FGF21 expression and release in muscle cells: involvement of MyoD and regulation by mitochondria-driven signalling

2014 ◽  
Vol 463 (2) ◽  
pp. 191-199 ◽  
Author(s):  
Francesc Ribas ◽  
Joan Villarroya ◽  
Elayne Hondares ◽  
Marta Giralt ◽  
Francesc Villarroya
Keyword(s):  
P38 Mapk ◽  
Gene Transcription ◽  
Muscle Cells ◽  
Ros Production ◽  
Myogenic Factor ◽  
Subsequent Activation ◽  
Fgf21 Expression

FGF21 gene transcription in muscle cells is controlled by the myogenic factor MyoD. In muscle cells, FGF21 expression and release is induced by dysfunctional mitochondria signalling via enhanced ROS production and subsequent activation of p38 MAPK.

scholarly journals 17β-estradiol down-regulates lipopolysaccharide-induced MCP-1 production and cell migration in vascular smooth muscle cells

2010 ◽  
Vol 45 (2) ◽  
pp. 87-97 ◽  
Author(s):  
Ping Jiang ◽  
Jinwen Xu ◽  
Shuhui Zheng ◽  
Jinghe Huang ◽  
Qiuling Xiang ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
P38 Mapk ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Pyrrolidine Dithiocarbamate ◽  
17Β Estradiol ◽  
Anti Inflammatory

Atherosclerosis is an inflammatory disease where lipopolysaccharide (LPS) triggers the release of inflammatory cytokines that accelerate its initiation and progression. Estrogen has been proven to be vasoprotective against atherosclerosis; however, the anti-inflammatory function of estrogen in the vascular system remains obscure. In this study, we investigated the effect of estrogen on LPS-induced monocyte chemoattractant protein-1 (MCP-1; listed as CCL2 in the MGI database) production in vascular smooth muscle cells (VSMCs). LPS significantly enhances MCP-1 production and this is dependent on nuclear factor κ B (NFκB) signaling, since the use of NFκB inhibitor pyrrolidine dithiocarbamate or the silencing of NFκB subunit p65 expression with specific siRNA largely impairs LPS-enhanced MCP-1 production. On the contrary, 17β-estradiol (E2) inhibits LPS-induced MCP-1 production in a time- and dose-dependent manner, which is related to the suppression of p65 translocation to nucleus. Furthermore, p38 MAPK is rapidly activated in response to LPS, while E2 markedly inhibits p38 MAPK activation. Transfection with p38 MAPK siRNA or the use of p38 MAPK inhibitor SB203580 markedly attenuates LPS-stimulated p65 translocation to nucleus and MCP-1 production, suggesting that E2 suppresses NFκB signaling by the inactivation of p38 MAPK signaling. LPS promotes VSMCs migration and this is abrogated by MCP-1 antibody, implying that MCP-1 may play a major role as an autocrine factor in atherosclerosis. In addition, E2 inhibits LPS-promoted cell migration by downregulation of MCP-1 production. Overall, our results demonstrate that E2 exerts anti-inflammatory property antagonistic to LPS in VSMCs by reducing MCP-1 production, and this effect is related to the inhibition of p38 MAPK/NFκB cascade.

Xenopus Myf-5 marks early muscle cells and can activate muscle genes ectopically in early embryos

Development ◽  
1991 ◽  
Vol 111 (2) ◽  
pp. 551-560 ◽  
Author(s):  
N.D. Hopwood ◽  
A. Pluck ◽  
J.B. Gurdon
Keyword(s):  
Ectopic Expression ◽  
Muscle Cells ◽  
Muscle Differentiation ◽  
Cardiac Actin ◽  
Early Embryos ◽  
Muscle Genes ◽  
Myogenic Factor ◽  
Somitic Mesoderm

We have cloned a Xenopus cDNA that encodes a homologue of the human myogenic factor, Myf-5. Xenopus Myf-5 (XMyf5) transcripts first accumulate in the prospective somite region of early gastrulae. The pattern of XMyf5 expression is similar to that of the Xenopus MyoD (XMyoD) gene, except that XMyf5 transcripts are largely restricted to posterior somitic mesoderm even before any somites have formed. Transient ectopic expression of XMyf5 activates cardiac actin and XMyoD genes in animal cap cells, but does not cause full myogenesis, even in combination with XMyoD. These results suggest that XMyf5 acts together with XMyoD as one of the set of genes regulating the earliest events of myogenesis, additional factors being required for complete muscle differentiation.

scholarly journals Koumine Promotes ROS Production to Suppress Hepatocellular Carcinoma Cell Proliferation Via NF-κB and ERK/p38 MAPK Signaling

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 559 ◽  
Author(s):  
Yuan ◽  
Liang ◽  
Yi ◽  
Chen ◽  
Li ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Proliferation ◽  
Membrane Potential ◽  
P38 Mapk ◽  
Developed Countries ◽  
Mapk Signaling ◽  
Dependent Manner ◽  
Ros Production ◽  
Mitochondria Membrane Potential ◽  
Hcc Cells

In the past decades, hepatocellular carcinoma (HCC) has been receiving increased attention due to rising morbidity and mortality in both developing and developed countries. Koumine, one of the significant alkaloidal constituents of Gelsemium elegans Benth., has been regarded as a promising anti-inflammation, anxiolytic, and analgesic agent, as well as an anti-tumor agent. In the present study, we attempted to provide a novel mechanism by which koumine suppresses HCC cell proliferation. We demonstrated that koumine might suppress the proliferation of HCC cells and promote apoptosis in HCC cells dose-dependently. Under koumine treatment, the mitochondria membrane potential was significantly decreased while reactive oxygen species (ROS) production was increased in HCC cells; in the meantime, the phosphorylation of ERK, p38, p65, and IκBα could all be inhibited by koumine treatment dose-dependently. More importantly, the effects of koumine upon mitochondria membrane potential, ROS production, and the phosphorylation of ERK, p38, p65, and IκBα could be significantly reversed by ROS inhibitor, indicating that koumine affects HCC cell fate and ERK/p38 MAPK and NF-κB signaling activity through producing excess ROS. In conclusion, koumine could inhibit the proliferation of HCC cells and promote apoptosis in HCC cells; NF-κB and ERK/p38 MAPK pathways could contribute to koumine functions in a ROS-dependent manner.

p21-activated kinase 1 participates in tracheal smooth muscle cell migration by signaling to p38 MAPK

2001 ◽  
Vol 281 (1) ◽  
pp. C123-C132 ◽  
Author(s):  
Melissa A. Dechert ◽  
Jennifer M. Holder ◽  
William T. Gerthoffer
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Smooth Muscle Cells ◽  
P38 Mapk ◽  
Mammalian Cells ◽  
Muscle Cells ◽  
Mitogen Activated Protein Kinase ◽  
Tracheal Smooth Muscle ◽  
Wild Type ◽  
P21 Activated Kinase

Cell migration contributes to many physiological processes and requires dynamic changes in the cytoskeleton. These migration-dependent cytoskeletal changes are partly mediated by p21-activated protein kinases (PAKs). At least four closely related isoforms, PAK1, PAK2, PAK3, and PAK4, exist in mammalian cells. In smooth muscle cells, little is known about the expression, activation, or ability of PAKs to regulate migration. Our study revealed the existence of three PAK isoforms in cultured tracheal smooth muscle cells (TSMCs). Additionally, we constructed adenoviral vectors encoding wild type and a catalytically inactive PAK1 mutant to investigate PAK activation and its role in TSMC migration. Stimulation of TSMCs with platelet-derived growth factor (PDGF) increased the activity of PAK1 over time. Overexpression of mutant PAK1 blocked PDGF-induced chemotactic cell migration. Phosphorylation of p38 mitogen-activated protein kinase (MAPK) in cells overexpressing wild-type PAK1 was similar to vector controls; however, p38 MAPK phosphorylation was severely reduced by overexpression of the PAK1 mutant. Collectively, these results suggest a role for PAK1 in chemotactic TSMC migration that involves catalytic activity and may require signaling to p38 MAPK among other pathways.

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