Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCα activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in .The results are the means±SD of four independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity. The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005), and among the DG molecular species ( # P <0.05).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCβΙΙ activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in . The results are the means ± SD of three independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity. The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCγ activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in . The results are the means±SD of five independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity. The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005), and among the DG molecular species ( # P <0.05).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCδ activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in . The results are the means±SD of four independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity. The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005), and among the DG molecular species ( # P <0.05, ## P <0.01).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCε activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in . The results are the means±SD of four independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity. The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005), and among the DG molecular species ( # P <0.05).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCη activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in . The results are the means±SD of four independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity.

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on the activation of PKCη expressed in COS-7 cells. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs, as described in . The activities of vector-transfected cells were subtracted. The results are the means±SD of three independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG). The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005), and among the DG molecular species ( # P <0.05, ## P <0.01).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay, Plasmid Preparation, Transfection

Journal: Biochemistry and Biophysics Reports

Article Title: Activation of conventional and novel protein kinase C isozymes by different diacylglycerol molecular species

doi: 10.1016/j.bbrep.2016.07.017

Figure Lengend Snippet: Effects of different DG molecular species on PKCθ activation. Lipid vesicles were prepared with different DG molecular species (16:0/16:0-, 16:0/18:1-, 18:1/18:1-, 18:0/20:4- and 18:0/22:6-DG) and PKC activity toward MBP was determined in vesicles as a function of increasing concentrations of DGs as described in . The results are the means ± SD of three independent experiments. The left axis shows the relative activity compared to the control (0 mmol% DG) and the right axis shows the specific activity. The data are significantly different from the control, 0 mmol% DG (* P <0.05, ** P <0.01, *** P <0.005), and among the DG molecular species ( # P <0.05, ## P <0.01).

Article Snippet: PKC isoforms (α (product number: 01-133), βΙΙ (01-165), γ (01-137), δ (01-135), ε (01-136), η (01-138) and θ (01-140)) were obtained from Carna Biosciences (Kobe, Japan).

Techniques: Activation Assay, Activity Assay

Journal: Cell Stem Cell

Article Title: Single-Cell Sequencing of iPSC-Dopamine Neurons Reconstructs Disease Progression and Identifies HDAC4 as a Regulator of Parkinson Cell Phenotypes

doi: 10.1016/j.stem.2018.10.023

Figure Lengend Snippet:

Article Snippet: PRKCB , ProSci , Cat#43-319.

Techniques: Recombinant, Control, Expressing, Reverse Transcription, SYBR Green Assay, Software

Journal: Journal of Clinical Bioinformatics

Article Title: Proteomic characterization of non-small cell lung cancer in a comprehensive translational thoracic oncology database

doi: 10.1186/2043-9113-1-8

Figure Lengend Snippet: Source of Antibodies

Article Snippet: PKCB-β2 , GeneTex.

Techniques:

Journal: Cell reports

Article Title: PKCε Inhibits Neuronal Dendritic Spine Development through Dual Phosphorylation of Ephexin5

doi: 10.1016/j.celrep.2018.11.005

Figure Lengend Snippet: (A) Protein kinase C (PKC) isoform expression is detectable in the developing brain and increases with age. Mouse brains were dissected and lysed at indicated ages and immunoblotted with isoform specific PKC antibodies. (B) PKC isoforms are brain enriched. Lysates from indicated mouse tissues (Br, brain; Ht, heart; Kd, kidney; Li, liver) at postnatal day 6 (P6) were immunoblotted for the PKC isoforms shown. Equal protein loading was confirmed using Silver Stain. (C) PKC isoforms are expressed in the hippocampus early in development.Lysates were prepared from cerebral cortex (Ctx), hippocampus (Hip), diencephalon/midbrain/hindbrain (DMH), and olfactory bulbs (OB) from P6 mice and immunoblotted for the PKC isoforms shown. (D) Experimental setup. Fractionation protocol for collecting samples tomeasure PKC membrane association. (E) PKC isoforms are localized at neuronal membranes in the hippocampusearly in development, indicative of their activation. Fractionated extracts generated from neonatal mouse hippocampi were immunoblotted for the PKC isoforms shown. Cyto, cytosolic proteins co-fractionating with Tuj1; Mem, membrane-associated proteins co-fractionating with transferrin receptor (TFRC); Insol, remaining fraction of detergent-insoluble proteins. (F) PKC isoform expression in hippocampal neuronal cultures increases withage of the culture. Cultured hippocampal neurons were lysed at indicated days in vitro (DIV) and immunoblotted for the PKC isoforms shown. (G) PKCa, PKCb, and PKCg are localized at neuronal membranes in immature hippocampal neuronal cultures. PKCε membrane localization is scarce by comparison. Fractionated extracts of DIV11 neuronal cultures were prepared as in (D) and immunoblotted. See also .

Article Snippet: The following antibodies are commercially available and used according to manufacturer’s suggestions for Western Blots, immunocytochemistry and immunoprecipitation: PKCa (BD Biosciences 610107), PKCb (BD Biosciences 610127), PKCg (Santa Cruz Biotechnology SC-211), PKCε (BD Biosciences 610085), RhoA (Santa Cruz Biotechnology SC-418), b-Actin (Abcam ab8226), Tuj1/bIII-tubulin (EMD Millipore TU-20), Transferrin receptor (Invitrogen 136800), HA (Sigma H3663), Myc (Abcam ab32), Synapsin (Millipore AB1543P), Synaptophysin (Millipore MAB368), PSD95 (Thermo Scientific MA1–046), and GAPDH ( ).

Techniques: Expressing, Silver Staining, Fractionation, Activation Assay, Generated, Cell Culture, In Vitro