The Experts below are selected from a list of 177075 Experts worldwide ranked by ideXlab platform
Zicai Liang - One of the best experts on this subject based on the ideXlab platform.
-
Malat1 regulates serum response factor through miR-133 as a competing endogenous RNA in myogenesis
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2015Co-Authors: Xiaorui Han, Feng Yang, Huiqing Cao, Zicai LiangAbstract:Metastasis-associated lung adenocarcinoma transcript 1 (Malat1) is an example of a functional long noncoding RNA involved in many biologic processes. However, the mechanisms for Malat1 in myogenesis are unclear. Serum response factor (SRF) is a pivotal transcription factor for muscle proliferation and differentiation and is reported to be a target gene for muscle-specific microRNA-133 (miR-133). In this study, we initially found that silencing Malat1 in the mouse myoblast C2C12 Cell Line inhibited myocyte differentiation and decreased Srf at both the RNA and protein levels. Srf silencing decreased Malat1 expression as well. Further study revealed that Malat1 contained an miR-133 functional target site, and the interplay between Malat1 and Srf was miR-133 dependent. We demonstrated that Malat1 modulates Srf through miR-133 as a competing endogenous RNA and established a novel connection among Malat1, miR-133, and Srf in myoblast differentiation.
-
malat1 regulates serum response factor through mir 133 as a competing endogenous rna in myogenesis
The FASEB Journal, 2015Co-Authors: Feng Yang, Zicai LiangAbstract:Metastasis-associated lung adenocarcinoma transcript 1 (Malat1) is an example of a functional long noncoding RNA involved in many biologic processes. However, the mechanisms for Malat1 in myogenesis are unclear. Serum response factor (SRF) is a pivotal transcription factor for muscle proliferation and differentiation and is reported to be a target gene for muscle-specific microRNA-133 (miR-133). In this study, we initially found that silencing Malat1 in the mouse myoblast C2C12 Cell Line inhibited myocyte differentiation and decreased Srf at both the RNA and protein levels. Srf silencing decreased Malat1 expression as well. Further study revealed that Malat1 contained an miR-133 functional target site, and the interplay between Malat1 and Srf was miR-133 dependent. We demonstrated that Malat1 modulates Srf through miR-133 as a competing endogenous RNA and established a novel connection among Malat1, miR-133, and Srf in myoblast differentiation.—Han, X., Yang, F., Cao, H., Liang. Z. Malat1 regulates serum ...
Jonathan Levin - One of the best experts on this subject based on the ideXlab platform.
-
Inhibition of myoblast differentiation by Sfrp1 and Sfrp2
Cell and Tissue Research, 2008Co-Authors: Simon Descamps, Hayat Arzouk, Henri Bernardi, Yann Fedon, Yves Reyne, Bernadette Rossano, Francis Bacou, Jonathan LevinAbstract:Secreted Frizzled-related proteins (Sfrps) are extraCellular regulators of Wnt signalling and play important roles in developmental and oncogenic processes. They are known to be upregulated in regenerating muscle and in myoblast cultures but their function is unknown. Here, we show that the addition of recombinant Sfrp1 or Sfrp2 to C2C12 Cell Line cultures or to primary cultures of satellite Cells results in the inhibition of myotube formation with no significant effect on the Cell cycle or apoptosis. Even though at confluence, treated and untreated cultures are identical in appearance, analyses have shown that, for maximum effect, the Cells have to be treated while they are proliferating. Furthermore, removal of Sfrp from the culture medium during differentiation restores normal myotube formation. We conclude that Sfrp1 and Sfrp2 act to prevent myoblasts from entering the terminal differentiation process.
-
Inhibition of myoblast differentiation by Sfrp1 and Sfrp2
Cell and Tissue Research, 2008Co-Authors: Simon Descamps, Hayat Arzouk, Henri Bernardi, Yann Fedon, Yves Reyne, Bernadette Rossano, Francis Bacou, Jonathan LevinAbstract:Secreted Frizzled-related proteins (Sfrps) are extraCellular regulators of Wnt signalling and play important roles in developmental and oncogenic processes. They are known to be upregulated in regenerating muscle and in myoblast cultures but their function is unknown. Here, we show that the addition of recombinant Sfrp1 or Sfrp2 to C2C12 Cell Line cultures or to primary cultures of satellite Cells results in the inhibition of myotube formation with no significant effect on the Cell cycle or apoptosis. Even though at confluence, treated and untreated cultures are identical in appearance, analyses have shown that, for maximum effect, the Cells have to be treated while they are proliferating. Furthermore, removal of Sfrp from the culture medium during differentiation restores normal myotube formation. We conclude that Sfrp1 and Sfrp2 act to prevent myoblasts from entering the terminal differentiation process.
Simon Descamps - One of the best experts on this subject based on the ideXlab platform.
