Anisomycin activates p38 MAP kinase to induce LTD in mouse primary visual cortex

Xiong, Wei; Kojic, Luba; Zhang, Lanjing; Prasad, Shiv S.; Douglas, Robert M.; Wang, Yu Tian; Cynader, Max S.

doi:10.1016/j.brainres.2006.02.015

Cited by 40 publications

(31 citation statements)

References 23 publications

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“…Our recent report showed that nanomolar A␤ was able to phosphorylate p38 MAPK in cultured cortical neurons at concentrations and incubation time comparable with those used for LTP inhibition (Origlia et al, 2008;Takuma et al, 2009). In the present paper, we reported that p38 MAPK phosphorylation is required for LTD in EC, in agreement with previous reports (Bolshakov et al, 2000;Rush et al, 2002;Huang et al, 2004;Xiong et al, 2006). Furthermore, we showed that p38 MAPK phosphorylation is also required for LTD impairment.…”

Section: Discussionsupporting

confidence: 92%

“…1 B). This result indicates that p38 MAPK, but not JNK, is required for LTD expression in the EC, which is in agreement with previous studies showing a role for p38MAK activation in both metabotropic glutamate receptor (mGluR)-dependent and NMDA-dependent LTD in the hippocampus (Bolshakov et al, 2000;Rush et al, 2002;Zhu et al, 2002;Huang et al, 2004;Hsieh et al, 2006) and neocortex (Xiong et al, 2006). Next, we examined the effect of JNK that is not involved in physiological mechanisms underlying LFS-LTD with the aim of preventing A␤-dependent LTD inhibition.…”

Section: A␤-induced Synaptic Depression and Ltd Inhibition Is Preventsupporting

confidence: 89%

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Microglial Receptor for Advanced Glycation End Product-Dependent Signal Pathway Drives β-Amyloid-Induced Synaptic Depression and Long-Term Depression Impairment in Entorhinal Cortex

Origlia

Bonadonna²,

Rosellini³

et al. 2010

J. Neurosci.

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Overproduction of ␤-amyloid (A␤) is a pathologic feature of Alzheimer's disease, leading to cognitive impairment. Here, we investigated the impact of cell-specific receptor for advanced glycation end products (RAGE) on A␤-induced entorhinal cortex (EC) synaptic dysfunction. We found both a transient depression of basal synaptic transmission and inhibition of long-term depression (LTD) after the application of A␤ in EC slices. Synaptic depression and LTD impairment induced by A␤ were rescued by functional suppression of RAGE. Remarkably, the rescue was only observed in slices from mice expressing a defective form of RAGE targeted to microglia, but not in slices from mice expressing defective RAGE targeted to neurons. Moreover, we found that the inflammatory cytokine IL-1␤ (interleukin-1␤) and stress-activated kinases [p38 MAPK (p38 mitogen-activated protein kinase) and JNK (c-Jun N-terminal kinase)] were significantly altered and involved in RAGE signaling pathways depending on RAGE expression in neuron or microglia. These findings suggest a prominent role of microglial RAGE signaling in A␤-induced EC synaptic dysfunction.

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Section: Discussionsupporting

confidence: 92%

Section: A␤-induced Synaptic Depression and Ltd Inhibition Is Preventsupporting

confidence: 89%

Microglial Receptor for Advanced Glycation End Product-Dependent Signal Pathway Drives β-Amyloid-Induced Synaptic Depression and Long-Term Depression Impairment in Entorhinal Cortex

Origlia

Bonadonna²,

Rosellini³

et al. 2010

J. Neurosci.

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“…In addition, PKC-␦ was implicated in the translocation of nSMase2 from the Golgi to the plasma membrane during such treatments (20,21). Here we show that treatments with either PMA or anisomycin, the respective stimulators of the "conventional" PKC(s) and p38 MAPK (22,23) elevate nSMase2 phosphorylation (Fig. 3).…”

Section: Resultssupporting

confidence: 54%

Neutral Sphingomyelinase 2 (nSMase2) Is a Phosphoprotein Regulated by Calcineurin (PP2B)

