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A Accumulation of MAPK, PI3K/AKT, YAP and PKC signalling effectors including total and <t>phosphorylated</t> DUSP6, <t>MARCKS,</t> ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 10 nM Trametinib (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. . B Expression levels of pS6 and DUSP6 (normalised to total S6 or REVERT staining, respectively) in vehicle control or 10 nM Trametinib-treated GNAQ/GNA11 -mutant (solid dot) or wild-type (crossed dot) UM cell lines. Data derived from three independent biological experiments ( n = 3), and P values were calculated using paired t tests. ns not significant. C Percentage of cells undergoing S-phase inhibition (dotted line set at 50% S-phase inhibition) and change in % sub-G1 (dotted line set at 30% sub-G1) in GNAQ/GNA11 -mutant (solid circle) or wild-type (crossed circle) UM cell lines treated with 5 µM IDE196 (data derived from ), 10 nM Trametinib or 2 µM BEZ235. Data derived from three independent biological experiments ( n = 3).

Phosphorylated Marcks, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 103 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "PKC-independent PI3K signalling diminishes PKC inhibitor sensitivity in uveal melanoma"

Article Title: PKC-independent PI3K signalling diminishes PKC inhibitor sensitivity in uveal melanoma

Journal: Oncogenesis

doi: 10.1038/s41389-024-00511-8

A Accumulation of MAPK, PI3K/AKT, YAP and PKC signalling effectors including total and phosphorylated DUSP6, MARCKS, ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 10 nM Trametinib (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. . B Expression levels of pS6 and DUSP6 (normalised to total S6 or REVERT staining, respectively) in vehicle control or 10 nM Trametinib-treated GNAQ/GNA11 -mutant (solid dot) or wild-type (crossed dot) UM cell lines. Data derived from three independent biological experiments ( n = 3), and P values were calculated using paired t tests. ns not significant. C Percentage of cells undergoing S-phase inhibition (dotted line set at 50% S-phase inhibition) and change in % sub-G1 (dotted line set at 30% sub-G1) in GNAQ/GNA11 -mutant (solid circle) or wild-type (crossed circle) UM cell lines treated with 5 µM IDE196 (data derived from ), 10 nM Trametinib or 2 µM BEZ235. Data derived from three independent biological experiments ( n = 3).

Figure Legend Snippet: A Accumulation of MAPK, PI3K/AKT, YAP and PKC signalling effectors including total and phosphorylated DUSP6, MARCKS, ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 10 nM Trametinib (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. . B Expression levels of pS6 and DUSP6 (normalised to total S6 or REVERT staining, respectively) in vehicle control or 10 nM Trametinib-treated GNAQ/GNA11 -mutant (solid dot) or wild-type (crossed dot) UM cell lines. Data derived from three independent biological experiments ( n = 3), and P values were calculated using paired t tests. ns not significant. C Percentage of cells undergoing S-phase inhibition (dotted line set at 50% S-phase inhibition) and change in % sub-G1 (dotted line set at 30% sub-G1) in GNAQ/GNA11 -mutant (solid circle) or wild-type (crossed circle) UM cell lines treated with 5 µM IDE196 (data derived from ), 10 nM Trametinib or 2 µM BEZ235. Data derived from three independent biological experiments ( n = 3).

Techniques Used: Control, Western Blot, Staining, Expressing, Mutagenesis, Derivative Assay, Inhibition

A Fold change in DUSP6 and pS6 expression (normalised log 2 protein expression in drug-treated – normalised log 2 protein expression in control-treated cells) in GNAQ/GNA11 -mutant (solid circle) and wild-type (crossed circle) UM cell lines treated with 5 µM IDE196, 10 nM Trametinib, or 2 µM BEZ235. Data compared using one-way ANOVA with the Geisser–Greenhouse correction and Tukey’s multiple comparison test, adjusted P values are shown. Data derived from three independent biological experiments ( n = 3, mean ± SD). B Accumulation of MAPK, PI3K, YAP and PKC signalling effectors, including total and phosphorylated DUSP6, MARCKS, ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 2 µM BEZ235 (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. .

Figure Legend Snippet: A Fold change in DUSP6 and pS6 expression (normalised log 2 protein expression in drug-treated – normalised log 2 protein expression in control-treated cells) in GNAQ/GNA11 -mutant (solid circle) and wild-type (crossed circle) UM cell lines treated with 5 µM IDE196, 10 nM Trametinib, or 2 µM BEZ235. Data compared using one-way ANOVA with the Geisser–Greenhouse correction and Tukey’s multiple comparison test, adjusted P values are shown. Data derived from three independent biological experiments ( n = 3, mean ± SD). B Accumulation of MAPK, PI3K, YAP and PKC signalling effectors, including total and phosphorylated DUSP6, MARCKS, ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 2 µM BEZ235 (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. .