-
Inhibition of myoblast differentiation by Sfrp1 and Sfrp2
Cell and Tissue Research, 2008Co-Authors: Simon Descamps, Hayat Arzouk, Henri Bernardi, Yann Fedon, Yves Reyne, Bernadette Rossano, Francis Bacou, Jonathan LevinAbstract:Secreted Frizzled-related proteins (Sfrps) are extraCellular regulators of Wnt signalling and play important roles in developmental and oncogenic processes. They are known to be upregulated in regenerating muscle and in myoblast cultures but their function is unknown. Here, we show that the addition of recombinant Sfrp1 or Sfrp2 to C2C12 Cell Line cultures or to primary cultures of satellite Cells results in the inhibition of myotube formation with no significant effect on the Cell cycle or apoptosis. Even though at confluence, treated and untreated cultures are identical in appearance, analyses have shown that, for maximum effect, the Cells have to be treated while they are proliferating. Furthermore, removal of Sfrp from the culture medium during differentiation restores normal myotube formation. We conclude that Sfrp1 and Sfrp2 act to prevent myoblasts from entering the terminal differentiation process.
-
Inhibition of myoblast differentiation by Sfrp1 and Sfrp2
Cell and Tissue Research, 2008Co-Authors: Simon Descamps, Hayat Arzouk, Henri Bernardi, Yann Fedon, Yves Reyne, Bernadette Rossano, Francis Bacou, Jonathan LevinAbstract:Secreted Frizzled-related proteins (Sfrps) are extraCellular regulators of Wnt signalling and play important roles in developmental and oncogenic processes. They are known to be upregulated in regenerating muscle and in myoblast cultures but their function is unknown. Here, we show that the addition of recombinant Sfrp1 or Sfrp2 to C2C12 Cell Line cultures or to primary cultures of satellite Cells results in the inhibition of myotube formation with no significant effect on the Cell cycle or apoptosis. Even though at confluence, treated and untreated cultures are identical in appearance, analyses have shown that, for maximum effect, the Cells have to be treated while they are proliferating. Furthermore, removal of Sfrp from the culture medium during differentiation restores normal myotube formation. We conclude that Sfrp1 and Sfrp2 act to prevent myoblasts from entering the terminal differentiation process.
Feng Yang - One of the best experts on this subject based on the ideXlab platform.
-
Malat1 regulates serum response factor through miR-133 as a competing endogenous RNA in myogenesis
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2015Co-Authors: Xiaorui Han, Feng Yang, Huiqing Cao, Zicai LiangAbstract:Metastasis-associated lung adenocarcinoma transcript 1 (Malat1) is an example of a functional long noncoding RNA involved in many biologic processes. However, the mechanisms for Malat1 in myogenesis are unclear. Serum response factor (SRF) is a pivotal transcription factor for muscle proliferation and differentiation and is reported to be a target gene for muscle-specific microRNA-133 (miR-133). In this study, we initially found that silencing Malat1 in the mouse myoblast C2C12 Cell Line inhibited myocyte differentiation and decreased Srf at both the RNA and protein levels. Srf silencing decreased Malat1 expression as well. Further study revealed that Malat1 contained an miR-133 functional target site, and the interplay between Malat1 and Srf was miR-133 dependent. We demonstrated that Malat1 modulates Srf through miR-133 as a competing endogenous RNA and established a novel connection among Malat1, miR-133, and Srf in myoblast differentiation.
-
malat1 regulates serum response factor through mir 133 as a competing endogenous rna in myogenesis
The FASEB Journal, 2015Co-Authors: Feng Yang, Zicai LiangAbstract:Metastasis-associated lung adenocarcinoma transcript 1 (Malat1) is an example of a functional long noncoding RNA involved in many biologic processes. However, the mechanisms for Malat1 in myogenesis are unclear. Serum response factor (SRF) is a pivotal transcription factor for muscle proliferation and differentiation and is reported to be a target gene for muscle-specific microRNA-133 (miR-133). In this study, we initially found that silencing Malat1 in the mouse myoblast C2C12 Cell Line inhibited myocyte differentiation and decreased Srf at both the RNA and protein levels. Srf silencing decreased Malat1 expression as well. Further study revealed that Malat1 contained an miR-133 functional target site, and the interplay between Malat1 and Srf was miR-133 dependent. We demonstrated that Malat1 modulates Srf through miR-133 as a competing endogenous RNA and established a novel connection among Malat1, miR-133, and Srf in myoblast differentiation.—Han, X., Yang, F., Cao, H., Liang. Z. Malat1 regulates serum ...
Reza Meshkani - One of the best experts on this subject based on the ideXlab platform.
-
Leukocyte antigen-related inhibition attenuates palmitate-induced insulin resistance in muscle Cells
The Journal of endocrinology, 2012Co-Authors: Sattar Gorgani-firuzjaee, Salar Bakhtiyari, Abolfazl Golestani, Reza MeshkaniAbstract:Palmitate has been shown to induce insulin resistance in skeletal muscle Cells. The aim of this study was to investigate the role of the leukocyte common antigen-related (LAR) gene in palmitate-induced insulin resistance in C2C12 Cells. A stable C2C12 Cell Line was generated using LAR short hairpin RNA. The levels of LAR protein and phosphorylation of insulin receptor substrate-1 (IRS1) and Akt were detected by western blot analysis. 2-Deoxyglucose uptake was measured in LAR knockdown and control Cells using d-[2-(3)H]glucose. LAR protein level was decreased by 65% in the stable Cell Line compared with the control Cells. Palmitate (0.5 mM) significantly induced LAR mRNA (65%) and protein levels (40%) in myotubes compared with untreated Cells. Palmitate significantly reduced insulin-stimulated glucose uptake in both the control and LAR knockdown Cells by 33 and 51% respectively. However, LAR depletion improved insulin-stimulated glucose uptake in myotubes treated with palmitate. Furthermore, the inhibition of LAR prevented palmitate-induced decreases in phosphorylation of IRS1(Tyr632) and Akt(Ser473) in C2C12 Cells. In conclusion, these results reveal that palmitate induces LAR expression in C2C12 Cells. We also provided evidence that the inhibition of LAR attenuates palmitate-induced insulin resistance in myotubes.
-
Protein Tyrosine Phosphatase-1B (PTP-1B) Knockdown Improves Palmitate-Induced Insulin Resistance in C2C12 Skeletal Muscle Cells
Lipids, 2010Co-Authors: Salar Bakhtiyari, Reza Meshkani, Mohammad Taghikhani, Bagher Larijani, Khosrow AdeliAbstract:Insulin resistance is the central defect in type 2 diabetes and obesity. During the development of insulin resistance a lipid accumulation is accompanied by increased PTP-1B expression in the muscle. The aim of this study was to examine the effects of PTP-1B knockdown on insulin signaling and insulin resistance in the presence or absence of palmitate in C2C12 skeletal muscle Cells. A stable C2C12 Cell Line was established using short hairpin RNA (shRNA) to knockdown protein expression of PTP1B. Analysis of PTP-1B protein expression and phosphorylation and protein levels of IRS-1 and Akt were detected by western blot. The effects of PTP-1B knockdown on the glucose uptake was also measured in C2C12 Cells. The stable C2C12 Cell Line harboring the PTP-1B shRNA showed 62% decrease in the PTP-1B protein levels. 0.5 mM palmitate significantly induced insulin resistance in both control (26%) and PTP-1B knockdown Cells (16.5%) compared to the untreated Cells. Under treatment with palmitate, insulin stimulated phosphorylation of IRS-1 (Tyr632) and Akt (Ser473) in knockdown Cells was significantly 1.55- and 1.86-fold, respectively, greater than the controls. In the presence of palmitate, insulin dependent glucose uptake was significantly about 3-fold higher in PTP-1B knockdown stable C2C12 Cells compared to the control Cells. Our data showed that decreasing the PTP-1B protein level by shRNA can enhance the activity of important elements of insulin signaling. The improvement in insulin action persisted even in palmitate treated insulin resistant myotubes.
-
Protein Tyrosine Phosphatase‐1B (PTP‐1B) Knockdown Improves Palmitate‐Induced Insulin Resistance in C2C12 Skeletal Muscle Cells
Lipids, 2010Co-Authors: Salar Bakhtiyari, Reza Meshkani, Mohammad Taghikhani, Bagher Larijani, Khosrow AdeliAbstract:Insulin resistance is the central defect in type 2 diabetes and obesity. During the development of insulin resistance a lipid accumulation is accompanied by increased PTP-1B expression in the muscle. The aim of this study was to examine the effects of PTP-1B knockdown on insulin signaling and insulin resistance in the presence or absence of palmitate in C2C12 skeletal muscle Cells. A stable C2C12 Cell Line was established using short hairpin RNA (shRNA) to knockdown protein expression of PTP1B. Analysis of PTP-1B protein expression and phosphorylation and protein levels of IRS-1 and Akt were detected by western blot. The effects of PTP-1B knockdown on the glucose uptake was also measured in C2C12 Cells. The stable C2C12 Cell Line harboring the PTP-1B shRNA showed 62% decrease in the PTP-1B protein levels. 0.5 mM palmitate significantly induced insulin resistance in both control (26%) and PTP-1B knockdown Cells (16.5%) compared to the untreated Cells. Under treatment with palmitate, insulin stimulated phosphorylation of IRS-1 (Tyr632) and Akt (Ser473) in knockdown Cells was significantly 1.55- and 1.86-fold, respectively, greater than the controls. In the presence of palmitate, insulin dependent glucose uptake was significantly about 3-fold higher in PTP-1B knockdown stable C2C12 Cells compared to the control Cells. Our data showed that decreasing the PTP-1B protein level by shRNA can enhance the activity of important elements of insulin signaling. The improvement in insulin action persisted even in palmitate treated insulin resistant myotubes.
