Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase

Li, Yingqiu; Jiang, Bing-Hua; Ensign, Wayne; Vogt, Peter K.; Han, Jiahuai

doi:10.1016/s0898-6568(00)00120-0

Cited by 103 publications

(84 citation statements)

References 40 publications

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“…These observations suggest an important role of endocytosis induced by the T␤RII-p38 MAPK signaling pathway in activating endothelial proliferation and reducing endothelial apoptosis. Our results are in agreement with studies showing that p38 MAPK activation is a crucial determinant of cell proliferation (6,13).…”

Section: Discussionsupporting

confidence: 93%

p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity

Siddiqui¹,

Siddiqui²,

Uddin³

et al. 2007

American Journal of Physiology-Lung Cellular and Molecular Phys

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We show in rat lung microvessel endothelial cells (RLMVEC) that endocytosis is a critical determinant of activation of mitogen-activated protein kinase (MAPK) and thereby regulates endothelial monolayer integrity. In RLMVEC grown in serum-free medium, we observed that albumin supplementation induced the phosphorylation of p38 MAPK within 30 min, which persisted for up to 2 h. Engagement of the endocytic machinery regulated the activation of p38 MAPK that contributed to endothelial cell proliferation and reduction of apoptosis. We also observed an interaction between the caveolar protein caveolin-1 and p38 MAPK with reciprocal coimmunoprecipitation assays and colocalization using double-label immunofluorescence staining. Knockdown of caveolin-1 expression with small interfering RNA significantly reduced endocytosis and activation of p38 MAPK and interfered with the ability of endothelial cells to form a confluent monolayer. Thus caveolae-mediated endocytosis and concomitant activation of p38 MAPK may help to maintain endothelial monolayer integrity by signaling proliferation and survival of endothelial cells.

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Section: Discussionsupporting

confidence: 93%

p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity

Siddiqui¹,

Siddiqui²,

Uddin³

et al. 2007

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…For example, ADAM12 cell signaling may positively influence myogenesis, because membrane-bound ADAM12 activates phosphatidylinositol (PI) 3-kinase by mediating its recruitment to the membrane , active PI 3-kinase being crucially involved in terminal differentiation of myogenic cells (Jiang et al, 1998;Li et al, 2000). Moreover, the ADAM12 cytoplasmic tail binds ␣-actinin 1 and 2 (Galliano et al, 2000;Cao et al, 2001), this binding being required for full-blown fusion of C2C12 myogenic cells (Galliano et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Lafuste

Sonnet

Chazaud

et al. 2005

MBoC

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Knowledge on molecular systems involved in myogenic precursor cell (mpc) fusion into myotubes is fragmentary. Previous studies have implicated the a disintegrin and metalloproteinase (ADAM) family in most mammalian cell fusion processes. ADAM12 is likely involved in fusion of murine mpc and human rhabdomyosarcoma cells, but it requires yet unknown molecular partners to launch myogenic cell fusion. ADAM12 was shown able to mediate cell-to-cell attachment through binding ␣ 9 ␤ 1 integrin. We report that normal human mpc express both ADAM12 and ␣ 9 ␤ 1 integrin during their differentiation. Expression of ␣ 9 parallels that of ADAM12 and culminates at time of fusion. ␣ 9 and ADAM12 coimmunoprecipitate and participate to mpc adhesion. Inhibition of ADAM12/␣ 9 ␤ 1 integrin interplay, by either ADAM12 antisense oligonucleotides or blocking antibody to ␣ 9 ␤ 1 , inhibited overall mpc fusion by 47-48%, with combination of both strategies increasing inhibition up to 62%. By contrast with blockade of vascular cell adhesion molecule-1/␣ 4 ␤ 1 , which also reduced fusion, exposure to ADAM12 antisense oligonucleotides or anti-␣ 9 ␤ 1 antibody did not induce detachment of mpc from extracellular matrix, suggesting specific involvement of ADAM12-␣ 9 ␤ 1 interaction in the fusion process. Evaluation of the fusion rate with regard to the size of myotubes showed that both ADAM12 antisense oligonucleotides and ␣ 9 ␤ 1 blockade inhibited more importantly formation of large (>5 nuclei) myotubes than that of small (2-4 nuclei) myotubes. We conclude that both ADAM12 and ␣ 9 ␤ 1 integrin are expressed during postnatal human myogenic differentiation and that their interaction is mainly operative in nascent myotube growth. INTRODUCTIONAdult skeletal muscle regeneration after injury results from activation, proliferation, and fusion of mononucleated myogenic precursor cells (mpc) (Hawke and Garry, 2001). The mpc fusion results from an ordered sequence of events, including clustering and alignment of cells, establishment of close cell-to-cell contacts, and plasma membrane merging (Doberstein et al., 1997;Taylor, 2003). Various membrane proteins have been implicated in myotube formation, including N-and M-cadherins, neural cell adhesion molecule (NCAM), and vascular cell adhesion molecule (VCAM), ␣ 4 ␤ 1 and other integrins, and a disintegrin and metalloproteinases (ADAMs) (Abmayr et al., 2003). ADAMs form a family of Ͼ30 transmembrane glycoproteins with a unique domain organization, including a prodomain, a proteolytic domain (metalloprotease), an adhesion integrin-binding site formed by both disintegrin and cysteine-rich domains, an epidermal growth factor-like domain, a transmembrane domain, and a signaling cytoplasmic tail (Huovila et al., 1996;Primakoff and Myles, 2002;White, 2003). In addition, some ADAMs contain a hydrophobic sequence in a cysteine-rich region that may represent a fusion peptide, suggesting that this subclass of ADAMs might participate to plasma membrane merging (Huovila et al., 1996). Some ADAMs have been implicated i...