Filosto¹,

Fry²,

Knowlton

et al. 2010

Journal of Biological Chemistry

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We previously reported that exposure of human airway epithelial cells to oxidative stress increased ceramide generation via specific activation of neutral sphingomyelinase2 (nSMase2). Here we show that nSMase2 is a phosphoprotein exclusively phosphorylated at serine residues. The level of nSMase2 phosphorylation can be modulated by treatment with anisomycin or phorbol 12-myristate 13-acetate (PMA/12-O-tetradecanoylphorbol-13-acetate), suggesting that p38 mitogen-activated protein kinase (MAPK) and protein kinases Cs are upstream of nSMase2 phosphorylation. Oxidative stress enhances both the activity and phosphorylation of nSMase2. Strikingly, we show here that nSMase2 is bound directly by the phosphatase calcineurin (CaN), which acts as an on/off switch for nSMase2 phosphorylation in the presence or absence of oxidative stress. Specifically, CaN is being inhibited/degraded and therefore does not bind nSMase2 under oxidative stress, and a mutant nSMase2 that lacks the CaN binding site exhibits constitutively elevated phosphorylation and increased activity relative to wild type nSMase2. Importantly, the phosphorylation and activity of the mutant no longer responds to oxidative stress, confirming that CaN is the critical link that allows oxidative stress to modulate nSMase2 phosphorylation and function.We have shown that ceramide generation coordinates stress responses and is elevated in HAE cells in response to reactive oxygen species (1-8).Ceramide is synthesized through either a de novo pathway involving serine palmitoyl-CoA transferase and ceramide synthase, or from breakdown of membrane sphingomyelin (N-acylsphingosine-1-phosphocholine) (Fig. 1A), a phospholipid preferentially concentrated in the plasma membrane of mammalian cells (9). Sphingomyelin catabolism occurs via the action of sphingomyelinases (SMases), 3 which are sphingomyelin-specific forms of phospholipase C that hydrolyze the phosphodiester bond of sphingomyelin, yielding ceramide and phosphorylcholine. Ceramide then serves as a second messenger, leading to apoptotic DNA degradation.We suggested that reactive oxidants up-regulate ceramide generation and cause elevated apoptosis in human airway epithelial (HAE) cells, thereby leading to lung injury pathologies. However, the mechanisms and target molecules of reactive oxidants affecting the HAE cells are not fully understood. Therefore, we proposed that increased oxidative stress and elevated ceramide generation are coupled at the molecular level by an unknown SMase that generates ceramide by hydrolysis of sphingomyelin (Fig. 1B). To proceed from the cellular to the molecular level, we searched for the specific SMase that is modulated by reactive oxygen species in lung epithelial cells, which led to our isolation of the novel nSMase2 from monkey lung tissue and HAE cells (1). This nSMase2 was previously found in the brain (10).We then demonstrated that nSMase2 is the only member of the sphingomyelin phosphodiesterases family that is up-regulated and responsible for ceramide generation in HAE cells ...

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“…It can bind with the 60S ribosomal subunit and prevent peptide bond formation to result in block of peptide elongation and degradation of polyribosome, functionally inhibiting synthesis of numerous proteins and DNA [2]. Recent studies show that anisomycin activates c-jun N-terminal kinase/stress-activated protein kinase (JNK) and p38 mitogen activated protein kinase (p38) to protect the neurons of cerebral cortex [3]. Therefore, it is frequently used as an activation agent in mitogenactivated protein kinase signaling pathways.…”

Section: Introductionmentioning

confidence: 99%

Low-dose anisomycin is sufficient to alter the bio-behaviors of Jurkat T cells

Sun¹,

Xing²,

S³

et al. 2013

Open Life Sciences

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Anisomycin is a pyrrolidine antibiotic isolated from Streptomyces griseolus. It has been found that a quite low dose of anisomycin is sufficient to block proliferation of primary T lymphocytes. The focus of this study is to explore the possibility of anisomycin to treat human acute leukemia Jurkat T cells in vitro. The results indicated that the low dose of anisomycin could significantly inhibit the colony formation of Jurkat T cells and elevate the inhibition rate of Jurkat T cell growth along with its increasing concentrations. Jurkat T cell cycle was blocked into S-phase by anisomycin. Consistent with the increased proportion of sub-G1 phase, anisomycin promoted Jurkat T cell apoptosis. The CD69 and CD25 expression on the surface of Jurkat T cells was also down-regulated prominently along with the enhancing concentrations of anisomycin, followed by the decreased production of IL-4, IL-10, IL-17, TGF-β and IFN-γ, and the down-regulated expression of phosphorylated-ERK1/2. The results suggest that the suppressive effect of anisomycin on Jurkat T cell growth may be related to inhibiting TGF-β production and ERK1/2 activation, arresting the cell cycle at S-phase and promoting the apoptosis of Jurkat T cells.

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Anisomycin activates p38 MAP kinase to induce LTD in mouse primary visual cortex

Cited by 40 publications

References 23 publications

Microglial Receptor for Advanced Glycation End Product-Dependent Signal Pathway Drives β-Amyloid-Induced Synaptic Depression and Long-Term Depression Impairment in Entorhinal Cortex

Microglial Receptor for Advanced Glycation End Product-Dependent Signal Pathway Drives β-Amyloid-Induced Synaptic Depression and Long-Term Depression Impairment in Entorhinal Cortex

Neutral Sphingomyelinase 2 (nSMase2) Is a Phosphoprotein Regulated by Calcineurin (PP2B)

Low-dose anisomycin is sufficient to alter the bio-behaviors of Jurkat T cells

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