Stimulation of Myogenic Differentiation by a Neuregulin, Glial Growth Factor 2

Florini, James R.; Samuel, Derina S.; Ewton, Daina Z.; Kirk, Cassandra; Sklar, R.

doi:10.1074/jbc.271.22.12699

Cited by 61 publications

(34 citation statements)

References 31 publications

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“…6B). An enhanced rate of cell fusion induced by neuregulins is in agreement with previous reports in other muscle cell lines (29,30). Chronic HRG caused an enhanced expression of myosin heavy chain (MHC, Fig.…”

Section: Chronic Incubation With Heregulin Stimulates Glucose Transposupporting

confidence: 81%

“…Neuregulins also affect the biology of skeletal muscle; they are potent activators of the expression of acetylcholine receptors (26 -28). In addition, the neuregulins GGF2 and NRG␣1 activate myogenic differentiation (29,30). There is also evidence for the operation of a neuregulin-ErbB3 autocrine signaling pathway during an early stage of myoblast differentiation (30).…”

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confidence: 99%

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A Novel Role of Neuregulin in Skeletal Muscle

Suárez¹,

Bach²,

Cadefau

et al. 2001

Journal of Biological Chemistry

100

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Neuregulins regulate the expression of acetylcholine receptor genes and induce development of the neuromuscular junction in muscle. In studying whether neuregulins regulate glucose uptake in muscle, we analyzed the effect of a recombinant neuregulin, r heregulin-␤1-(177-244) (HRG), on L6E9 muscle cells, which express the neuregulin receptors ErbB2 and ErbB3. L6E9 responded acutely to HRG by a time-and concentrationdependent stimulation of 2-deoxyglucose uptake. HRGinduced stimulation of glucose transport was additive to the effect of insulin. The acute stimulation of the glucose transport induced by HRG was a consequence of the translocation of GLUT4, GLUT1, and GLUT3 glucose carriers to the cell surface. The effect of HRG on glucose transport was dependent on phosphatidylinositol 3-kinase activity. HRG also stimulated glucose transport in the incubated soleus muscle and was additive to the effect of insulin. Chronic exposure of L6E9 cells to HRG potentiated myogenic differentiation, and under these conditions, glucose transport was also stimulated. The activation of glucose transport after chronic HRG exposure was due to enhanced cell content of GLUT1 and GLUT3 and to increased abundance of these carriers at the plasma membrane. However, under these conditions, GLUT4 expression was markedly down-regulated. Muscle denervation is associated with GLUT1 induction and GLUT4 repression. In this connection, muscle denervation caused a marked increase in the content of ErbB2 and ErbB3 receptors, which occurred in the absence of alterations in neuregulin mRNA levels. This fact suggests that neuregulins regulate glucose transporter expression in denervated muscle. We conclude that neuregulins regulate glucose uptake in L6E9 muscle cells by mechanisms involving the recruitment of glucose transporters to the cell surface and modulation of their expression. Neuregulins may also participate in the adaptations in glucose transport that take place in the muscle fiber after denervation.

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Section: Chronic Incubation With Heregulin Stimulates Glucose Transposupporting

confidence: 81%

mentioning

confidence: 99%

A Novel Role of Neuregulin in Skeletal Muscle

Suárez¹,

Bach²,

Cadefau

et al. 2001

Journal of Biological Chemistry

100

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“…Inhibition of myogenin expression by antisense oligonucleotides blocked the myogenic effect of IGF-I in myoblasts (46). Our work indicates a correlation between the expression of myogenin and the activity of PI3-K (Figs.…”

Section: Discussionmentioning

confidence: 54%

Phosphoinositide 3-Kinase Induces the Transcriptional Activity of MEF2 Proteins during Muscle Differentiation

Tamir

Bengal

2000

Journal of Biological Chemistry

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The activity of phosphoinositide 3-kinase (PI3-K) is essential for the differentiation of skeletal muscle cells by largely unknown mechanisms. Here we show that inhibition of PI3-K activity by the pharmacological agent LY294002 affects early processes of myoblast differentiation including the transcriptional activation of myogenin. Previous studies indicated that transcription of myogenin was dependent on MyoD and MEF2 proteins. We find that expression of a dominant negative form of PI3-K or growth in the presence of LY294002 inhibits cellular activity of MEF2 but not of MyoD. Evidence reveals that whereas MEF2 transcriptional activity is inhibited, its DNA binding activity remains unaffected. Recent studies demonstrated that phosphorylation by p38 mitogen-activated protein kinase (MAPK) induced transcriptional activity of MEF2 proteins. We show that the phosphorylation of MEF2 occurring during muscle differentiation is prevented if the activity of PI3-K is inhibited. However, our results also indicate that p38 MAPK is not affected by PI3-K in muscle cells. Nevertheless, p38 MAPK can substitute for PI3-K in the induction of MEF2 and muscle transcription. Together, these findings indicate that PI3-K affects skeletal muscle differentiation by inducing phosphorylation and transcriptional activity of MEF2 proteins in a parallel but distinct route from p38 MAPK.

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“…14). Antisense oligonucleotides to myogenin mRNA blocked IGF-I-mediated stimulation of myogenic differentiation but had no effect on stimulation of proliferation, suggesting that IGF-I activates multiple signal transduction pathways in myoblasts and that myogenin is an essential intermediate only in the differentiation pathway (15). Paradoxically, Brown et al (16) and Rosen et aL (11) have shown that the increase in IGF-II mRNA levels upon withdrawal of serum occurred after activation of the myogenin gene.…”

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confidence: 99%

“…Approximately 106 cells were cotransfected with 15 ,tg of a plasmid containing the mouse MyoD or myogenin cDNAs under the control of the mouse sarcoma virus long terminal repeat, together with 1.5 ,gg of pSV2neo. The DNA was removed 24 h later with the addition of fresh growth medium.…”

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confidence: 99%