2d dige phosphor-proteomics analysis and protein identification Search Results


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Effects of short-term taurine supplementation on the relative mRNA expression levels of skeletal muscle function-related genes in GAS ( A ), soleus ( B ), plantaris ( C ), and TA ( D ) muscles of rats in the water, 0.5% taurine, and 1% taurine groups. Skeletal muscles of SD rats at 14 weeks of age were collected 4 h after administration on the 10th day and analyzed via quantitative reverse transcription-polymerase chain reaction (qRT-PCR) to determine the mRNA expression levels of myocyte enhancer factor <t>2A</t> ( <t>Mef2a</t> / MEF2A), peroxisome proliferator-activated receptor gamma coactivator 1-alpha ( Ppargc1a /PGC-1α), succinate dehydrogenase complex flavoprotein subunit A ( Sdha /SDH), cytochrome c, somatic ( Cycs /Cycs), myoglobin ( Mb ), solute carrier family 2 member 4 ( Slc2a4 /GLUT4), and solute carrier family 6 member 6 ( Slc6a6 /TauT). The administration levels of taurine are indicated in . Values shown represent the mean ± SE (n = 3–6). * p < 0.05, ** p < 0.01, *** p <0.001, statistically significant versus the value of the water group. Results were analyzed using Dunnett’s test.
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Applied Biomics 2d dige phosphor-proteomics analysis and protein identification
Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by <t>2D</t> gel <t>electrophoresis,</t> followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).
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Image Search Results


Effects of short-term taurine supplementation on the relative mRNA expression levels of skeletal muscle function-related genes in GAS ( A ), soleus ( B ), plantaris ( C ), and TA ( D ) muscles of rats in the water, 0.5% taurine, and 1% taurine groups. Skeletal muscles of SD rats at 14 weeks of age were collected 4 h after administration on the 10th day and analyzed via quantitative reverse transcription-polymerase chain reaction (qRT-PCR) to determine the mRNA expression levels of myocyte enhancer factor 2A ( Mef2a / MEF2A), peroxisome proliferator-activated receptor gamma coactivator 1-alpha ( Ppargc1a /PGC-1α), succinate dehydrogenase complex flavoprotein subunit A ( Sdha /SDH), cytochrome c, somatic ( Cycs /Cycs), myoglobin ( Mb ), solute carrier family 2 member 4 ( Slc2a4 /GLUT4), and solute carrier family 6 member 6 ( Slc6a6 /TauT). The administration levels of taurine are indicated in . Values shown represent the mean ± SE (n = 3–6). * p < 0.05, ** p < 0.01, *** p <0.001, statistically significant versus the value of the water group. Results were analyzed using Dunnett’s test.

Journal: International Journal of Molecular Sciences

Article Title: Taurine Stimulates AMP-Activated Protein Kinase and Modulates the Skeletal Muscle Functions in Rats via the Induction of Intracellular Calcium Influx

doi: 10.3390/ijms24044125

Figure Lengend Snippet: Effects of short-term taurine supplementation on the relative mRNA expression levels of skeletal muscle function-related genes in GAS ( A ), soleus ( B ), plantaris ( C ), and TA ( D ) muscles of rats in the water, 0.5% taurine, and 1% taurine groups. Skeletal muscles of SD rats at 14 weeks of age were collected 4 h after administration on the 10th day and analyzed via quantitative reverse transcription-polymerase chain reaction (qRT-PCR) to determine the mRNA expression levels of myocyte enhancer factor 2A ( Mef2a / MEF2A), peroxisome proliferator-activated receptor gamma coactivator 1-alpha ( Ppargc1a /PGC-1α), succinate dehydrogenase complex flavoprotein subunit A ( Sdha /SDH), cytochrome c, somatic ( Cycs /Cycs), myoglobin ( Mb ), solute carrier family 2 member 4 ( Slc2a4 /GLUT4), and solute carrier family 6 member 6 ( Slc6a6 /TauT). The administration levels of taurine are indicated in . Values shown represent the mean ± SE (n = 3–6). * p < 0.05, ** p < 0.01, *** p <0.001, statistically significant versus the value of the water group. Results were analyzed using Dunnett’s test.