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“…on April 7, 2019 by guest http://mcb.asm.org/ shown to be crucial for myogenesis (5,9,10,32,44,62,66). Both inactivation and hyperactivation of Cdc42 or Rac-1 result in inhibition of myogenesis (reference 36 and references therein), pointing to a complex regulation of myogenic differentiation and a delicate equilibrium between promyogenic and antimyogenic signaling pathways.…”

Section: Vol 24 2004 Rage Engagement Stimulates Myogenesis 4891mentioning

confidence: 99%

“…However, IGF I and IGF II were reported to promote or inhibit myogenic differentiation depending on the absence or presence of TNF-␣, respectively (16), and down-regulation of nerve growth factor low-affinity receptor was shown to be required for myoblast terminal differentiation (12). Signaling pathways implicated in the transduction of the effects of these agents acting on myoblasts include (i) the mitogen-activated protein (MAP) kinase (MAPK) p38 and Akt, the activation of which is required for myogenesis (5,9,10,17,32,44,55,57,62,66); (ii) an NF-B-dependent pathway activated by cytokines such as TNF-␣, which interferes with myogenesis (30); (iii) a PW1-dependent, NF-Bindependent activation of caspases in the absence of apoptosis (8); (iv) the Ras-MEK-extracellular signal-regulated kinase (ERK) pathway, which suppresses myogenesis (4,42,43,61) but is required at a later stage of muscle differentiation (4); and (v) activation of inducible nitric oxide synthase via NF-B, which results in stimulation of myogenesis (25).Recently, we found that S100B, a member of a multigenic family of Ca 2ϩ -modulated proteins of the EF-hand type with both intracellular and extracellular regulatory activities (11,19), inhibited myoblast differentiation and myotube formation when administered to the rat myoblast cell line L6 (51). Inhibition of myogenesis was registered at picomolar doses of S100B and was reversible, pointing to S100B binding to a cell surface receptor with a relatively high affinity.…”

mentioning

confidence: 99%

Amphoterin Stimulates Myogenesis and Counteracts the Antimyogenic Factors Basic Fibroblast Growth Factor and S100B via RAGE Binding

Sorci

Riuzzi

Arcuri

et al. 2004

Molecular and Cellular Biology

115

136

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The receptor for advanced glycation end products (RAGE), a multiligand receptor of the immunoglobulin superfamily, has been implicated in the inflammatory response, diabetic angiopathy and neuropathy, neurodegeneration, cell migration, tumor growth, neuroprotection, and neuronal differentiation. We show here that (i) RAGE is expressed in skeletal muscle tissue and its expression is developmentally regulated and (ii) RAGE engagement by amphoterin (HMGB1), a RAGE ligand, in rat L6 myoblasts results in stimulation of myogenic differentiation via activation of p38 mitogen-activated protein kinase (MAPK), up-regulation of myogenin and myosin heavy chain expression, and induction of muscle creatine kinase. No such effects were detected in myoblasts transfected with a RAGE mutant lacking the transducing domain or myoblasts transfected with a constitutively inactive form of the p38 MAPK upstream kinase, MAPK kinase 6, Cdc42, or Rac-1. Moreover, amphoterin counteracted the antimyogenic activity of the Ca 2؉ -modulated protein S100B, which was reported to inhibit myogenic differentiation via inactivation of p38 MAPK, and basic fibroblast growth factor (bFGF), a known inhibitor of myogenic differentiation, in a manner that was inversely related to the S100B or bFGF concentration and directly related to the extent of RAGE expression. These data suggest that RAGE and amphoterin might play an important role in myogenesis, accelerating myogenic differentiation via Cdc42-Rac-1-MAPK kinase 6-p38 MAPK.Myogenesis is a multistep process in which myoblasts cease to proliferate, express genes responsible for differentiation, and fuse into multinucleated cells, the myotubes, which finally build up the myofibrils (1,2,18,31,33,39,59). Several extracellular factors have been identified that participate in the regulation of myogenesis, some of which promote myoblast differentiation and/or myotube formation, while other factors inhibit these processes. Insulin, insulin-like growth factors (IGF I and IGF II), neuregulin, and nerve growth factor belong to the first category of agents (13-15, 28, 45), while tumor necrosis factor alpha (TNF-␣), basic fibroblast growth factor (bFGF), and transforming growth factor ␤ belong to the second category (12,29,30,35,37,40,42,50,56). However, IGF I and IGF II were reported to promote or inhibit myogenic differentiation depending on the absence or presence of TNF-␣, respectively (16), and down-regulation of nerve growth factor low-affinity receptor was shown to be required for myoblast terminal differentiation (12). Signaling pathways implicated in the transduction of the effects of these agents acting on myoblasts include (i) the mitogen-activated protein (MAP) kinase (MAPK) p38 and Akt, the activation of which is required for myogenesis (5,9,10,17,32,44,55,57,62,66); (ii) an NF-B-dependent pathway activated by cytokines such as TNF-␣, which interferes with myogenesis (30); (iii) a PW1-dependent, NF-Bindependent activation of caspases in the absence of apoptosis (8); (iv) the Ras-MEK-extracellular sign...

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Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase

Cited by 103 publications

References 40 publications

p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity

p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Amphoterin Stimulates Myogenesis and Counteracts the Antimyogenic Factors Basic Fibroblast Growth Factor and S100B via RAGE Binding

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Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase

Cited by 103 publications

References 40 publications

p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity

p38 MAPK activation coupled to endocytosis is a determinant of endothelial monolayer integrity

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

Amphoterin Stimulates Myogenesis and Counteracts the Antimyogenic Factors Basic Fibroblast Growth Factor and S100B via RAGE Binding

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ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation