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  • 99
    Cell Signaling Technology Inc phospho erk1 2
    ( A . (b) Densitometry analysis determined from western blots. Phosphorylated <t>(p-ERK1/2)</t> relative to total (t-ERK1/2). Values represent mean ± SD ( n = 3). * represents significant difference compared to 0 h by student’s t test, p
    Phospho Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 9979 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phosphorylated erk1 2
    ( A . (b) Densitometry analysis determined from western blots. Phosphorylated <t>(p-ERK1/2)</t> relative to total (t-ERK1/2). Values represent mean ± SD ( n = 3). * represents significant difference compared to 0 h by student’s t test, p
    Phosphorylated Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2640 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phospho p44 42 mapk
    ( A . (b) Densitometry analysis determined from western blots. Phosphorylated <t>(p-ERK1/2)</t> relative to total (t-ERK1/2). Values represent mean ± SD ( n = 3). * represents significant difference compared to 0 h by student’s t test, p
    Phospho P44 42 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2563 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phospho erk1 2 thr202 tyr204
    ( A . (b) Densitometry analysis determined from western blots. Phosphorylated <t>(p-ERK1/2)</t> relative to total (t-ERK1/2). Values represent mean ± SD ( n = 3). * represents significant difference compared to 0 h by student’s t test, p
    Phospho Erk1 2 Thr202 Tyr204, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1648 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phospho erk 1 2
    BpV(pic) protect against OGD induced neuronal death through ERK 1/2 activation and PTEN lipid phosphatase activity inhibition.  a  and  b  Western blots analysis of p-AKT ( a ) and p-ERK 1/2 ( b ) levels in cultured primary neurons, bpV(pic) (200 nM) againsts the OGD-induced p-AKT and p-ERK 1/2 down-regulation. Quantification analysis of the levels are on the right (n = 6 independent cultures, *P 
    Phospho Erk 1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 835 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc phosphor erk1 2
    BpV(pic) protect against OGD induced neuronal death through ERK 1/2 activation and PTEN lipid phosphatase activity inhibition.  a  and  b  Western blots analysis of p-AKT ( a ) and p-ERK 1/2 ( b ) levels in cultured primary neurons, bpV(pic) (200 nM) againsts the OGD-induced p-AKT and p-ERK 1/2 down-regulation. Quantification analysis of the levels are on the right (n = 6 independent cultures, *P 
    Phosphor Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 3558 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology phosphorylated erk1 2
    Real-time PCR demonstrates that AGE-induced de novo α-SMA and loss of E-cadherin mRNA expression are regulated by RAGE through the <t>ERK1/2</t> MAP kinase pathway. Real-time PCR demonstrates that AGE-induced α-SMA ( a ) and reduced E-cadherin ( b ) mRNA expression by NRK52E cells at 24 hours are completely blocked by a neutralizing RAGE antibody (RAGE Ab) and a specific ERK1/2 MAP kinase inhibitor, PD 98059. CTL Ab, control antibody (rabbit IgG). Each bar represents the mean ± SD for three independent experiments. **, P
    Phosphorylated Erk1 2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 407 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    ( A . (b) Densitometry analysis determined from western blots. Phosphorylated (p-ERK1/2) relative to total (t-ERK1/2). Values represent mean ± SD ( n = 3). * represents significant difference compared to 0 h by student’s t test, p

    Journal: International Journal of Molecular Sciences

    Article Title: Chlorogenic Acid (CGA) Isomers Alleviate Interleukin 8 (IL-8) Production in Caco-2 Cells by Decreasing Phosphorylation of p38 and Increasing Cell Integrity

    doi: 10.3390/ijms19123873

    Figure Lengend Snippet: ( A . (b) Densitometry analysis determined from western blots. Phosphorylated (p-ERK1/2) relative to total (t-ERK1/2). Values represent mean ± SD ( n = 3). * represents significant difference compared to 0 h by student’s t test, p

    Article Snippet: Specifically, the membrane that was used for the detection of p-Erk1/2 was washed three times with TBST and incubated in a mixture antibody solution that contained both anti-phospho-Erk1/2 (phospho Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb (1:2000 dilution) (4370S, Cell Signaling Technology, Danvers, MA, USA) and anti-Erk1/2 (137F5) Rabbit mAb (1:1000 dilution) (4695S, Cell Signaling Technology, Danvers, MA, USA).

    Techniques: Western Blot

    The GluN2B CaMKII Binding Site Is Dispensable for Theta Burst LTP (A–C) Activity-dependent signaling to ERK1/2 does not require GluN2B CTD-specific sequences. DIV9 cortical neurons of the indicated genotypes were treated with TTX (500 nM), KN-62 (10 μM), or MK-801 (10 μM) for 1 hr, after which protein extracts were made and subjected to western blot analysis for phospho-ERK1/2 levels, normalized to total ERK1/2. (A) shows quantitation and (B) and (C) show example blots. ∗ p

    Journal: Cell Reports

    Article Title: The Developmental Shift of NMDA Receptor Composition Proceeds Independently of GluN2 Subunit-Specific GluN2 C-Terminal Sequences

    doi: 10.1016/j.celrep.2018.09.089

    Figure Lengend Snippet: The GluN2B CaMKII Binding Site Is Dispensable for Theta Burst LTP (A–C) Activity-dependent signaling to ERK1/2 does not require GluN2B CTD-specific sequences. DIV9 cortical neurons of the indicated genotypes were treated with TTX (500 nM), KN-62 (10 μM), or MK-801 (10 μM) for 1 hr, after which protein extracts were made and subjected to western blot analysis for phospho-ERK1/2 levels, normalized to total ERK1/2. (A) shows quantitation and (B) and (C) show example blots. ∗ p

