Requirement of p38 stress-activated MAP kinase for cell death in the developing retina depends on the stage of cell differentiation

2006 ◽  
Vol 49 (5) ◽  
pp. 494-499 ◽  
Author(s):  
Claudia B.L. Campos ◽  
Pierre-André Bédard ◽  
Rafael Linden
Keyword(s):  
Cell Death ◽  
Cell Differentiation ◽  
Map Kinase

Mechanisms of Manganese-Induced Rat Pheochromocytoma (PC12) Cell Death and Cell Differentiation

2002 ◽  
Vol 23 (2) ◽  
pp. 147-157 ◽  
Author(s):  
Jerome A. Roth ◽  
Craig Horbinski ◽  
Dennis Higgins ◽  
Pamela Lein ◽  
Michael D. Garrick
Keyword(s):  
Cell Death ◽  
Cell Differentiation ◽  
Pc12 Cell ◽  
Pheochromocytoma Pc12

scholarly journals Differentiating life and death: An inflammatory affair

2018 ◽  
Author(s):  
Dustin Lane
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cell Death ◽  
Cell Differentiation ◽  
Programmed Cell Death ◽  
Signaling Networks ◽  
Inhibitors Of Apoptosis ◽  
Life And Death ◽  
Cell Death Signaling ◽  
Cycle Dependent

Programmed cell death signaling networks are frequently activated to coordinate the process of cell differentiation, and a variety of apoptotic events can mediate the process. This can include the ligation of death receptors, the activation of downstream caspases, and the induction of chromatin fragmentation, and all of these events can occur without downstream induction of death. Importantly, regulators of programmed cell death also have established roles in mediating differentiation. This review will provide an overview of apoptosis and its regulation by Inhibitors of Apoptosis (IAPs) and Bcl-2 family members. It will then outline the cross-talk between NF-ĸB and apoptotic signaling in the regulation of apoptosis before discussing the function of these regulators in the control of cell differentiation. It will end on a discussion of how a DNA damage-directed, cell cycle-dependent differentiation program may be controlled across multiple passages through cell cycle, and will assert that the failure to properly differentiate is the underlying cause of cancer.

scholarly journals MAP Kinase OsMEK2 and OsMPK1 Signaling for Ferroptotic Cell Death in Rice-Magnaporthe oryzae Interactions

2020 ◽  
Author(s):  
Sarmina Dangol ◽  
Raksha Singh ◽  
Khoa Nam Nguyen ◽  
Yafei Chen ◽  
Juan Wang ◽  
...  
Keyword(s):  
Cell Death ◽  
Map Kinase ◽  
Signaling Pathways ◽  
Magnaporthe Oryzae ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Microbial Pathogens ◽  
Blast Disease ◽  
Related Cell ◽  
Mitogen Activated Protein

ABSTRACTMitogen-activated protein kinase (MAPK) signaling is required for plant cell death responses to invading microbial pathogens. Ferric ions and reactive oxygen species (ROS) accumulate in rice (Oryza sativa) tissues undergoing cell death during Magnaporthe oryzae infection. Here, we report that rice MAP kinase (OsMEK2 and OsMPK1) signaling cascades are involved in iron- and ROS-dependent ferroptotic cell death responses of rice to M. oryzae infection. OsMEK2 interacted with OsMPK1 in the cytoplasm, and OsMPK1 moved from the cytoplasm into the nucleus to bind to the OsWRKY90 transcription factor. OsMEK2 expression may trigger OsMPK1-OsWRKY90 signaling pathways in the nucleus. Avirulent M. oryzae infection in ΔOsmek2 mutant rice did not trigger iron and ROS accumulation and lipid peroxidation, and also downregulated OsMPK1, OsWRKY90, OsRbohB, and OsPR-1b expression. However, OsMEK2 overexpression induced ROS-and iron-dependent cell death in rice during M. oryzae infection. The downstream MAP kinase (OsMPK1) overexpression induced ROS- and iron-dependent ferroptotic cell death in the compatible rice-M. oryzae interaction. These data suggest that the OsMEK2-OsMPK1-OsWRKY90 signaling cascade is involved in the ferroptotic cell death in rice. The small-molecule inducer erastin triggered iron- and lipid ROS-dependent, but OsMEK2-independent, ferroptotic cell death in ΔOsmek2 mutant plants during M. oryzae infection. Disease-related cell death was lipid ROS-dependent and iron-independent in the ΔOsmek2 mutant plants. These combined results suggest that OsMEK2 and OsMPK1 expression positively regulates iron- and ROS-dependent ferroptotic cell death via OsMEK2-OsMPK1-OsWRKY90 signaling pathways, and blast disease (susceptibility)-related cell death was ROS-dependent but iron-independent in rice-M. oryzae interactions.

