Role of estrogen receptors, PKC and Src in ERK2 and p38 MAPK signaling triggered by 17β-estradiol in skeletal muscle cells

2010 ◽  
Vol 122 (4) ◽  
pp. 287-294 ◽  
Author(s):  
Ana C. Ronda ◽  
Claudia Buitrago ◽  
Ricardo Boland
Keyword(s):  
Skeletal Muscle ◽  
Estrogen Receptors ◽  
P38 Mapk ◽  
Muscle Cells ◽  
Mapk Signaling ◽  
Skeletal Muscle Cells ◽  
17Β Estradiol

scholarly journals Extracellular-regulated kinase and p38 mitogen-activated protein kinases are involved in the antiapoptotic action of 17β-estradiol in skeletal muscle cells

2010 ◽  
Vol 206 (2) ◽  
pp. 235-246 ◽  
Author(s):  
Ana Carolina Ronda ◽  
Andrea Vasconsuelo ◽  
Ricardo Boland
Keyword(s):  
Skeletal Muscle ◽  
P38 Mapk ◽  
Muscle Cells ◽  
C2c12 Cells ◽  
Skeletal Muscle Cells ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
17Β Estradiol ◽  
Mapk Inhibitors ◽  
Extracellular Regulated Kinase

17β-Estradiol (E2) stimulates the mitogen-activated protein kinases (MAPKs) in various cellular types. We have shown that the hormone activates extracellular-regulated kinase (ERK) and p38 MAPK in skeletal muscle cells. However, the functions of MAPK modulation by the estrogen in muscle cells have not been studied yet. We have recently reported antiapoptotic actions of E2 in C2C12 cells. Here, the role of MAPKs mediating the hormone effect in muscle cells was investigated. The results showed that cells exposed to 0.5 mM hydrogen peroxide (H2O2) presented cytoskeleton disorganization, mitochondrial redistribution, and picnotic/fragmented nuclei. Pretreatment with 10−8 M E2 prevented these morphological apoptotic characteristics, except in the presence of ERK or p38 MAPK inhibitors, U0126 and SB203580 respectively. Mitochondrial membrane integrity was also studied. Preincubation of cultures with 10−8 M E2 abrogated H2O2 effects such as Janus Green oxidation, presence of cytochrome c oxidase activity in the cytoplasm, and SMAC/DIABLO release from mitochondria. When MAPKs were inhibited, the hormone could not prevent mitochondrial membrane damage exerted by oxidative stress. Blocking experiments with small interfering RNAs confirmed that both ERK and p38 MAPKs mediate the antiapoptotic effects of the hormone at the mitochondrial level. Further, some of the molecular mechanisms involved were also investigated. Thus, E2 was able to induce AKT (Ser473) and BAD (Ser112) phosphorylation in C2C12 cells in the absence or in the presence of H2O2 but not when the cultures were incubated with H2O2 and MAPK inhibitors. Altogether, these results show that E2 exerts a survival action in skeletal muscle cells involving ERK and p38 MAPK activation.

17β-Estradiol signaling in skeletal muscle cells and its relationship to apoptosis

Steroids ◽  
2008 ◽  
Vol 73 (9-10) ◽  
pp. 859-863 ◽  
Author(s):  
R BOLAND ◽  
A VASCONSUELO ◽  
L MILANESI ◽  
A RONDA ◽  
A DEBOLAND
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
17Β Estradiol

scholarly journals Zinc Modulates Several Transcription-Factor Regulated Pathways in Mouse Skeletal Muscle Cells

Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 5098
Author(s):  
Parisa Vahidi Ferdowsi ◽  
Rachel Ng ◽  
John Adulcikas ◽  
Sukhwinder Singh Sohal ◽  
Stephen Myers
Keyword(s):  
Skeletal Muscle ◽  
Transcription Factor ◽  
Metal Ion ◽  
Insulin Signalling ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Western Blots ◽  
Insulin Signalling Pathway ◽  
C2c12 Skeletal Muscle Cells

Zinc is an essential metal ion involved in many biological processes. Studies have shown that zinc can activate several molecules in the insulin signalling pathway and the concomitant uptake of glucose in skeletal muscle cells. However, there is limited information on other potential pathways that zinc can activate in skeletal muscle. Accordingly, this study aimed to identify other zinc-activating pathways in skeletal muscle cells to further delineate the role of this metal ion in cellular processes. Mouse C2C12 skeletal muscle cells were treated with insulin (10 nM), zinc (20 µM), and the zinc chelator TPEN (various concentrations) over 60 min. Western blots were performed for the zinc-activation of pAkt, pErk, and pCreb. A Cignal 45-Reporter Array that targets 45 signalling pathways was utilised to test the ability of zinc to activate pathways that have not yet been described. Zinc and insulin activated pAkt over 60 min as expected. Moreover, the treatment of C2C12 skeletal muscle cells with TPEN reduced the ability of zinc to activate pAkt and pErk. Zinc also activated several associated novel transcription factor pathways including Nrf1/Nrf2, ATF6, CREB, EGR1, STAT1, AP-1, PPAR, and TCF/LEF, and pCREB protein over 120 min of zinc treatment. These studies have shown that zinc’s activity extends beyond that of insulin signalling and plays a role in modulating novel transcription factor activated pathways. Further studies to determine the exact role of zinc in the activation of transcription factor pathways will provide novel insights into this metal ion actions.

scholarly journals 17β-Estradiol abrogates apoptosis in murine skeletal muscle cells through estrogen receptors: role of the phosphatidylinositol 3-kinase/Akt pathway

2007 ◽  
Vol 196 (2) ◽  
pp. 385-397 ◽  
Author(s):  
Andrea Vasconsuelo ◽  
Lorena Milanesi ◽  
Ricardo Boland
Keyword(s):  
Skeletal Muscle ◽  
Protective Action ◽  
Muscle Cells ◽  
Cellular Systems ◽  
C2c12 Cells ◽  
Skeletal Muscle Cells ◽  
Akt Pathway ◽  
Akt Activation ◽  
17Β Estradiol ◽  
Murine Skeletal Muscle

Estrogens can regulate apoptosis in various cellular systems. The present study shows that 17β-estradiol (E2), at physiological concentrations, abrogates DNA damage, poly (ADP-ribose) polymerase cleavage, and mitochondrial cytochrome c release induced by H2O2 or etoposide in mouse skeletal muscle C2C12 cells. This protective action, which involved PI3K/Akt activation and Bcl-2 associated death agonist (BAD) phosphorylation, was inhibited by antibodies against the estrogen receptor (ER) α or β isoforms, or transfecting siRNA specific for each isoform. The inhibition of the antiapoptotic action of E2 at the mitochondrial level was more pronounced when ER-β was immunoneutralized or suppressed by mRNA silencing, whereas transfection of C2C12 cells with either ER-α siRNA or ER-β siRNA blocked the activation of Akt by E2, suggesting differential involvement of ER isoforms depending on the step of the apoptotic/survival pathway evaluated. These results indicate that E2 exerts antiapoptotic effects in skeletal muscle cells which are mediated by ER-β and ER-α and involve the PI3K/Akt pathway.

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