

    Effects of AMOT overexpression on the intracellular signaling. The MCF-7 cells transfected with vector or AMOT-recombinant overexpression plasmid were exposed to vehicle or 2.0 μmol/L of Apatinib for 28 h. Then, the mRNA expressions of Cyclin D1 and LATS1/2 were detected with qRT-PCR (A), and the protein levels of Cyclin D1, LATS1/2, p-YAP, ERK1/2 and p-ERK1/2 were determined with western blot (B). *P

    Journal: American Journal of Translational Research

    Article Title: Apatinib suppresses breast cancer cells proliferation and invasion via angiomotin inhibition

    doi:

    Figure Lengend Snippet: Effects of AMOT overexpression on the intracellular signaling. The MCF-7 cells transfected with vector or AMOT-recombinant overexpression plasmid were exposed to vehicle or 2.0 μmol/L of Apatinib for 28 h. Then, the mRNA expressions of Cyclin D1 and LATS1/2 were detected with qRT-PCR (A), and the protein levels of Cyclin D1, LATS1/2, p-YAP, ERK1/2 and p-ERK1/2 were determined with western blot (B). *P

    Article Snippet: After blocking with 5% skim milk powder, blots were incubated with primary antibodies against AMOT, YAP, p-YAP, LAST1, LAST2, Cyclin D1, ERK1/2, p-ERK1/2 and GAPDH (all from Abcam, Cambridge, US) overnight at 4°C.

    Techniques: Over Expression, Transfection, Plasmid Preparation, Recombinant, Quantitative RT-PCR, Western Blot

    Effects of Apatinib on the intracellular signaling. MCF-7 and T-474 cells were treated with vehicle or 0.2, 2 or 20 μmol/L of Apatinib for 48 h. Then, the mRNA expressions of VEGFR-2, AMOT, YAP, LATS1/2 and Cyclin D1 were determined with qRT-PCR (A), and the protein levels of YAP, p-YAP, LATS1/2, Cyclin D1, ERK, p-ERK1/2 were determined with Western blotting (B). *P

    Journal: American Journal of Translational Research

    Article Title: Apatinib suppresses breast cancer cells proliferation and invasion via angiomotin inhibition

    doi:

    Figure Lengend Snippet: Effects of Apatinib on the intracellular signaling. MCF-7 and T-474 cells were treated with vehicle or 0.2, 2 or 20 μmol/L of Apatinib for 48 h. Then, the mRNA expressions of VEGFR-2, AMOT, YAP, LATS1/2 and Cyclin D1 were determined with qRT-PCR (A), and the protein levels of YAP, p-YAP, LATS1/2, Cyclin D1, ERK, p-ERK1/2 were determined with Western blotting (B). *P

    Article Snippet: After blocking with 5% skim milk powder, blots were incubated with primary antibodies against AMOT, YAP, p-YAP, LAST1, LAST2, Cyclin D1, ERK1/2, p-ERK1/2 and GAPDH (all from Abcam, Cambridge, US) overnight at 4°C.

    Techniques: Quantitative RT-PCR, Western Blot

    miR-338 up-regulates the phosphorylation of ERK1/2, P38 MAPK and Akt via NRP1. (A)The phosphorylation and total expression levels of ERK1/2, Akt and P38MAPK in AGS cells infected with LV-hsa-mir-338 or cont-miR. (B) An immunoblot analysis of NRP1 expression in AGS cells infected with LV-hsa-mir-338 or cont-miR, with or without NRP1 restoration. (C) The phosphorylation and total expression levels of ERK1/2, Akt and P38MAPK in AGS cells infected with LV-hsa-mir-338 or cont-miR, with or without NRP1 restoration. The expression levels of the phosphorylated proteins were normalized to those of the respective total proteins. The data represent the means±s.d.; *p

    Journal: PLoS ONE

    Article Title: MicroRNA-338 Inhibits Growth, Invasion and Metastasis of Gastric Cancer by Targeting NRP1 Expression

    doi: 10.1371/journal.pone.0094422

    Figure Lengend Snippet: miR-338 up-regulates the phosphorylation of ERK1/2, P38 MAPK and Akt via NRP1. (A)The phosphorylation and total expression levels of ERK1/2, Akt and P38MAPK in AGS cells infected with LV-hsa-mir-338 or cont-miR. (B) An immunoblot analysis of NRP1 expression in AGS cells infected with LV-hsa-mir-338 or cont-miR, with or without NRP1 restoration. (C) The phosphorylation and total expression levels of ERK1/2, Akt and P38MAPK in AGS cells infected with LV-hsa-mir-338 or cont-miR, with or without NRP1 restoration. The expression levels of the phosphorylated proteins were normalized to those of the respective total proteins. The data represent the means±s.d.; *p

    Article Snippet: Phospho-Erk1/2, phospho-Akt, and phospho-P38MAPK were purchased from Abcam (Cambridge, UK), and total Erk1/2, Akt, and P38MAPK were from BD Biosciences (USA).