Neurogenesis response to hypoxia-induced cell death: map kinase signal transduction mechanisms

2004 ◽  
Vol 1021 (1) ◽  
pp. 8-19 ◽  
Author(s):  
Li Zhou ◽  
Keith Del Villar ◽  
Zhaohui Dong ◽  
Carol A. Miller
Keyword(s):  
Signal Transduction ◽  
Cell Death ◽  
Map Kinase ◽  
Transduction Mechanisms

scholarly journals Hexosamine Biosynthetic Pathway Inhibition Leads to AML Cell Differentiation and Cell Death

2018 ◽  
Vol 17 (10) ◽  
pp. 2226-2237 ◽  
Author(s):  
Abhishek Asthana ◽  
Parameswaran Ramakrishnan ◽  
Yorleny Vicioso ◽  
Keman Zhang ◽  
Reshmi Parameswaran
Keyword(s):  
Cell Death ◽  
Cell Differentiation ◽  
Biosynthetic Pathway ◽  
Hexosamine Biosynthetic Pathway ◽  
Pathway Inhibition

scholarly journals Dual-specificity phosphatase 4 is upregulated during skeletal muscle atrophy and modulates extracellular signal-regulated kinase activity

2019 ◽  
Vol 316 (4) ◽  
pp. C567-C581 ◽  
Author(s):  
Ashley N. Haddock ◽  
Sydney A. Labuzan ◽  
Amy E. Haynes ◽  
Caleb S. Hayes ◽  
Karina M. Kakareka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Map Kinase ◽  
Reporter Gene ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Skeletal Muscle Atrophy ◽  
Kinase Signaling ◽  
Muscle Cell Differentiation ◽  
Map Kinase Signaling

Skeletal muscle atrophy results from disparate physiological conditions, including denervation, corticosteroid treatment, and aging. The purpose of this study was to describe and characterize the function of dual-specificity phosphatase 4 (Dusp4) in skeletal muscle after it was found to be induced in response to neurogenic atrophy. Quantitative PCR and Western blot analysis revealed that Dusp4 is expressed during myoblast proliferation but rapidly disappears as muscle cells differentiate. The Dusp4 regulatory region was cloned and found to contain a conserved E-box element that negatively regulates Dusp4 reporter gene activity in response to myogenic regulatory factor expression. In addition, the proximal 3′-untranslated region of Dusp4 acts in an inhibitory manner to repress reporter gene activity as muscle cells progress through the differentiation process. To determine potential function, Dusp4 was fused with green fluorescent protein, expressed in C2C12 cells, and found to localize to the nucleus of proliferating myoblasts. Furthermore, Dusp4 overexpression delayed C2C12 muscle cell differentiation and resulted in repression of a MAP kinase signaling pathway reporter gene. Ectopic expression of a Dusp4 dominant negative mutant blocked muscle cell differentiation and attenuated MAP kinase signaling by preferentially targeting the ERK1/2 branch, but not the p38 branch, of the MAP kinase signaling cascade in skeletal muscle cells. The findings presented in this study provide the first description of Dusp4 in skeletal muscle and suggest that Dusp4 may play an important role in the regulation of muscle cell differentiation by regulating MAP kinase signaling.

scholarly journals Mitogen-activated protein kinase activation is insufficient for growth factor receptor-mediated PC12 cell differentiation.

1995 ◽  
Vol 15 (7) ◽  
pp. 3644-3653 ◽  
Author(s):  
R R Vaillancourt ◽  
L E Heasley ◽  
J Zamarripa ◽  
B Storey ◽  
M Valius ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Growth Factor ◽  
Map Kinase ◽  
Pc12 Cells ◽  
Pc12 Cell ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Kinase Pathway

When expressed in PC12 cells, the platelet-derived growth factor beta receptor (beta PDGF-R) mediates cell differentiation. Mutational analysis of the beta PDGF-R indicated that persistent receptor stimulation of the Ras/Raf/mitogen-activated protein (MAP) kinase pathway alone was insufficient to sustain PC12 cell differentiation. PDGF receptor activation of signal pathways involving p60c-src or the persistent regulation of phospholipase C gamma was required for PC12 cell differentiation. beta PDGF-R regulation of phosphatidylinositol 3-kinase, the GTPase-activating protein of Ras, and the tyrosine phosphatase, Syp, was not required for PC12 cell differentiation. In contrast to overexpression of oncoproteins involved in regulating the MAP kinase pathway, growth factor receptor-mediated differentiation of PC12 cells requires the integration of other signals with the Ras/Raf/MAP kinase pathway.

171 MAP KINASE-DEPENDENT PATHWAYS ARE ACTIVATED DURING PROGRAMMED CELL DEATH IN A VIRAL MODEL OF FULMINANT HEPATIC FAILURE

2008 ◽  
Vol 48 ◽  
pp. S73
Author(s):  
R. Garcia-Lastra ◽  
M. Alvarez ◽  
B. San-Miguel ◽  
F. Jorquera ◽  
J. Gonzalez-Gallego ◽  
...  
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Map Kinase ◽  
Fulminant Hepatic Failure ◽  
Hepatic Failure
Sign in / Sign up

Export Citation Format

Share Document