Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases

Bennett, Anton M.; Tonks, Nicholas K.

doi:10.1126/science.278.5341.1288

Cited by 342 publications

(304 citation statements)

References 22 publications

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“…62 In nonleukemic cells, several groups have demonstrated that MAPK signaling can both promote and inhibit adipogenesis and myogenesis in pre-adipocytes and myoblasts, respectively, in a time and context-dependent manner. [63][64][65][66] Thus in some established cell systems, constitutive elevation of MAP kinase activity can stimulate proliferation, whereas in others it triggers increased p21 Cip-1/MDA6/WAF1 levels, cell cycle arrest, and cellular maturation. In contrast, in other cell types, prolonged inhibition of the MAP kinase pathway may also promote maturation and lead to increased p21 Cip-1/MDA6/WAF1 expression.…”

Section: An Overview For the Role Of The Map Kinase Pathway In Prolifmentioning

confidence: 99%

“…For example, inhibition of the PKC function by sphingosine or by specific catalytic site inhibitors (eg staurosporine) potentiates neoplastic cell apotosis and the reduction in clonogenicity induced by cytotoxic lipids (eg ceramide), cytotoxic drugs (eg 1-␤-D-arabinofuranosylcytosine (ara-C)), and other stresses (eg ionizing radiation). 86,89,90 In addition, pretreatment of leukemic cells with PKC activators such as PMA, which also activate MAP kinase, 66 has the net effect of opposing leukemic cell apoptosis in response to drugs such as topoisomerase inhibitors. 91 The downstream target of PKC responsible for its cytoprotective effect is uncertain, but the MAP kinase pathway, which is known to be activated by PKC 60 represents a plausible candidate.…”

Section: The Potential Roles Of Protein Kinase C and Map Kinase Signamentioning

confidence: 99%

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The roles of signaling by the p42/p44 mitogen-activated protein (MAP) kinase pathway; a potential route to radio- and chemo-sensitization of tumor cells resulting in the induction of apoptosis and loss of clonogenicity

et al. 1998

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During the last 10 years, multiple signal transduction pathways within cells have been discovered. These pathways have been linked to the regulation of many diverse cellular events such as proliferation, senescence, differentiation and apoptosis. This review will focus upon the many roles of signaling by the p42/p44 mitogen-activated protein (MAP) kinase pathway. Recent evidence suggests that signaling by the MAP kinase pathway can both enhance proliferation by increased expression of molecules such as cyclin D1, but also cause growth arrest by increased expression of molecules such as the cyclin kinase inhibitor protein p21 Cip-1/MDA6/WAF1 . These differential effects on growth have been correlated to the amplitude and duration of the MAP kinase activity signal. Furthermore several laboratories are reporting data suggesting that inhibition of the MAP kinase pathway, as well as a family of upstream MAP kinase activators, the protein kinase C family, represent an important route to both radio-and chemo-sensitization of tumor cells. Herein, we describe the historical discovery and characterization of the MAP kinase pathway. In addition we describe potential mechanisms by which inhibition of protein kinase C, the MAP kinase pathway, and potentially of p21 Cip-1/MDA6/WAF1 expression, may alter the sensitivities of leukemic and carcinoma cells to cytotoxic insults, leading to increased apoptosis and loss of clonogenicity.

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Section: An Overview For the Role Of The Map Kinase Pathway In Prolifmentioning

confidence: 99%

Section: The Potential Roles Of Protein Kinase C and Map Kinase Signamentioning

confidence: 99%

The roles of signaling by the p42/p44 mitogen-activated protein (MAP) kinase pathway; a potential route to radio- and chemo-sensitization of tumor cells resulting in the induction of apoptosis and loss of clonogenicity

et al. 1998

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“…They are important molecules in signalling cascades involved in cell differentiation, proliferation and cell death [20][21][22], and are activated through phosphorylation of tyrosine/threonine residues in signal transduction cascades. Once a MAPK is activated, transcription factors, RNA-binding proteins and other kinases may be phosphorylated, initiating events such as gene expression and post-translational protein modifications.…”

Section: Introductionmentioning

confidence: 99%

Porphyromonas gingivalis induces RANKL in bone marrow stromal cells: Involvement of the p38 MAPK