Techniques Used: Expressing, Control, Mutagenesis, Comparison, Derivative Assay, Western Blot, Staining

Control:

Article Title: MARCKS as a negative regulator of lipopolysaccharide signaling.
Article Snippet: A total of 50 mg total cell protein was loaded on SDS-PAGE and transferred to nitrocellulose membrane (GE Healthcare). .. Detection of phosphorylated MARCKS was done using specific primary Abs (Ser152/156; Cell Signaling Technology) and appropriate secondary goat anti-rabbit IgG-HRP (Abcam). a/bTubulin Abs (Cell Signaling Technology) were used as loading control. .. HEK293 cells were transiently transfected with 200 ng MARCKS siRNA cassette (59-TCCTGTCCGTTCGCTTTGTTGATATCCGCAAAGCGAACGGACAGGA-39) (GenScript) or control siRNA (psiRNA h7SKgz scr; InvivoGen), pFLAG-TLR4, pEFBOS-MD-2 expression plasmids and pELAM1-NF-ΚB–dependent or pGL-IP10 promotor-dependent luciferase, and constitutive Renilla (phRL-TK; Promega) reporter plasmids.

Incubation:

Article Title: PKC-independent PI3K signalling diminishes PKC inhibitor sensitivity in uveal melanoma
Article Snippet: Protein lysates (20 μg) were loaded onto 8–10% resolving SDS-PAGE and transferred to Immobilon-FL (Sigma-Aldrich) PVDF membranes. .. Membranes were incubated at 4 °C overnight in primary antibodies diluted in Intercept Blocking Buffer (TBS) (Li-Cor, Lincoln, NE, USA) or Odyssey Blocking Buffer (Li-Cor) with Tween 20 (0.05%), as follows: total MARCKS (1:1000, 2C2, WH0004082M6, Sigma-Aldrich), phosphorylated MARCKS (pMARCKS; Ser 152/156 , 1:1000, 2741 S, Cell Signaling Technology, Danvers, MA, USA), DUSP6 (1:250 or 1:1000, EPR129Y, ab76310, Abcam, Cambridge, UK), total AKT (1:1000, 40D4, 2920S, Cell Signaling Technology), phosphorylated AKT (pAKT; Ser 473 , 1:100, D9E, 4060S, Cell Signaling Technology), pAKT (Ser 473 , 1:500, 736E11, 3787, Cell Signaling Technology), total ribosomal S6 (1:500, 54D2, 2317 S, Cell Signaling Technology), phosphorylated ribosomal S6 (pS6; Ser 235/236 , 1:1000, 2F9, 4856S, Cell Signaling Technology), total YAP (1:500, 1A12, 12395S, Cell Signaling Technology), phosphorylated YAP (pYAP; Ser 127 , 1:2000, 4911, Cell Signaling Technology), total ERK (1:2 000, 137F5, 4695S, Cell Signaling Technology), phosphorylated ERK (pERK; Tyr 204 , 1:250, E-4, SC-7383, Santa Cruz, Dallas, TX, USA), and MEK1/2 (1:500, L38C12, 4694S, Cell Signaling Technology). .. Membranes were washed with tris-buffered saline with 0.05% Tween 20 (TTBS) and incubated for one hour in secondary antibodies IRDye® 800CW Rabbit anti-Mouse, IRDye® 800CW Mouse anti-Rabbit, IRDye® 680LT Rabbit anti-Mouse or IRDye® 680LT Mouse anti-Rabbit (all at 1:20,000, Li-Cor), diluted 1:1 in Intercept Blocking Buffer (Li-Cor) or Odyssey Blocking Buffer (Li-Cor) with TTBS.

Blocking Assay:

other:

Article Title: Platelet-derived growth factor (PDGF)-induced activation of Erk5 MAP-kinase is dependent on Mekk2, Mek1/2, PKC and PI3-kinase, and affects BMP signaling.
Article Snippet: Platelet-derived growth factor (PDGF)-induced activation of Erk5 MAPkinase is dependent on Mekk2, Mek1/2, PKC and PI3-kinase, and affects BMP signaling Maria Tsioumpekou, Natalia Papadopoulos, Fatima Burovic, Carl-Henrik Heldin, Johan Lennartsson PII: S0898-6568(16)30147-4 DOI: doi: 10.1016/j.cellsig.2016.06.013 Reference: CLS 8714 To appear in: Cellular Signalling Received date: 8 February 2016 Revised date: 16 June 2016 Accepted date: 16 June 2016 Please cite this article as: Maria Tsioumpekou, Natalia Papadopoulos, Fatima Burovic, Carl-Henrik Heldin, Johan Lennartsson, Platelet-derived growth factor (PDGF)-induced activation of Erk5 MAP-kinase is dependent on Mekk2, Mek1/2, PKC and PI3-kinase, and affects BMP signaling, Cellular Signalling (2016), doi: 10.1016/j.cellsig.2016.06.013 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form.

Western Blot:

Article Title: Protein kinase inhibitor responses in uveal melanoma reflects a diminished dependency on PKC-MAPK signaling
Article Snippet: Total proteins (20 μg) were resolved on 10% SDS-PAGE and transferred to Immobilon-P membranes (Millipore). .. Western blots were probed with the following antibodies: total ERK (1:2000, 4695, Cell Signaling, Danvers, MA), phosphorylated ERK (Tyr204,1:1000, SC-7383, Santa Cruz, Dallas, TX), total AKT (1:1000, 2920, Cell Signaling), phosphorylated AKT (Ser473, 1:500, 3787, Cell Signaling), DUSP6 (1:1000, AB76310, Abcam, Cambridge, United Kingdom), total YAP (1A12, 1:500, 123955, Cell Signaling), phosphorylated YAP (Ser127, 1:2000, 4911, Cell Signaling), total MARCKS (FC141–2C2, Sigma), phosphorylated MARCKS (Ser152/156, 1:1000, 2741S, Cell Signaling), total ribosomal S6 (1:500, 54D2, Cell Signaling), phosphorylated ribosomal S6 (Ser235/236, 1:1000, 2F9, Cell Signaling) overnight at 4 °C. .. Membranes were washed with tris-buffered saline with 0.05% Tween-20 and then incubated with secondary antibodies IRDye® 800CW Donkey anti-Mouse, IRDye® 800CW Donkey anti-Rabbit, IRDye® 680LT Donkey anti-Mouse, IRDye® 680LT Donkey anti-Rabbit (LI-COR, Lincoln, NE).

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Journal: Oncogenesis

Article Title: PKC-independent PI3K signalling diminishes PKC inhibitor sensitivity in uveal melanoma

doi: 10.1038/s41389-024-00511-8

Figure Lengend Snippet: A Accumulation of MAPK, PI3K/AKT, YAP and PKC signalling effectors including total and phosphorylated DUSP6, MARCKS, ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 10 nM Trametinib (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. . B Expression levels of pS6 and DUSP6 (normalised to total S6 or REVERT staining, respectively) in vehicle control or 10 nM Trametinib-treated GNAQ/GNA11 -mutant (solid dot) or wild-type (crossed dot) UM cell lines. Data derived from three independent biological experiments ( n = 3), and P values were calculated using paired t tests. ns not significant. C Percentage of cells undergoing S-phase inhibition (dotted line set at 50% S-phase inhibition) and change in % sub-G1 (dotted line set at 30% sub-G1) in GNAQ/GNA11 -mutant (solid circle) or wild-type (crossed circle) UM cell lines treated with 5 µM IDE196 (data derived from ), 10 nM Trametinib or 2 µM BEZ235. Data derived from three independent biological experiments ( n = 3).

Article Snippet: Membranes were incubated at 4 °C overnight in primary antibodies diluted in Intercept Blocking Buffer (TBS) (Li-Cor, Lincoln, NE, USA) or Odyssey Blocking Buffer (Li-Cor) with Tween 20 (0.05%), as follows: total MARCKS (1:1000, 2C2, WH0004082M6, Sigma-Aldrich), phosphorylated MARCKS (pMARCKS; Ser 152/156 , 1:1000, 2741 S, Cell Signaling Technology, Danvers, MA, USA), DUSP6 (1:250 or 1:1000, EPR129Y, ab76310, Abcam, Cambridge, UK), total AKT (1:1000, 40D4, 2920S, Cell Signaling Technology), phosphorylated AKT (pAKT; Ser 473 , 1:100, D9E, 4060S, Cell Signaling Technology), pAKT (Ser 473 , 1:500, 736E11, 3787, Cell Signaling Technology), total ribosomal S6 (1:500, 54D2, 2317 S, Cell Signaling Technology), phosphorylated ribosomal S6 (pS6; Ser 235/236 , 1:1000, 2F9, 4856S, Cell Signaling Technology), total YAP (1:500, 1A12, 12395S, Cell Signaling Technology), phosphorylated YAP (pYAP; Ser 127 , 1:2000, 4911, Cell Signaling Technology), total ERK (1:2 000, 137F5, 4695S, Cell Signaling Technology), phosphorylated ERK (pERK; Tyr 204 , 1:250, E-4, SC-7383, Santa Cruz, Dallas, TX, USA), and MEK1/2 (1:500, L38C12, 4694S, Cell Signaling Technology).

Techniques: Control, Western Blot, Staining, Expressing, Mutagenesis, Derivative Assay, Inhibition

Journal: Oncogenesis

Article Title: PKC-independent PI3K signalling diminishes PKC inhibitor sensitivity in uveal melanoma

doi: 10.1038/s41389-024-00511-8

Figure Lengend Snippet: A Fold change in DUSP6 and pS6 expression (normalised log 2 protein expression in drug-treated – normalised log 2 protein expression in control-treated cells) in GNAQ/GNA11 -mutant (solid circle) and wild-type (crossed circle) UM cell lines treated with 5 µM IDE196, 10 nM Trametinib, or 2 µM BEZ235. Data compared using one-way ANOVA with the Geisser–Greenhouse correction and Tukey’s multiple comparison test, adjusted P values are shown. Data derived from three independent biological experiments ( n = 3, mean ± SD). B Accumulation of MAPK, PI3K, YAP and PKC signalling effectors, including total and phosphorylated DUSP6, MARCKS, ERK, YAP, S6 and AKT 24 h after treatment with vehicle control (−) or 2 µM BEZ235 (+). Western blot analyses were performed using three independent biological replicates ( n = 3). kD kilodalton. REVERT total protein loading stain is shown in Supplementary Fig. .

Techniques: Expressing, Control, Mutagenesis, Comparison, Derivative Assay, Western Blot, Staining

ROS production is suppressed by PKCβ KO and PKC inhibitor Staurosporine, and MARCKS level and Ser167/170 phosphorylation are not affected in PKCβ KO cells. THP-1-derived PKCβ KO cells (generated using the CRISPR/Cas9 technique) and THP-1 WT cells were differentiated with 100 nM calcitriol for 5 d. Subsequently, ROS production was induced by PMA (100 nM) and determined (in RLU/s) via luminol-amplified chemiluminescence. ( A , B ) Kinetics ( A ) and the respective cumulated production (i.e., the AUC) within 60 min following stimulation ( B ) of total ROS generated by differentiated THP-1 WT and PKCβ KO cells (representative experiment, n = 3). ( C , D ) Kinetics ( C ) and the respective cumulated production within 60 min following stimulation ( D ) of intracellular ROS generated by differentiated THP-1 and PKCβ KO cells (representative experiment, n = 3). ( E ) Primary human monocytes were incubated in medium with Staurosprine (Stauro; 80 nM) for 2.5 h. Subsequently, PMA-induced total ROS production was assessed and depicted as cumulated ROS production within 30 min following stimulation (mean ± SD; n = 2). ( F ) THP-1 WT and PKCβ KO cells were treated with 100 nM PMA. At the indicated time points, cells were harvested. Total cell extracts were prepared, and MARCKS ED phosphorylation (Ser167/170) and protein levels were determined (Western Blot; loading control: GAPDH; representative experiment, n = 3).

Journal: Antioxidants

Article Title: MARCKS Is an Essential Regulator of Reactive Oxygen Species Production in the Monocytic Cell Type

doi: 10.3390/antiox11081600

Figure Lengend Snippet: ROS production is suppressed by PKCβ KO and PKC inhibitor Staurosporine, and MARCKS level and Ser167/170 phosphorylation are not affected in PKCβ KO cells. THP-1-derived PKCβ KO cells (generated using the CRISPR/Cas9 technique) and THP-1 WT cells were differentiated with 100 nM calcitriol for 5 d. Subsequently, ROS production was induced by PMA (100 nM) and determined (in RLU/s) via luminol-amplified chemiluminescence. ( A , B ) Kinetics ( A ) and the respective cumulated production (i.e., the AUC) within 60 min following stimulation ( B ) of total ROS generated by differentiated THP-1 WT and PKCβ KO cells (representative experiment, n = 3). ( C , D ) Kinetics ( C ) and the respective cumulated production within 60 min following stimulation ( D ) of intracellular ROS generated by differentiated THP-1 and PKCβ KO cells (representative experiment, n = 3). ( E ) Primary human monocytes were incubated in medium with Staurosprine (Stauro; 80 nM) for 2.5 h. Subsequently, PMA-induced total ROS production was assessed and depicted as cumulated ROS production within 30 min following stimulation (mean ± SD; n = 2). ( F ) THP-1 WT and PKCβ KO cells were treated with 100 nM PMA. At the indicated time points, cells were harvested. Total cell extracts were prepared, and MARCKS ED phosphorylation (Ser167/170) and protein levels were determined (Western Blot; loading control: GAPDH; representative experiment, n = 3).

Article Snippet: For protein detection, membranes were incubated (4 °C, overnight) with primary antibodies specific for MARCKS (D88D11 XP ® ), phosphorylated (p)-MARCKS (Ser167/170; D13E4 XP ® ), PKCβ (D3E70), Akt (C67E7), or p-Akt (Thr308; D25E6 XP ® ; Cell Signaling Technology, Danvers, MA, USA) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH; Sigma Aldrich, St. Louis, MO, USA).

Techniques: Phospho-proteomics, Derivative Assay, Generated, CRISPR, Amplification, Incubation, Western Blot, Control

Increased monocytic ROS production following TNF long-term preincubation is dependent on MARCKS and PKCβ. ( A , B ) Kinetics ( A ) and the respective cumulated production (i.e., the AUC) within 180 min ( B ) of opsonized bacteria-induced (≥5 bacteria/cell) total ROS generated by 5 d calcitriol-differentiated THP-1 cells following preincubation with 80 ng/mL TNF for 48 h (i.e., added at day 3). Total ROS production was assessed via luminol-amplified chemiluminescence (in RLU/s) (representative experiment, n = 3). ( C , D ) Kinetics ( C ) and the respective cumulated production within 180 min ( D ) of opsonized bacteria-induced intracellular ROS generated by differentiated THP-1 cells following TNF preincubation as described in ( A ) (representative experiment, n = 3). ( E , F ) Kinetics ( E ) and the respective cumulated production within 30 min ( F ) of PMA-induced (100 nM) total ROS generated by primary human monocytes following TNF preincubation (80 ng/mL TNF for 48 h; representative experiment, n = 4). ( G ) Cumulated intracellular ROS production in MARCKS WT and KO clones (incubated as in ( A )) within 180 min following stimulation with bacteria (representative experiment, n = 3). ( H ) Cumulated intracellular ROS production in THP-1 and PKCβ KO cells (incubated as in ( A )) within 180 min following stimulation with bacteria (representative experiment, n = 3).

Journal: Antioxidants

Article Title: MARCKS Is an Essential Regulator of Reactive Oxygen Species Production in the Monocytic Cell Type

doi: 10.3390/antiox11081600

Figure Lengend Snippet: Increased monocytic ROS production following TNF long-term preincubation is dependent on MARCKS and PKCβ. ( A , B ) Kinetics ( A ) and the respective cumulated production (i.e., the AUC) within 180 min ( B ) of opsonized bacteria-induced (≥5 bacteria/cell) total ROS generated by 5 d calcitriol-differentiated THP-1 cells following preincubation with 80 ng/mL TNF for 48 h (i.e., added at day 3). Total ROS production was assessed via luminol-amplified chemiluminescence (in RLU/s) (representative experiment, n = 3). ( C , D ) Kinetics ( C ) and the respective cumulated production within 180 min ( D ) of opsonized bacteria-induced intracellular ROS generated by differentiated THP-1 cells following TNF preincubation as described in ( A ) (representative experiment, n = 3). ( E , F ) Kinetics ( E ) and the respective cumulated production within 30 min ( F ) of PMA-induced (100 nM) total ROS generated by primary human monocytes following TNF preincubation (80 ng/mL TNF for 48 h; representative experiment, n = 4). ( G ) Cumulated intracellular ROS production in MARCKS WT and KO clones (incubated as in ( A )) within 180 min following stimulation with bacteria (representative experiment, n = 3). ( H ) Cumulated intracellular ROS production in THP-1 and PKCβ KO cells (incubated as in ( A )) within 180 min following stimulation with bacteria (representative experiment, n = 3).

Techniques: Bacteria, Generated, Amplification, Clone Assay, Incubation

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