    Article Snippet: The membranes were incubated at 4°C overnight with the primary antibodies diluted in blocking solution: anti phospho-(Ser-1303) GluN2B (1: 2000, Millipore), anti-phospho (Tyr-1472) GluN2B (1:2000, Millipore), anti-phospho (Ser1480) GluN2B (1:2000, Abcam), anti-GluN2B (C terminus, 1:4000, BD Transduction Laboratories), anti-GluN2B (N terminus 1:2000, Thermo Fisher Scientific), anti-GluN2A (N terminus, 1:1000, Thermo Fisher Scientific), anti-CamKiiα (1:8000, Thermo Fisher Scientific), anti-ERK1/2 (1:2000, Cell Signaling), anti-phospho ERK1/2 (1:2000, Cell Signaling) and anti-beta actin (1:200000, Abcam).

    Techniques: Binding Assay, Activity Assay, Western Blot, Quantitation Assay

    Genotypic comparisons of ERK1/2 and CREB expressions in the amygdala of naïve WT and nNOS KO mice (n=9–14/group). No differences in ERK1/2 phosphorylation or expression were observed, however pCREB was significantly elevated in nNOS KO mice compared to WT mice. (A) Representative immunoblots for ERK1/2 experiments. (B) No genotypic differences were observed for pERK1/2. (C) No genotypic differences were observed for ERK1/2 expression. (D) Representative immunoblots for CREB experiments. (E) pCREB levels were 2-fold higher in nNOS KO mice than in WT mice (* P =0.005). (F) No genotypic differences were observed for total CREB expression.

    Journal: Neuroscience

    Article Title: Long-term memory of visually cued fear conditioning: roles of the nNOS gene and CREB

    doi: 10.1016/j.neuroscience.2010.11.005

    Figure Lengend Snippet: Genotypic comparisons of ERK1/2 and CREB expressions in the amygdala of naïve WT and nNOS KO mice (n=9–14/group). No differences in ERK1/2 phosphorylation or expression were observed, however pCREB was significantly elevated in nNOS KO mice compared to WT mice. (A) Representative immunoblots for ERK1/2 experiments. (B) No genotypic differences were observed for pERK1/2. (C) No genotypic differences were observed for ERK1/2 expression. (D) Representative immunoblots for CREB experiments. (E) pCREB levels were 2-fold higher in nNOS KO mice than in WT mice (* P =0.005). (F) No genotypic differences were observed for total CREB expression.

    Article Snippet: Next, membranes were incubated with anti-phosphorylated CREB (Ser133) (1:1000) at 4°C for 72 h or anti-phosphorylated ERK1/2 (1:2000) at RT for 1 h (both Cell Signaling, Beverly, MA) diluted in TBS-T + 5% BSA.

    Techniques: Mouse Assay, Expressing, Western Blot

    BpV(pic) protect against OGD induced neuronal death through ERK 1/2 activation and PTEN lipid phosphatase activity inhibition.  a  and  b  Western blots analysis of p-AKT ( a ) and p-ERK 1/2 ( b ) levels in cultured primary neurons, bpV(pic) (200 nM) againsts the OGD-induced p-AKT and p-ERK 1/2 down-regulation. Quantification analysis of the levels are on the right (n = 6 independent cultures, *P 

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: BpV(pic) protect against OGD induced neuronal death through ERK 1/2 activation and PTEN lipid phosphatase activity inhibition. a and b Western blots analysis of p-AKT ( a ) and p-ERK 1/2 ( b ) levels in cultured primary neurons, bpV(pic) (200 nM) againsts the OGD-induced p-AKT and p-ERK 1/2 down-regulation. Quantification analysis of the levels are on the right (n = 6 independent cultures, *P 

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Activation Assay, Activity Assay, Inhibition, Western Blot, Cell Culture

    The mechanism of bpV(pic)-mediateded neuroprotect in ischaemia–reperfusion cerebral injury. After ischaemia–reperfusion, the phospho-AKT (Ser 473 ) and phospho-ERK 1/2 (Thr 202 /Tyr 204 ) were down-regulated, inducing the increase of neuronal death and cerebral injury (left). When treated with bpV(pic), we found that bpV(pic) can not only enhance the level of p-AKT and p-ERK 1/2 through inhibiting PTEN lipid phosphatase activity, but also in a PTEN independent pathway to up regulation of ERK 1/2 activity, leading to neuronal survival and animal functional recovery

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: The mechanism of bpV(pic)-mediateded neuroprotect in ischaemia–reperfusion cerebral injury. After ischaemia–reperfusion, the phospho-AKT (Ser 473 ) and phospho-ERK 1/2 (Thr 202 /Tyr 204 ) were down-regulated, inducing the increase of neuronal death and cerebral injury (left). When treated with bpV(pic), we found that bpV(pic) can not only enhance the level of p-AKT and p-ERK 1/2 through inhibiting PTEN lipid phosphatase activity, but also in a PTEN independent pathway to up regulation of ERK 1/2 activity, leading to neuronal survival and animal functional recovery

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Activity Assay, Functional Assay

    BpV(pic) through PTEN inhibition and ERK 1/2 activation reduces the infarct volume in ischemic stroke animals.  a  Sample images of TTC staining brain sections show that bpV(pic) decreases the infarct volume in brain 24 h after ischemia onset was prevented by IV and U0126.  b  Quantification analysis of the infarct volume [n = 6, *P 