Reddi

Brown

Belibasakis

2011

Microbial Pathogenesis

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Periodontitis is a bacterially-induced oral inflammatory disease that is characterised by tissue degradation and bone loss. Porphyromonas gingivalis is a gram negative bacterial species highly associated with the pathogenesis of chronic periodontitis. Receptor activator of nuclear factor-kB ligand (RANKL) induces bone resorption whilst osteoprotegerin (OPG) is a decoy receptor that blocks this process. Cyclooxygenase-2 (COX-2) is an enzyme responsible for the production of prostaglandin (PGE)(2,) which is a major inflammatory mediator of bone resorption. Mitogen-activated protein kinases (MAPK) are intracellular signalling molecules involved in various cell processes, including inflammation. This study aimed to investigate the effect of P. gingivalis on MAPKs and their involvement in the regulation of RANKL, OPG and COX-2 expression in bone marrow stromal cells. P. gingivalis challenge resulted in the phosphorylation of primarily the p38 MAPK. RANKL and COX-2 mRNA expressions were upregulated, whereas OPG was down-regulated by P. gingivalis. The p38 synthetic inhibitor SB203580 abolished the P. gingivalis-induced RANKL and COX-2 expression, but did not affect OPG. Collectively, these results suggest that the p38 MAPK pathway is involved in the induction of RANKL and COX-2 by P. gingivalis, providing further insights into the pathogenic mechanisms of periodontitis. AbstractPeriodontitis is a bacterially-induced oral inflammatory disease that is characterised by tissue degradation and bone loss. Porphyromonas gingivalis is a gram negative bacterial species highly associated with the pathogenesis of chronic periodontitis. Receptor activator of nuclear factor-kB ligand (RANKL) induces bone resorption whilst osteoprotegerin (OPG) is a decoy receptor that blocks this process. Cyclooxygenase-2 (COX-2) is an enzyme responsible for the production of prostaglandin (PGE) 2, which is a major inflammatory mediator of bone resorption. Mitogen-activated protein kinases (MAPK) are intracellular signalling molecules involved in various cell processes, including inflammation. This study aimed to investigate the effect of P. gingivalis on MAPKs and their involvement in the regulation of RANKL, OPG and COX-2 expression in bone marrow stromal cells. P. gingivalis challenge resulted in the phosphorylation of primarily the p38 MAPK. RANKL and COX-2 mRNA expressions were up-regulated, whereas OPG was down-regulated by P. gingivalis. The p38 synthetic inhibitor SB203580 abolished the P. gingivalis-induced RANKL and COX-2 expression, but did not affect OPG. Collectively, these results suggest that the p38 MAPK pathway is involved in the induction of RANKL and COX-2 by P. gingivalis, providing further insights into the pathogenic mechanisms of periodontitis. KeywordsPorphyromonas gingivalis, Bone marrow stromal cells, Receptor activator of nuclear factor-kB ligand, Osteoprotegerin, Cyclooxygenase -2, p38 MAPK.3

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“…5 And despite the potential for redundancy among the large repertoire of cellular phosphatases identified, MKP-1 knock-out (KO) mice exhibit heightened inflammation, autoimmunity and metabolic defects. 6,7 Clues from the literature also suggest MKP-1 activity is associated with cell injury. MKP-1 is a target of the pro-apoptotic transcription factors p53 and E2F-1, and accumulates following oxidant, hyperosmotic or hypoxic stress.…”

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confidence: 99%

MKP-1 antagonizes C/EBP β activity and lowers the apoptotic threshold after ischemic injury

et al. 2012

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The dual specificity phosphatase MAPK phosphatase-1 (MKP-1) feeds back on MAP kinase signaling to regulate metabolic, inflammatory and survival responses. MKP-1 is widely expressed in the central nervous system (CNS) and induced after ischemic stress, although its function in these contexts remains unclear. Here we report that MKP-1 activated several cell death factors, including BCL2 and adenovirus E1B 19 kDa interacting protein 3, and caspases 3 and 12 culminating in apoptotic cell death in vitro. MKP-1 also exerted inhibitory effects on the bZIP transcription factor CCAAT/enhancer-binding protein (C/EBPb), previously shown to have neuroprotective properties. These effects included reduced expression of the full-length C/EBPb variant and hypo-phosphorylation at the MEK-ERK1/2-sensitive Thr 188 site. Notably, enforced expression C/EBPb rescued cells from MKP-1-induced toxicity. Studies performed in knock-out mice indicate that the MKP-1 activity is required to exclude C/EBPb from the nucleus basally, and that MKP-1 antagonizes C/EBPb expression after global forebrain ischemia, particularly within the vulnerable CA1 sector of the hippocampus. Overall, MKP-1 appears to lower the cellular apoptotic threshold by inhibiting C/EBPb and enhancing both BH3 protein expression and cellular caspase activity. Thus, although manipulation of the MKP-1-C/EBPb axis could have therapeutic value in ischemic disorders, our observations using MKP-1 catalytic mutants suggest that approaches geared towards inhibiting MKP-1's phosphatase activity alone may be ineffective.

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Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases

Cited by 342 publications

References 22 publications

The roles of signaling by the p42/p44 mitogen-activated protein (MAP) kinase pathway; a potential route to radio- and chemo-sensitization of tumor cells resulting in the induction of apoptosis and loss of clonogenicity

The roles of signaling by the p42/p44 mitogen-activated protein (MAP) kinase pathway; a potential route to radio- and chemo-sensitization of tumor cells resulting in the induction of apoptosis and loss of clonogenicity

Porphyromonas gingivalis induces RANKL in bone marrow stromal cells: Involvement of the p38 MAPK

MKP-1 antagonizes C/EBP β activity and lowers the apoptotic threshold after ischemic injury

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