    Techniques: Expressing, Infection

    Imatinib mesylate treatment blocks activation of the kinases Akt and Erk 1/2 in the heart

    Journal: Cancer

    Article Title: Rare Incidence of Congestive Heart Failure in Gastrointestinal Stromal Tumor and Other Sarcoma Patients Receiving Imatinib Mesylate (IM)

    doi: 10.1002/cncr.24683

    Figure Lengend Snippet: Imatinib mesylate treatment blocks activation of the kinases Akt and Erk 1/2 in the heart

    Article Snippet: Blots were probed with antibodies directed against phospho Akt (Ser473), phospho Erk 1/2 (Thr202/Tyr204), total Akt, total Erk 1/2 (Cell Signaling Technology).

    Techniques: Activation Assay

    Proposed molecular mechanisms for (a) the loss or (b) the preservation of liver weight by glycemic levels in the presence of insulin deficiency. In the liver of euglycemic rats with insulin deficiency, AMPK is activated and the activity of Akt, a major insulin signaling molecule, decreases (the decreased Akt activity is also influenced by PTEN activation), compared with those in hyperglycemic rats with insulin deficiency. The increased AMPK and decreased Akt activities, in turn, decrease the activity of mTOR. As a result, excessive autophagy is induced not only by the activated AMPK but also by the inhibition of protective role of mTOR against autophagy through ERK-1 activation and caspase-3 inhibition. Then excessive autophagy leads to hepatic cell death, partially via apoptosis mediated by caspase-3 activation, resulting in the loss of liver weight in euglycemic rats with insulin deficiency. On the other hand, in the liver of hyperglycemic rats with insulin deficiency, AMPK is not activated while Akt and mTOR are activated, compared with those in euglycemic rats with insulin deficiency. Thus, excessive autophagy and hepatic cell death are prevented not only because of the protective role of mTOR against autophagy but also because of the low AMPK activity, resulting in the preservation of liver weight in hyperglycemic rats with insulin deficiency.

    Journal: Journal of Diabetes Research

    Article Title: Euglycemia in Diabetic Rats Leads to Reduced Liver Weight via Increased Autophagy and Apoptosis through Increased AMPK and Caspase-3 and Decreased mTOR Activities

    doi: 10.1155/2015/497431

    Figure Lengend Snippet: Proposed molecular mechanisms for (a) the loss or (b) the preservation of liver weight by glycemic levels in the presence of insulin deficiency. In the liver of euglycemic rats with insulin deficiency, AMPK is activated and the activity of Akt, a major insulin signaling molecule, decreases (the decreased Akt activity is also influenced by PTEN activation), compared with those in hyperglycemic rats with insulin deficiency. The increased AMPK and decreased Akt activities, in turn, decrease the activity of mTOR. As a result, excessive autophagy is induced not only by the activated AMPK but also by the inhibition of protective role of mTOR against autophagy through ERK-1 activation and caspase-3 inhibition. Then excessive autophagy leads to hepatic cell death, partially via apoptosis mediated by caspase-3 activation, resulting in the loss of liver weight in euglycemic rats with insulin deficiency. On the other hand, in the liver of hyperglycemic rats with insulin deficiency, AMPK is not activated while Akt and mTOR are activated, compared with those in euglycemic rats with insulin deficiency. Thus, excessive autophagy and hepatic cell death are prevented not only because of the protective role of mTOR against autophagy but also because of the low AMPK activity, resulting in the preservation of liver weight in hyperglycemic rats with insulin deficiency.

    Article Snippet: Primary antibodies against total and phosphorylated AMPK (Cell Signaling Technology, CST, Denver, MA, USA; 1 : 5000), total and phosphorylated mTOR (CST; 1 : 1000), LC3B (CST; 1 : 1000), caspase-3 (CST; 1 : 1000), total and phosphorylated ERK-1 (CST; 1 : 5000), total and phosphorylated Akt (CST; 1 : 5000), and total and phosphorylated PTEN (CST; 1 : 1000) were applied overnight at 4°C.

    Techniques: Preserving, Activity Assay, Activation Assay, Inhibition

    Western blot analyses related to the regulation of cell growth/proliferation and apoptosis in liver tissue. (a) The ratio of pERK-1 to ERK-1. (b) The ratio of cleaved to mature caspase-3. The blots shown are representative of triplicates. Data are presented as means ± SD and were analyzed with one-way ANOVA followed by Tukey's post hoc test unless marked with an asterisk indicating that the unpaired t -test was used. 19S: sham-operated rats fed standard chow ad libitum (protein 19.4, carbohydrate 68.8, and lipid 11.8 kcal%); 19AL: pancreatectomized diabetic rats fed standard chow ad libitum ; 19R: pancreatectomized diabetic rats fed calorie-controlled standard chow to achieve euglycemia during the diet control period; 6R: pancreatectomized diabetic rats fed a calorie-controlled low protein diet (protein 6.0, carbohydrate 82.2, and lipid 11.8 kcal%) to achieve euglycemia during the diet control period.

    Journal: Journal of Diabetes Research

    Article Title: Euglycemia in Diabetic Rats Leads to Reduced Liver Weight via Increased Autophagy and Apoptosis through Increased AMPK and Caspase-3 and Decreased mTOR Activities

    doi: 10.1155/2015/497431

    Figure Lengend Snippet: Western blot analyses related to the regulation of cell growth/proliferation and apoptosis in liver tissue. (a) The ratio of pERK-1 to ERK-1. (b) The ratio of cleaved to mature caspase-3. The blots shown are representative of triplicates. Data are presented as means ± SD and were analyzed with one-way ANOVA followed by Tukey's post hoc test unless marked with an asterisk indicating that the unpaired t -test was used. 19S: sham-operated rats fed standard chow ad libitum (protein 19.4, carbohydrate 68.8, and lipid 11.8 kcal%); 19AL: pancreatectomized diabetic rats fed standard chow ad libitum ; 19R: pancreatectomized diabetic rats fed calorie-controlled standard chow to achieve euglycemia during the diet control period; 6R: pancreatectomized diabetic rats fed a calorie-controlled low protein diet (protein 6.0, carbohydrate 82.2, and lipid 11.8 kcal%) to achieve euglycemia during the diet control period.

    Article Snippet: Primary antibodies against total and phosphorylated AMPK (Cell Signaling Technology, CST, Denver, MA, USA; 1 : 5000), total and phosphorylated mTOR (CST; 1 : 1000), LC3B (CST; 1 : 1000), caspase-3 (CST; 1 : 1000), total and phosphorylated ERK-1 (CST; 1 : 5000), total and phosphorylated Akt (CST; 1 : 5000), and total and phosphorylated PTEN (CST; 1 : 1000) were applied overnight at 4°C.

    Techniques: Western Blot

    Effect of  LNT  on  STZ ‐induced  JNK  and p38  MAPK  activation in  INS ‐1 cells. ( A ) Following pre‐incubation with  LNT  for 30 min., the cells were treated with the indicated concentrations of  LNT  and  STZ  (0.5 mM) for 24 hrs. Phospho (P‐ JNK ) and total (T‐ JNK ) form of  JNK  were analysed by Western blot assay. ( B ) Quantitative analysis of phosphorylation of  JNK  was detected as in  A . ( C )  INS ‐1 cells were treated as in  A , and the phosphorylation of p38  MAPK  (P‐P38) was determined by Western blot analysis. ( D ) Quantitative analysis of P‐P38 was detected as in  C . ( E )  INS ‐1 cells were treated as in  A , and the phosphorylation of  ERK 1/2 ( PERK 1/2) was determined by Western blot analysis. ( F ) Quantitative analysis of phosphorylation of  ERK 1/2 was detected as in  E . The data are presented as the means ±S.E.M. for three independent experiments. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Lentinan protects pancreatic β cells from STZ‐induced damage

    doi: 10.1111/jcmm.12865

    Figure Lengend Snippet: Effect of LNT on STZ ‐induced JNK and p38 MAPK activation in INS ‐1 cells. ( A ) Following pre‐incubation with LNT for 30 min., the cells were treated with the indicated concentrations of LNT and STZ (0.5 mM) for 24 hrs. Phospho (P‐ JNK ) and total (T‐ JNK ) form of JNK were analysed by Western blot assay. ( B ) Quantitative analysis of phosphorylation of JNK was detected as in A . ( C ) INS ‐1 cells were treated as in A , and the phosphorylation of p38 MAPK (P‐P38) was determined by Western blot analysis. ( D ) Quantitative analysis of P‐P38 was detected as in C . ( E ) INS ‐1 cells were treated as in A , and the phosphorylation of ERK 1/2 ( PERK 1/2) was determined by Western blot analysis. ( F ) Quantitative analysis of phosphorylation of ERK 1/2 was detected as in E . The data are presented as the means ±S.E.M. for three independent experiments. * P

    Article Snippet: Membranes were blocked in PBST/5% non‐fat dry milk powder and incubated with antibodies against inducible nitric oxide synthase (iNOS), NF‐κB p65, Histone H3, GAPDH (Santa Cruz Biotechnology, Santa Cruz, CA, USA), phospho‐c‐Jun N‐terminal kinase (P‐JNK), total JNK (T‐JNK), phospho‐p38 Map out (P‐P38), total p38 (T‐P38), phosphorylated ERK 1/2 (P‐ERK1/2) and total ERK1/2 (T‐ERK1/2) (Abcam).

    Techniques: Activation Assay, Incubation, Western Blot

    Attenuation of cystitis-induced Akt and ERK1/2 phosphorylation in the urinary bladder by NGF antibody. In the control IgG-treated animals, cystitis increased the phosphorylation levels of Akt ( A and B ) and ERK1/2 ( C and D ) in the inflamed bladder. Administration

    Journal: The Journal of Biological Chemistry

    Article Title: Endogenous Nerve Growth Factor Regulates Collagen Expression and Bladder Hypertrophy through Akt and MAPK Pathways during Cystitis *

    doi: 10.1074/jbc.M109.040444

    Figure Lengend Snippet: Attenuation of cystitis-induced Akt and ERK1/2 phosphorylation in the urinary bladder by NGF antibody. In the control IgG-treated animals, cystitis increased the phosphorylation levels of Akt ( A and B ) and ERK1/2 ( C and D ) in the inflamed bladder. Administration

    Article Snippet: Antibodies against type I collagen, Akt/phospho-Akt, ERK1/2/phospho-ERK1/2, JNK/phospho-JNK, p38 MAPK/phospho-p38 MAPK, were from Cell Signaling Technology (Danvers, MA).

    Techniques:

    Expression level of the apoptotic-related proteins in MCF-7 cells treated with EADs at different time point as determined by Western blot analysis. (A) Expression of p21, p53, Bax, Bcl-2, PARP and caspase-8 in MCF-7 cells treated with 25 and 50 μg/mL of EADs (B) Fold change of Bax to Bcl-2 ratio at 24 and 48 hours. (C) Expression of AKT-1, phosphor-AKT, JNK-1, phosphor-JNK, ERK-1 and phosphor-ERK1 in MCF-7 cells treated with 25 and 50 μg/mL of EADs. The expression of proteins was normalized against beta actin and compared to the control. The data are represented as mean ± SD of at least three replicates from three independent tests. An asterisk a indicates statistically significantly different from the untreated control (P

    Journal: PLoS ONE

    Article Title: Induction of Apoptosis in MCF-7 Cells via Oxidative Stress Generation, Mitochondria-Dependent and Caspase-Independent Pathway by Ethyl Acetate Extract of Dillenia suffruticosa and Its Chemical Profile

    doi: 10.1371/journal.pone.0127441

    Figure Lengend Snippet: Expression level of the apoptotic-related proteins in MCF-7 cells treated with EADs at different time point as determined by Western blot analysis. (A) Expression of p21, p53, Bax, Bcl-2, PARP and caspase-8 in MCF-7 cells treated with 25 and 50 μg/mL of EADs (B) Fold change of Bax to Bcl-2 ratio at 24 and 48 hours. (C) Expression of AKT-1, phosphor-AKT, JNK-1, phosphor-JNK, ERK-1 and phosphor-ERK1 in MCF-7 cells treated with 25 and 50 μg/mL of EADs. The expression of proteins was normalized against beta actin and compared to the control. The data are represented as mean ± SD of at least three replicates from three independent tests. An asterisk a indicates statistically significantly different from the untreated control (P

    Article Snippet: Other antibodies such as polyclonal rabbit anti-p21 (ab7960), monoclonal mouse anti-Bax (ab5714), polyclonal rabbit anti-Bcl-2 (ab7973), polyclonal rabbit anti-caspase 8 (ab25901), monoclonal rabbit anti-AKT-1 (ab32505), polyclonal rabbit anti-JNK-1 (ab10664), polyclonal rabbit anti-p-JNK-1 (ab47337), monoclonal rabbit anti-ERK-1 (ab32537), polyclonal rabbit anti-p-ERK-1 (ab47310), polyclonal rabbit anti-PARP (ab137653) and monoclonal mouse anti-beta actin (ab8226) were obtained from ABCAM (Cambridge, MA, USA).