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: BpV(pic) through PTEN inhibition and ERK 1/2 activation reduces the infarct volume in ischemic stroke animals. a Sample images of TTC staining brain sections show that bpV(pic) decreases the infarct volume in brain 24 h after ischemia onset was prevented by IV and U0126. b Quantification analysis of the infarct volume [n = 6, *P 

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Inhibition, Activation Assay, Staining

    BpV(pic) induces the functional recovery in ischemic stroke animals through PTEN inhibition and ERK 1/2 activation.  a  Animals treated with bpV(pic) have lower scores in mNSS test at day 7 and 14 after ischemia–reperfusion injury compared with I/R + Vehicle group. Animals injected with IV and/or U0126 before injected with bpV(pic) show a higher scores in mNSS test at day 7 and 14 after ischemia–reperfusion than I/R + bpV(pic) group [n = 6 for each group, *P 

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: BpV(pic) induces the functional recovery in ischemic stroke animals through PTEN inhibition and ERK 1/2 activation. a Animals treated with bpV(pic) have lower scores in mNSS test at day 7 and 14 after ischemia–reperfusion injury compared with I/R + Vehicle group. Animals injected with IV and/or U0126 before injected with bpV(pic) show a higher scores in mNSS test at day 7 and 14 after ischemia–reperfusion than I/R + bpV(pic) group [n = 6 for each group, *P 

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Functional Assay, Inhibition, Activation Assay, Injection

    After ischemic stroke p-AKT and P-ERK 1/2 levels are decreased.  a  and  b  Double-immunofluorescence staining of p-AKT or p-ERK 1/2 with NeuN in the peri-infarct area of cortex 24 h or 72 h after I/R compared with the ipsilateral sham, NeuN performes green, P-AKT and p-ERK 1/2 is shown in red and hochest is shown in blue. Scale bar, 20 µm.  c  and  d  Western blots showing a decreasing expression in p-AKT ( c ) and p-ERK 1/2 ( d ) at the indicated time points after I/R at rats (left). Right: quantification analysis of normalized p-AKT and p-ERK 1/2 levels (n = 6 per time points, *P 

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: After ischemic stroke p-AKT and P-ERK 1/2 levels are decreased. a and b Double-immunofluorescence staining of p-AKT or p-ERK 1/2 with NeuN in the peri-infarct area of cortex 24 h or 72 h after I/R compared with the ipsilateral sham, NeuN performes green, P-AKT and p-ERK 1/2 is shown in red and hochest is shown in blue. Scale bar, 20 µm. c and d Western blots showing a decreasing expression in p-AKT ( c ) and p-ERK 1/2 ( d ) at the indicated time points after I/R at rats (left). Right: quantification analysis of normalized p-AKT and p-ERK 1/2 levels (n = 6 per time points, *P 

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Double Immunofluorescence Staining, Western Blot, Expressing

    BpV(pic) up-regulated the p-AKT and p-ERK 1/2 level in rats and protects against ischemia–reperfusion injury.  a  A time points diagram shows rat ischemia–reperfusion injury and IV (AKT inhibitor), U0126 (ERK 1/2 inhibitor), bpV(pic) treatment procedure.  b  and  c  Western blots showing an increased expression in p-AKT ( b ) and p-ERK 1/2 ( c ) after i.c.v inject bpV(pic) (100 µM, 5 µL) 24 h after ischemia–reperfusion injury comparing with I/R + vehicle group (left). Right: quantification analysis of p-AKT and p-ERK 1/2 levels (n = 6, *P 

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: BpV(pic) up-regulated the p-AKT and p-ERK 1/2 level in rats and protects against ischemia–reperfusion injury. a A time points diagram shows rat ischemia–reperfusion injury and IV (AKT inhibitor), U0126 (ERK 1/2 inhibitor), bpV(pic) treatment procedure. b and c Western blots showing an increased expression in p-AKT ( b ) and p-ERK 1/2 ( c ) after i.c.v inject bpV(pic) (100 µM, 5 µL) 24 h after ischemia–reperfusion injury comparing with I/R + vehicle group (left). Right: quantification analysis of p-AKT and p-ERK 1/2 levels (n = 6, *P 

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Western Blot, Expressing

    BpV(pic) not only through inhibit PTEN lipid phosphatase activity but also independently of PTEN to up-regulation p-ERK 1/2 level.  a  Western blots analysis of p-ERK 1/2 levels in SH-SY5Y cells treated with bpV(pic) (10–500 nM) on right. Left: quantification analysis of p-ERK 1/2 levels treated with bpV(pic) shows an increased expression of normalized p-ERK 1/2 compare with vehicle group (n = 6 independent cultures, *P 

    Journal: Neurochemical Research

    Article Title: ERK 1/2 Activation Mediates the Neuroprotective Effect of BpV(pic) in Focal Cerebral Ischemia–Reperfusion Injury

    doi: 10.1007/s11064-018-2558-z

    Figure Lengend Snippet: BpV(pic) not only through inhibit PTEN lipid phosphatase activity but also independently of PTEN to up-regulation p-ERK 1/2 level. a Western blots analysis of p-ERK 1/2 levels in SH-SY5Y cells treated with bpV(pic) (10–500 nM) on right. Left: quantification analysis of p-ERK 1/2 levels treated with bpV(pic) shows an increased expression of normalized p-ERK 1/2 compare with vehicle group (n = 6 independent cultures, *P 

    Article Snippet: The brain sections were treated with primary antibody rabbit anti- phospho-AKT (Ser473 ) (1:250), phospho-ERK 1/2 (Thr202 /Tyr204 ) (1:250) from Cell Signaling Technology, mouse anti- NeuN (neuronal-specific nuclear protein) from Chemicon.

    Techniques: Activity Assay, Western Blot, Expressing

    Real-time PCR demonstrates that AGE-induced de novo α-SMA and loss of E-cadherin mRNA expression are regulated by RAGE through the ERK1/2 MAP kinase pathway. Real-time PCR demonstrates that AGE-induced α-SMA ( a ) and reduced E-cadherin ( b ) mRNA expression by NRK52E cells at 24 hours are completely blocked by a neutralizing RAGE antibody (RAGE Ab) and a specific ERK1/2 MAP kinase inhibitor, PD 98059. CTL Ab, control antibody (rabbit IgG). Each bar represents the mean ± SD for three independent experiments. **, P

    Journal: The American Journal of Pathology

    Article Title: Advanced Glycation End Products Induce Tubular Epithelial-Myofibroblast Transition through the RAGE-ERK1/2 MAP Kinase Signaling Pathway

    doi:

    Figure Lengend Snippet: Real-time PCR demonstrates that AGE-induced de novo α-SMA and loss of E-cadherin mRNA expression are regulated by RAGE through the ERK1/2 MAP kinase pathway. Real-time PCR demonstrates that AGE-induced α-SMA ( a ) and reduced E-cadherin ( b ) mRNA expression by NRK52E cells at 24 hours are completely blocked by a neutralizing RAGE antibody (RAGE Ab) and a specific ERK1/2 MAP kinase inhibitor, PD 98059. CTL Ab, control antibody (rabbit IgG). Each bar represents the mean ± SD for three independent experiments. **, P

    Article Snippet: To detect phosphorylated ERK1/2, total ERK1/2, α-SMA, and E-cadherin, the membrane was incubated for 1 hour with mouse monoclonal (mAb) to phosphorylated ERK1/2, rabbit polyclonal antibodies (Ab) to ERK1/2 (Santa Cruz Biotechnology Inc., Santa Cruz, CA), and mAbs to α-SMA (1A4, Sigma) and E-cadherin (Transduction Laboratories, Lexington, KY).

    Techniques: Real-time Polymerase Chain Reaction, Expressing, CTL Assay

    Western blot analysis demonstrates that AGE-induced loss of E-cadherin protein expression is TGF-β-independent and RAGE-ERK-dependent. Results show that AGE-induced loss of E-cadherin expression by NRK52E cells at 24 hours is not inhibited by a neutralizing TGF-β antibody (A), but is prevented by addition of sRAGE and an ERK1/2 inhibitor, PD98059. The specificity of a neutralizing anti-TGF-β antibody to block TGF-β-induced loss of E-cadherin is demonstrated in the last two lanes . CTL Ab, control rabbit antibody (IgG). Each bar represents the mean ± SD for four independent experiments. *, P

    Journal: The American Journal of Pathology

    Article Title: Advanced Glycation End Products Induce Tubular Epithelial-Myofibroblast Transition through the RAGE-ERK1/2 MAP Kinase Signaling Pathway

    doi:

    Figure Lengend Snippet: Western blot analysis demonstrates that AGE-induced loss of E-cadherin protein expression is TGF-β-independent and RAGE-ERK-dependent. Results show that AGE-induced loss of E-cadherin expression by NRK52E cells at 24 hours is not inhibited by a neutralizing TGF-β antibody (A), but is prevented by addition of sRAGE and an ERK1/2 inhibitor, PD98059. The specificity of a neutralizing anti-TGF-β antibody to block TGF-β-induced loss of E-cadherin is demonstrated in the last two lanes . CTL Ab, control rabbit antibody (IgG). Each bar represents the mean ± SD for four independent experiments. *, P

    Article Snippet: To detect phosphorylated ERK1/2, total ERK1/2, α-SMA, and E-cadherin, the membrane was incubated for 1 hour with mouse monoclonal (mAb) to phosphorylated ERK1/2, rabbit polyclonal antibodies (Ab) to ERK1/2 (Santa Cruz Biotechnology Inc., Santa Cruz, CA), and mAbs to α-SMA (1A4, Sigma) and E-cadherin (Transduction Laboratories, Lexington, KY).

    Techniques: Western Blot, Expressing, Blocking Assay, CTL Assay

    Double immunocytochemistry demonstrates that AGEs induce TEMT as determined by de novo expression of α-SMA and a partial loss of E-cadherin in NRK52E cells. NRK52E cells were stimulated with control BSA (30 μg/ml, A ) or AGE-BSA (30 μg/ml, B–F ) for 24 hours in the presence of an isotype control normal rabbit IgG (10 μg/ml, C ), a neutralizing TGF-β antibody (10 μg/ml, D ), a neutralizing RAGE antibody (10 μg/ml, E ), or a specific ERK1/2 MAP kinase inhibitor (PD 98059, 10 μmol/L, F ). Cells were stained with mAbs to α-SMA (myofibroblasts, red) and E-cadherin (epithelial cells, blue). The percentage of transformed cells (α-SMA+) is shown in ( G ). Results show that AGE-induced α-SMA expression in TECs is blocked by a neutralizing RAGE and an ERK1/2 MAP kinase inhibitor, but not by a neutralizing TGF-β antibody. Tab, anti-TGF-β antibody; Cab, control antibody; Rab, anti-RAGE antibody; PD, PD 98059. Data represent the mean ± SD for five experiments. Nuclei are stained with hematoxylin. Magnification, ×250. ***, P

    Journal: The American Journal of Pathology

    Article Title: Advanced Glycation End Products Induce Tubular Epithelial-Myofibroblast Transition through the RAGE-ERK1/2 MAP Kinase Signaling Pathway

    doi:

    Figure Lengend Snippet: Double immunocytochemistry demonstrates that AGEs induce TEMT as determined by de novo expression of α-SMA and a partial loss of E-cadherin in NRK52E cells. NRK52E cells were stimulated with control BSA (30 μg/ml, A ) or AGE-BSA (30 μg/ml, B–F ) for 24 hours in the presence of an isotype control normal rabbit IgG (10 μg/ml, C ), a neutralizing TGF-β antibody (10 μg/ml, D ), a neutralizing RAGE antibody (10 μg/ml, E ), or a specific ERK1/2 MAP kinase inhibitor (PD 98059, 10 μmol/L, F ). Cells were stained with mAbs to α-SMA (myofibroblasts, red) and E-cadherin (epithelial cells, blue). The percentage of transformed cells (α-SMA+) is shown in ( G ). Results show that AGE-induced α-SMA expression in TECs is blocked by a neutralizing RAGE and an ERK1/2 MAP kinase inhibitor, but not by a neutralizing TGF-β antibody. Tab, anti-TGF-β antibody; Cab, control antibody; Rab, anti-RAGE antibody; PD, PD 98059. Data represent the mean ± SD for five experiments. Nuclei are stained with hematoxylin. Magnification, ×250. ***, P

    Article Snippet: To detect phosphorylated ERK1/2, total ERK1/2, α-SMA, and E-cadherin, the membrane was incubated for 1 hour with mouse monoclonal (mAb) to phosphorylated ERK1/2, rabbit polyclonal antibodies (Ab) to ERK1/2 (Santa Cruz Biotechnology Inc., Santa Cruz, CA), and mAbs to α-SMA (1A4, Sigma) and E-cadherin (Transduction Laboratories, Lexington, KY).

    Techniques: Immunocytochemistry, Expressing, Staining, Transformation Assay

    Western blot analysis demonstrates that AGE-induced α-SMA protein expression is TGF-β-independent, but RAGE-ERK-dependent. Results show that AGE-induced α-SMA expression by NRK52E cells at 24 hours is not inhibited by a neutralizing TGF-β antibody, but is completely blocked by sRAGE and an ERK1/2 inhibitor, PD98059. The specificity of a neutralizing anti-TGF-β antibody to block TGF-β-induced α-SMA expression is shown in the last two lanes . CTL Ab, control rabbit antibody (IgG). Each bar represents the mean ± SD for three independent experiments. *, P

    Journal: The American Journal of Pathology

    Article Title: Advanced Glycation End Products Induce Tubular Epithelial-Myofibroblast Transition through the RAGE-ERK1/2 MAP Kinase Signaling Pathway

    doi:

    Figure Lengend Snippet: Western blot analysis demonstrates that AGE-induced α-SMA protein expression is TGF-β-independent, but RAGE-ERK-dependent. Results show that AGE-induced α-SMA expression by NRK52E cells at 24 hours is not inhibited by a neutralizing TGF-β antibody, but is completely blocked by sRAGE and an ERK1/2 inhibitor, PD98059. The specificity of a neutralizing anti-TGF-β antibody to block TGF-β-induced α-SMA expression is shown in the last two lanes . CTL Ab, control rabbit antibody (IgG). Each bar represents the mean ± SD for three independent experiments. *, P

    Article Snippet: To detect phosphorylated ERK1/2, total ERK1/2, α-SMA, and E-cadherin, the membrane was incubated for 1 hour with mouse monoclonal (mAb) to phosphorylated ERK1/2, rabbit polyclonal antibodies (Ab) to ERK1/2 (Santa Cruz Biotechnology Inc., Santa Cruz, CA), and mAbs to α-SMA (1A4, Sigma) and E-cadherin (Transduction Laboratories, Lexington, KY).

    Techniques: Western Blot, Expressing, Blocking Assay, CTL Assay

    Western blot analysis demonstrates that AGEs signal through RAGE to activate the ERK1/2 signaling pathway. a: A representative Western blot shows that AGE-BSA (30 μg/ml) induces ERK1/2 phosphorylation in NRK52E in a time-dependent manner, being significant at 15 minutes. b: AGEs, but not BSA, induce ERK1/2 phosphorylation (at 30 minutes) in a dose-dependent manner and this is blocked by both sRAGE and a specific ERK1/2 inhibitor, PD 98059. Each sample represents the results from three independent experiments.

    Journal: The American Journal of Pathology

    Article Title: Advanced Glycation End Products Induce Tubular Epithelial-Myofibroblast Transition through the RAGE-ERK1/2 MAP Kinase Signaling Pathway

    doi:

    Figure Lengend Snippet: Western blot analysis demonstrates that AGEs signal through RAGE to activate the ERK1/2 signaling pathway. a: A representative Western blot shows that AGE-BSA (30 μg/ml) induces ERK1/2 phosphorylation in NRK52E in a time-dependent manner, being significant at 15 minutes. b: AGEs, but not BSA, induce ERK1/2 phosphorylation (at 30 minutes) in a dose-dependent manner and this is blocked by both sRAGE and a specific ERK1/2 inhibitor, PD 98059. Each sample represents the results from three independent experiments.

    Article Snippet: To detect phosphorylated ERK1/2, total ERK1/2, α-SMA, and E-cadherin, the membrane was incubated for 1 hour with mouse monoclonal (mAb) to phosphorylated ERK1/2, rabbit polyclonal antibodies (Ab) to ERK1/2 (Santa Cruz Biotechnology Inc., Santa Cruz, CA), and mAbs to α-SMA (1A4, Sigma) and E-cadherin (Transduction Laboratories, Lexington, KY).

    Techniques: Western Blot

    Western blot analysis shows that AGE-induced p-ERK1/2, α-SMA expression, and loss of E-cadherin are regulated by the ERK1/2 MAP kinase pathway. Results show that AGE-induced p-ERK1/2, up-regulation of α-SMA and decrease in E-cadherin expression by NRK52E cells at 24 hours are completely blocked by overexpression of DN-MEK1. However, cells with overexpression of WT-MEK1 show no significant increase in p-ERK1/2 and α-SMA or decrease in E-cadherin expression when compared to empty control vector. Each sample represents the results from at least three independent experiments.

    Journal: The American Journal of Pathology

    Article Title: Advanced Glycation End Products Induce Tubular Epithelial-Myofibroblast Transition through the RAGE-ERK1/2 MAP Kinase Signaling Pathway

    doi:

    Figure Lengend Snippet: Western blot analysis shows that AGE-induced p-ERK1/2, α-SMA expression, and loss of E-cadherin are regulated by the ERK1/2 MAP kinase pathway. Results show that AGE-induced p-ERK1/2, up-regulation of α-SMA and decrease in E-cadherin expression by NRK52E cells at 24 hours are completely blocked by overexpression of DN-MEK1. However, cells with overexpression of WT-MEK1 show no significant increase in p-ERK1/2 and α-SMA or decrease in E-cadherin expression when compared to empty control vector. Each sample represents the results from at least three independent experiments.

    Article Snippet: To detect phosphorylated ERK1/2, total ERK1/2, α-SMA, and E-cadherin, the membrane was incubated for 1 hour with mouse monoclonal (mAb) to phosphorylated ERK1/2, rabbit polyclonal antibodies (Ab) to ERK1/2 (Santa Cruz Biotechnology Inc., Santa Cruz, CA), and mAbs to α-SMA (1A4, Sigma) and E-cadherin (Transduction Laboratories, Lexington, KY).

    Techniques: Western Blot, Expressing, Over Expression, Plasmid Preparation

    LPS induced phosphorylation of ERK1/2 in both cytoplasm and nucleus . RAW264.7 cells were stimulated with 0.1 μg/ml of bacterial LPS for 0, 15, 30, 60 and 120 minutes and probed for phospho-ERK1/2 as before. (A) Phosphorylation of ERK1/2 in cytoplasm upon stimulation with LPS(0.1 μg/ml). (C) phosphorylation of ERK1/2 in nucleus. The data is a representative of three independent experiments. (B) and (D) Total ERK1/2 in cytoplasm and nucleus normalized for protein content. Costimulation of RAW264.7 cells with LPS (0.1 μg/ml) and 5 μg/ml of ESAT-6 for 0, 15, 30, 60 and 120 minutes. (E) ERK1/2 phosphorylation in cytoplasm upon stimulation with 5 μg/ml of ESAT-6 and 0.1 μg/ml of LPS. (G) Phosphorylation of ERK1/2 in the nucleus with both LPS and ESAT-6. (F) and (H) Total ERK1/2 protein in cytoplasm and nucleus respectively.

    Journal: BMC Immunology

    Article Title: Mycobacterium tuberculosis 6-kDa Early Secreted Antigenic Target (ESAT-6) protein downregulates Lipopolysaccharide induced c-myc expression by modulating the Extracellular Signal Regulated Kinases 1/2

    doi: 10.1186/1471-2172-8-24

    Figure Lengend Snippet: LPS induced phosphorylation of ERK1/2 in both cytoplasm and nucleus . RAW264.7 cells were stimulated with 0.1 μg/ml of bacterial LPS for 0, 15, 30, 60 and 120 minutes and probed for phospho-ERK1/2 as before. (A) Phosphorylation of ERK1/2 in cytoplasm upon stimulation with LPS(0.1 μg/ml). (C) phosphorylation of ERK1/2 in nucleus. The data is a representative of three independent experiments. (B) and (D) Total ERK1/2 in cytoplasm and nucleus normalized for protein content. Costimulation of RAW264.7 cells with LPS (0.1 μg/ml) and 5 μg/ml of ESAT-6 for 0, 15, 30, 60 and 120 minutes. (E) ERK1/2 phosphorylation in cytoplasm upon stimulation with 5 μg/ml of ESAT-6 and 0.1 μg/ml of LPS. (G) Phosphorylation of ERK1/2 in the nucleus with both LPS and ESAT-6. (F) and (H) Total ERK1/2 protein in cytoplasm and nucleus respectively.

    Article Snippet: Antibodies against ERK-1 and phospho-ERK1/2 were obtained from Santa Cruz Biotech, CA, USA.

    Techniques:

    Stimulation with ESAT-6 in presence of sodium orthovanadate caused appearance of phospho-ERK1/2 in the nucleus . Stimulation of RAW264.7 cells with 5 μg/ml of ESAT-6 and 1 mM Na 3 VO 4 for 0, 15, 30, 60 and 120 minutes. (A) Phosphorylation of ERK1/2 in cytoplasm. (C) ERK1/2 phosphorylation in the nucleus. (B) and (D) Total ERK1/2 in cytoplasm and nucleus respectively. (E) and (G) Phosphorylation of ERK1/2 in cytoplasm and the nucleus respectively upon treatment with 1 mM Na 3 VO 4 for 0, 15, 30, 60 and 120 minutes. (F) and (H) Total ERK1/2 in cytoplasm and nucleus respectively to show equal loading of proteins in all the lanes. The data is representative of three independent experiments.

    Journal: BMC Immunology

    Article Title: Mycobacterium tuberculosis 6-kDa Early Secreted Antigenic Target (ESAT-6) protein downregulates Lipopolysaccharide induced c-myc expression by modulating the Extracellular Signal Regulated Kinases 1/2

    doi: 10.1186/1471-2172-8-24

    Figure Lengend Snippet: Stimulation with ESAT-6 in presence of sodium orthovanadate caused appearance of phospho-ERK1/2 in the nucleus . Stimulation of RAW264.7 cells with 5 μg/ml of ESAT-6 and 1 mM Na 3 VO 4 for 0, 15, 30, 60 and 120 minutes. (A) Phosphorylation of ERK1/2 in cytoplasm. (C) ERK1/2 phosphorylation in the nucleus. (B) and (D) Total ERK1/2 in cytoplasm and nucleus respectively. (E) and (G) Phosphorylation of ERK1/2 in cytoplasm and the nucleus respectively upon treatment with 1 mM Na 3 VO 4 for 0, 15, 30, 60 and 120 minutes. (F) and (H) Total ERK1/2 in cytoplasm and nucleus respectively to show equal loading of proteins in all the lanes. The data is representative of three independent experiments.

    Article Snippet: Antibodies against ERK-1 and phospho-ERK1/2 were obtained from Santa Cruz Biotech, CA, USA.

    Techniques:

    ESAT-6 stimulated increase in the phosphatase activity associated with ERK1/2 in the nucleus . (A) RAW264.7 cells were stimulated for different time points of 0, 15, 30, 60 and 120 minutes, the ERK-1 was immunoprecipitated from the nuclear extract and the phosphatase activity was determined, the last column where cells were stimulated with ESAT-6 for 120 minutes but no ERK-1 antibody was added (antibody control). (B) After phosphatase assay was done, the immunoprecipitate was mixed with 2× sample buffer and run on 10% SDS-PAGE and after western blotting the membrane was probed with ERK-1 antibody to confirm equal pull down of ERK1/2 in all the samples. The graph shows the mean +/- S.D. of three independent experiments.

    Journal: BMC Immunology

    Article Title: Mycobacterium tuberculosis 6-kDa Early Secreted Antigenic Target (ESAT-6) protein downregulates Lipopolysaccharide induced c-myc expression by modulating the Extracellular Signal Regulated Kinases 1/2

    doi: 10.1186/1471-2172-8-24

    Figure Lengend Snippet: ESAT-6 stimulated increase in the phosphatase activity associated with ERK1/2 in the nucleus . (A) RAW264.7 cells were stimulated for different time points of 0, 15, 30, 60 and 120 minutes, the ERK-1 was immunoprecipitated from the nuclear extract and the phosphatase activity was determined, the last column where cells were stimulated with ESAT-6 for 120 minutes but no ERK-1 antibody was added (antibody control). (B) After phosphatase assay was done, the immunoprecipitate was mixed with 2× sample buffer and run on 10% SDS-PAGE and after western blotting the membrane was probed with ERK-1 antibody to confirm equal pull down of ERK1/2 in all the samples. The graph shows the mean +/- S.D. of three independent experiments.

    Article Snippet: Antibodies against ERK-1 and phospho-ERK1/2 were obtained from Santa Cruz Biotech, CA, USA.

    Techniques: Activity Assay, Immunoprecipitation, Phosphatase Assay, SDS Page, Western Blot

    ESAT-6 induced phosphorylation of ERK1/2 in cytoplasm but not in nucleus . 10 × 10 6 RAW264.7 cells were stimulated with 5 μg/ml of recombinant ESAT-6 for 0, 15, 30, 60 and 120 minutes; cytoplasmic and nuclear extracts were run on gel and probed with anti-phospho-ERK1/2 antibody. (A) phosphorylation of ERK1/2 in cytoplasm. (C) phosphorylation of ERK1/2 in nucleus. (B) and (D) Total ERK1/2 in the cytoplasmic and nuclear extracts respectively at different time points to confirm equal loading of samples in all the lanes. (E) and (G) represents phosphorylated p38 in cytoplasm and the nucleus respectively. (F) and (H) shows the total p38 protein in cytoplasm and nucleus respectively. Data is a representative from three experiments.

    Journal: BMC Immunology

    Article Title: Mycobacterium tuberculosis 6-kDa Early Secreted Antigenic Target (ESAT-6) protein downregulates Lipopolysaccharide induced c-myc expression by modulating the Extracellular Signal Regulated Kinases 1/2

    doi: 10.1186/1471-2172-8-24

    Figure Lengend Snippet: ESAT-6 induced phosphorylation of ERK1/2 in cytoplasm but not in nucleus . 10 × 10 6 RAW264.7 cells were stimulated with 5 μg/ml of recombinant ESAT-6 for 0, 15, 30, 60 and 120 minutes; cytoplasmic and nuclear extracts were run on gel and probed with anti-phospho-ERK1/2 antibody. (A) phosphorylation of ERK1/2 in cytoplasm. (C) phosphorylation of ERK1/2 in nucleus. (B) and (D) Total ERK1/2 in the cytoplasmic and nuclear extracts respectively at different time points to confirm equal loading of samples in all the lanes. (E) and (G) represents phosphorylated p38 in cytoplasm and the nucleus respectively. (F) and (H) shows the total p38 protein in cytoplasm and nucleus respectively. Data is a representative from three experiments.

    Article Snippet: Antibodies against ERK-1 and phospho-ERK1/2 were obtained from Santa Cruz Biotech, CA, USA.

    Techniques: Recombinant

    NF-kB inhibition prolongs EGF-induced ERK1/2 activation through downregulation of DUSP1 expression. HCEC were serum starved for 24 h at 80% to 90% confluence. Cells were exposed to 10 ng/ml EGF either in the presence or absence of 50 μM PDTC and

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: NF-kB inhibition prolongs EGF-induced ERK1/2 activation through downregulation of DUSP1 expression. HCEC were serum starved for 24 h at 80% to 90% confluence. Cells were exposed to 10 ng/ml EGF either in the presence or absence of 50 μM PDTC and

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Inhibition, Activation Assay, Expressing

    Pull-down experiments validate NKCC1-p-ERK1/2 interaction induced by EGF. HCEC were serum starved for 24 h at 80% to 90% confluence. (A) Cells were exposed to either 2.5 or 10 ng/ml EGF for 10 min. Membrane enriched pellets were obtained from different

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: Pull-down experiments validate NKCC1-p-ERK1/2 interaction induced by EGF. HCEC were serum starved for 24 h at 80% to 90% confluence. (A) Cells were exposed to either 2.5 or 10 ng/ml EGF for 10 min. Membrane enriched pellets were obtained from different

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques:

    Selective inhibition in DUSP6 overexpression HCEC subline (DUSP6+) of EGF and PDBu -induced ERK1/2 and p-NKCC1 phosphorylation. HCEC were serum starved for 24 h at 80% to 90% confluence. Representative Western blot analysis compares p-NKCC1, p-p38, p-JNK1/2/SAPK

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: Selective inhibition in DUSP6 overexpression HCEC subline (DUSP6+) of EGF and PDBu -induced ERK1/2 and p-NKCC1 phosphorylation. HCEC were serum starved for 24 h at 80% to 90% confluence. Representative Western blot analysis compares p-NKCC1, p-p38, p-JNK1/2/SAPK

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Inhibition, Over Expression, Western Blot

    Dependence of EGF-induced ERK1/2 and NKCC1 phosphorylation on [Ca 2+ ] i . HCEC were serum starved for 24 h at 80% to 90% confluence. Representative Western blot analysis compares the dose dependent inhibitory effects of exposure to BAPTA on 10 ng/ml EGF-induced

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: Dependence of EGF-induced ERK1/2 and NKCC1 phosphorylation on [Ca 2+ ] i . HCEC were serum starved for 24 h at 80% to 90% confluence. Representative Western blot analysis compares the dose dependent inhibitory effects of exposure to BAPTA on 10 ng/ml EGF-induced

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Western Blot

    Time-dependent changes in ERK1/2 and NKCC1 phosphorylation status induced by EGF and PDBu. HCEC were serum starved for 24 h at 80% to 90% confluence. Panel A shows the effects of exposure to 10 ng/ml EGF for up to 90 min with a representative Western

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: Time-dependent changes in ERK1/2 and NKCC1 phosphorylation status induced by EGF and PDBu. HCEC were serum starved for 24 h at 80% to 90% confluence. Panel A shows the effects of exposure to 10 ng/ml EGF for up to 90 min with a representative Western

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Western Blot

    Time-dependent changes in p-ERK1/2 association with NKCC. HCEC were serum starved for 24 h at 80% to 90% confluence. Cells were exposed to 10 ng/ml EGF for up to 120 min. Membrane-enriched fractions were obtained following centrifugation. Pellets were

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: Time-dependent changes in p-ERK1/2 association with NKCC. HCEC were serum starved for 24 h at 80% to 90% confluence. Cells were exposed to 10 ng/ml EGF for up to 120 min. Membrane-enriched fractions were obtained following centrifugation. Pellets were

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Centrifugation

    Inhibition of PDBu-induced PKC activation of NKCC1 and ERK1/2 phosphorylation. HCEC were serum starved for 24 h at 80% to 90% confluence. Representative Western blot analysis comparing the effects of exposure to 1 μM PDBu in the presence and absence

    Journal: Cellular Physiology and Biochemistry

    Article Title: Dependence of Corneal Epithelial Cell Proliferation on Modulation of Interactions Between ERK1/2 and NKCC1

    doi: 10.1159/000335764

    Figure Lengend Snippet: Inhibition of PDBu-induced PKC activation of NKCC1 and ERK1/2 phosphorylation. HCEC were serum starved for 24 h at 80% to 90% confluence. Representative Western blot analysis comparing the effects of exposure to 1 μM PDBu in the presence and absence

    Article Snippet: Anti-ERK1, phospho-ERK1/2, goat anti-mouse IgG-HRP, goat anti-rabbit IgG-HRP antibody, and anti-(H196) actin, anti-ERK1/2, anti-p38, and β-actin antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Inhibition, Activation Assay, Western Blot