Article Snippet: Antibodies against peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), myocyte enhancer factor 2A (MEF2A), and myoglobin were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Expressing, Muscles, Reverse Transcription, Polymerase Chain Reaction, Quantitative RT-PCR

Effects of short-term taurine supplementation on the phosphorylation of AMP-activated protein kinase (AMPK) ( A , E , I ) and expression levels of MEF2A ( B , F , J ), PGC-1α ( C , G , K ), and myoglobin ( D , H , L ) proteins in GAS, soleus, and TA muscles of rats in the water, 0.5% taurine, and 1% taurine groups. Skeletal muscles of SD rats at 14 weeks of age were collected 4 h after administration on the 10th day. The administration levels of taurine are indicated in . Proteins were extracted and analyzed by Western blot as described in the Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). * p < 0.05, ** p < 0.01, *** p < 0.001, statistically significant vs. the values of the water group. Results were analyzed using Dunnett’s test.

Journal: International Journal of Molecular Sciences

Article Title: Taurine Stimulates AMP-Activated Protein Kinase and Modulates the Skeletal Muscle Functions in Rats via the Induction of Intracellular Calcium Influx

doi: 10.3390/ijms24044125

Figure Lengend Snippet: Effects of short-term taurine supplementation on the phosphorylation of AMP-activated protein kinase (AMPK) ( A , E , I ) and expression levels of MEF2A ( B , F , J ), PGC-1α ( C , G , K ), and myoglobin ( D , H , L ) proteins in GAS, soleus, and TA muscles of rats in the water, 0.5% taurine, and 1% taurine groups. Skeletal muscles of SD rats at 14 weeks of age were collected 4 h after administration on the 10th day. The administration levels of taurine are indicated in . Proteins were extracted and analyzed by Western blot as described in the Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). * p < 0.05, ** p < 0.01, *** p < 0.001, statistically significant vs. the values of the water group. Results were analyzed using Dunnett’s test.

Article Snippet: Antibodies against peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), myocyte enhancer factor 2A (MEF2A), and myoglobin were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Phospho-proteomics, Expressing, Muscles, Western Blot

Effects of taurine on the expression levels of MEF2A, PGC-1α, myoglobin, GLUT4, and TauT genes in L6 myotubes. ( A ) L6 myotubes were treated with 0.3 mM taurine for the time periods indicated. ( B ) L6 cells were treated with 0, 0.05, 0.1, 0.2, and 0.3 mM taurine for 1 h. Total RNA was extracted from the cells after treatment with taurine and qRT-PCR analysis was carried out to determine the mRNA expression levels of Mef2a , Ppargc1a , Mb , Slc2a4 , and Slc6a6 in L6 cells, as described in the Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). Results were analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s test for multiple comparisons. Values with different superscript lowercase letters indicate significant differences ( p < 0.05).

Journal: International Journal of Molecular Sciences

Article Title: Taurine Stimulates AMP-Activated Protein Kinase and Modulates the Skeletal Muscle Functions in Rats via the Induction of Intracellular Calcium Influx

doi: 10.3390/ijms24044125

Figure Lengend Snippet: Effects of taurine on the expression levels of MEF2A, PGC-1α, myoglobin, GLUT4, and TauT genes in L6 myotubes. ( A ) L6 myotubes were treated with 0.3 mM taurine for the time periods indicated. ( B ) L6 cells were treated with 0, 0.05, 0.1, 0.2, and 0.3 mM taurine for 1 h. Total RNA was extracted from the cells after treatment with taurine and qRT-PCR analysis was carried out to determine the mRNA expression levels of Mef2a , Ppargc1a , Mb , Slc2a4 , and Slc6a6 in L6 cells, as described in the Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). Results were analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s test for multiple comparisons. Values with different superscript lowercase letters indicate significant differences ( p < 0.05).

Article Snippet: Antibodies against peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), myocyte enhancer factor 2A (MEF2A), and myoglobin were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Expressing, Quantitative RT-PCR

Taurine stimulates the phosphorylation of AMPK ( A ) and the expression of MEF2A ( B ), PGC-1α ( C ), myoglobin ( D ), and GLUT4 ( E ) proteins in L6 myotubes. L6 myotubes were treated with 0, 0.05, 0.1, 0.2, and 0.3 mM taurine for 1 h. After treatment, L6 cells were analyzed by Western blot, as described in Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). Results were analyzed using one-way ANOVA followed by Tukey’s test for multiple comparisons. Values with different superscript lowercase letters indicate significant differences ( p < 0.05).

Journal: International Journal of Molecular Sciences

Article Title: Taurine Stimulates AMP-Activated Protein Kinase and Modulates the Skeletal Muscle Functions in Rats via the Induction of Intracellular Calcium Influx

doi: 10.3390/ijms24044125

Figure Lengend Snippet: Taurine stimulates the phosphorylation of AMPK ( A ) and the expression of MEF2A ( B ), PGC-1α ( C ), myoglobin ( D ), and GLUT4 ( E ) proteins in L6 myotubes. L6 myotubes were treated with 0, 0.05, 0.1, 0.2, and 0.3 mM taurine for 1 h. After treatment, L6 cells were analyzed by Western blot, as described in Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). Results were analyzed using one-way ANOVA followed by Tukey’s test for multiple comparisons. Values with different superscript lowercase letters indicate significant differences ( p < 0.05).

Article Snippet: Antibodies against peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), myocyte enhancer factor 2A (MEF2A), and myoglobin were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Phospho-proteomics, Expressing, Western Blot

Phospholipase C (PLC) inhibitor suppresses the phosphorylation of AMPK and the expression levels of MEF2A, PGC-1α, myoglobin, and GLUT4 genes and proteins. L6 cells were treated with 0.3 mM taurine for 1 h in the presence or absence of 1.0 μM YM and preincubated for 5 min. After treatment, L6 cells were analyzed via qRT-PCR analysis ( A ) or Western blot ( B – F ), as described in the Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). The results were analyzed using one-way ANOVA followed by Tukey’s test for multiple comparisons. Values with different superscript lowercase letters indicate significant differences ( p < 0.05).

Journal: International Journal of Molecular Sciences

Article Title: Taurine Stimulates AMP-Activated Protein Kinase and Modulates the Skeletal Muscle Functions in Rats via the Induction of Intracellular Calcium Influx

doi: 10.3390/ijms24044125

Figure Lengend Snippet: Phospholipase C (PLC) inhibitor suppresses the phosphorylation of AMPK and the expression levels of MEF2A, PGC-1α, myoglobin, and GLUT4 genes and proteins. L6 cells were treated with 0.3 mM taurine for 1 h in the presence or absence of 1.0 μM YM and preincubated for 5 min. After treatment, L6 cells were analyzed via qRT-PCR analysis ( A ) or Western blot ( B – F ), as described in the Materials and Methods section. Values shown represent the mean ± SE (n = 3–6). The results were analyzed using one-way ANOVA followed by Tukey’s test for multiple comparisons. Values with different superscript lowercase letters indicate significant differences ( p < 0.05).

Article Snippet: Antibodies against peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), myocyte enhancer factor 2A (MEF2A), and myoglobin were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Phospho-proteomics, Expressing, Quantitative RT-PCR, Western Blot

List of sequences of PCR primers used in this study.

Journal: International Journal of Molecular Sciences

Article Title: Taurine Stimulates AMP-Activated Protein Kinase and Modulates the Skeletal Muscle Functions in Rats via the Induction of Intracellular Calcium Influx

doi: 10.3390/ijms24044125

Figure Lengend Snippet: List of sequences of PCR primers used in this study.

Article Snippet: Antibodies against peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α), myocyte enhancer factor 2A (MEF2A), and myoglobin were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

Techniques: Sequencing

Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by 2D gel electrophoresis, followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).

Journal: DNA repair

Article Title: Localization of X-ray cross complementing gene 1 protein in the nuclear matrix is controlled by casein kinase II-dependent phosphorylation in response to oxidative damage.

doi: 10.1016/j.dnarep.2009.06.003

Figure Lengend Snippet: Fig. 3. Phosphorylation status of XRCC1 in each cellular fraction. WT or CKM cells were exposed to H2O2 as described in Fig. 1C, and proteins from each fraction were analyzed by 2D gel electrophoresis, followed by Western blotting. The position of non-phosphorylated XRCC1 is indicated by a portion of proteins from WT cells that was treated with -PPase, fractionated, and analyzed simultaneously (lanes 9 and 10).

Article Snippet: The proteins were desalted and the buffers replaced with 2D electrophoresis buffer (7 M urea, 2 M thiourea and 4% CHAPS) with protein desalting spin columns (Pierce).

Techniques: Phospho-proteomics, Two-Dimensional Gel Electrophoresis, Electrophoresis, Western Blot