    Techniques: Expressing, Western Blot

    ErbB2 small interfering (si)RNA inhibits the expression of ErbB2, Akt, and ERK 1/2. A : cells were cultured after transfection with a specific ErbB2 siRNA or a control siRNA shortly after the time of plating. They were harvested at 48, 72, and 96 h after

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Cultured rat hepatocytes upregulate Akt and ERK in an ErbB-2-dependent manner

    doi: 10.1152/ajpgi.00597.2007

    Figure Lengend Snippet: ErbB2 small interfering (si)RNA inhibits the expression of ErbB2, Akt, and ERK 1/2. A : cells were cultured after transfection with a specific ErbB2 siRNA or a control siRNA shortly after the time of plating. They were harvested at 48, 72, and 96 h after

    Article Snippet: The phospho, total, and isoform-specific Akt (AKT Isoform Sampler kit) and ERK 1/2 antibodies were from Cell Signaling Technology (Beverly, MA).

    Techniques: Expressing, Cell Culture, Transfection

    Temporal expression of Akt and ERK 1/2 relative to markers of differentiation and proliferation. The expression of Akt and ERK 1/2 was compared with markers of hepatocyte differentiation (albumin and CYP 2E1) and proliferation (CDK-2 and cyclin D1). The

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Cultured rat hepatocytes upregulate Akt and ERK in an ErbB-2-dependent manner

    doi: 10.1152/ajpgi.00597.2007

    Figure Lengend Snippet: Temporal expression of Akt and ERK 1/2 relative to markers of differentiation and proliferation. The expression of Akt and ERK 1/2 was compared with markers of hepatocyte differentiation (albumin and CYP 2E1) and proliferation (CDK-2 and cyclin D1). The

    Article Snippet: The phospho, total, and isoform-specific Akt (AKT Isoform Sampler kit) and ERK 1/2 antibodies were from Cell Signaling Technology (Beverly, MA).

    Techniques: Expressing

    Temporal expression of Akt and ERK 1/2 proteins during rat hepatocyte culture. A : data shown were used to generate the graphs in B . Time 0 is 90 min after plating, when Williams’ medium E (WE) replaced the original plating medium. The effect of

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Cultured rat hepatocytes upregulate Akt and ERK in an ErbB-2-dependent manner

    doi: 10.1152/ajpgi.00597.2007

    Figure Lengend Snippet: Temporal expression of Akt and ERK 1/2 proteins during rat hepatocyte culture. A : data shown were used to generate the graphs in B . Time 0 is 90 min after plating, when Williams’ medium E (WE) replaced the original plating medium. The effect of

    Article Snippet: The phospho, total, and isoform-specific Akt (AKT Isoform Sampler kit) and ERK 1/2 antibodies were from Cell Signaling Technology (Beverly, MA).

    Techniques: Expressing

    Temporal expression of the active phosphorylated forms of Akt and ERK 1/2 proteins during rat hepatocyte culture. Time 0 is 90 min after plating, when Williams’ medium E replaced the original plating medium. The effect of insulin (100 nM) and

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Cultured rat hepatocytes upregulate Akt and ERK in an ErbB-2-dependent manner

    doi: 10.1152/ajpgi.00597.2007

    Figure Lengend Snippet: Temporal expression of the active phosphorylated forms of Akt and ERK 1/2 proteins during rat hepatocyte culture. Time 0 is 90 min after plating, when Williams’ medium E replaced the original plating medium. The effect of insulin (100 nM) and

    Article Snippet: The phospho, total, and isoform-specific Akt (AKT Isoform Sampler kit) and ERK 1/2 antibodies were from Cell Signaling Technology (Beverly, MA).

    Techniques: Expressing

    The time-dependent increase in Akt and ERK 1/2 correlates with increased acute EGF-dependent phosphorylation of Akt and ERK 1/2. We treated cells with either 10 −8 or 10 −6 M dexamethasone for 24 or 48 h. We then exposed them to EGF (50

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Cultured rat hepatocytes upregulate Akt and ERK in an ErbB-2-dependent manner

    doi: 10.1152/ajpgi.00597.2007

    Figure Lengend Snippet: The time-dependent increase in Akt and ERK 1/2 correlates with increased acute EGF-dependent phosphorylation of Akt and ERK 1/2. We treated cells with either 10 −8 or 10 −6 M dexamethasone for 24 or 48 h. We then exposed them to EGF (50

    Article Snippet: The phospho, total, and isoform-specific Akt (AKT Isoform Sampler kit) and ERK 1/2 antibodies were from Cell Signaling Technology (Beverly, MA).

    Techniques: