scholarly journals Irisin Stimulates Browning of White Adipocytes Through Mitogen-Activated Protein Kinase p38 MAP Kinase and ERK MAP Kinase Signaling

Diabetes ◽  
2013 ◽  
Vol 63 (2) ◽  
pp. 514-525 ◽  
Author(s):  
Y. Zhang ◽  
R. Li ◽  
Y. Meng ◽  
S. Li ◽  
W. Donelan ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Kinase Signaling ◽  
White Adipocytes ◽  
Map Kinase Signaling ◽  
Mitogen Activated Protein

Effects of exercise and insulin on mitogen-activated protein kinase signaling pathways in rat skeletal muscle

1996 ◽  
Vol 271 (2) ◽  
pp. E403-E408 ◽  
Author(s):  
L. J. Goodyear ◽  
P. Y. Chang ◽  
D. J. Sherwood ◽  
S. D. Dufresne ◽  
D. E. Moller
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Map Kinase ◽  
Signaling Pathways ◽  
Mammalian Cells ◽  
Mitogen Activated Protein Kinase ◽  
Kinase Signaling ◽  
Rat Skeletal Muscle ◽  
Map Kinase Signaling ◽  
Mitogen Activated Protein

Studies in mammalian cells have established the existence of at least three distinct mitogen-activated protein kinase (MAP kinase) signaling pathways that are activated by a variety of growth factors and/or environmental stressors. We determined whether physical exercise, a physiological stressor, and insulin, a metabolic stimulator and growth factor, activate the c-jun NH2-terminus kinase (JNK), the p38 kinase, and/or the extracellular regulatory kinases (ERK; p42MAPK and p44MAPK) signaling pathways in rat skeletal muscle. Animals were studied immediately after running on a motorized treadmill for 10-60 min (20 m/min, 10% grade) or 5-30 min after an intraperitoneal injection of insulin (20 U/rat). Exercise increased skeletal muscle JNK activity by two- to threefold throughout the time course studied, whereas insulin did not significantly increase JNK activity. The p38 activity was slightly stimulated by exercise and not by insulin. The ERK kinase pathway, as assessed by ribosomal S6 kinase-2 activity assays and phosphospecific p42MAPK/p4NAPK immunoblotting, was stimulated by both exercise and insulin. These data are the first demonstration of exercise stimulating multiple intracellular signaling pathways in skeletal muscle. Activation of these MAP kinase signaling pathways may mediate changes in skeletal muscle growth and metabolism that occur in response to exercise.

scholarly journals Protection of glioblastoma cells from cisplatin cytotoxicity via protein kinase Cι-mediated attenuation of p38 MAP kinase signaling

Oncogene ◽  
2005 ◽  
Vol 25 (20) ◽  
pp. 2909-2919 ◽  
Author(s):  
R M Baldwin ◽  
M Garratt-Lalonde ◽  
D A E Parolin ◽  
P M Krzyzanowski ◽  
M A Andrade ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Signaling ◽  
Glioblastoma Cells ◽  
Map Kinase Signaling

scholarly journals Role of MLK3 in the Regulation of Mitogen-Activated Protein Kinase Signaling Cascades

2005 ◽  
Vol 25 (9) ◽  
pp. 3670-3681 ◽  
Author(s):  
Deborah Brancho ◽  
Juan-Jose Ventura ◽  
Anja Jaeschke ◽  
Beth Doran ◽  
Richard A. Flavell ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Selective Reduction ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Signaling Cascades ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Jnk Activation ◽  
Protein Kinase Signaling

ABSTRACT Mixed-lineage protein kinase 3 (MLK3) is a member of the mitogen-activated protein (MAP) kinase kinase kinase group that has been implicated in multiple signaling cascades, including the NF-κB pathway and the extracellular signal-regulated kinase, c-Jun NH2-terminal kinase (JNK), and p38 MAP kinase pathways. Here, we examined the effect of targeted disruption of the murine Mlk3 gene. Mlk3 −/− mice were found to be viable and healthy. Primary embryonic fibroblasts prepared from these mice exhibited no major signaling defects. However, we did find that MLK3 deficiency caused a selective reduction in tumor necrosis factor (TNF)-stimulated JNK activation. Together, these data demonstrate that MLK3 contributes to the TNF signaling pathway that activates JNK.

scholarly journals Role of the JIP4 Scaffold Protein in the Regulation of Mitogen-Activated Protein Kinase Signaling Pathways

2005 ◽  
Vol 25 (7) ◽  
pp. 2733-2743 ◽  
Author(s):  
Nyaya Kelkar ◽  
Claire L. Standen ◽  
Roger J. Davis
Keyword(s):  
Map Kinase ◽  
Signaling Pathway ◽  
Scaffold Protein ◽  
P38 Map Kinase ◽  
Scaffold Proteins ◽  
Mitogen Activated Protein Kinase ◽  
Kinase Signaling ◽  
Interacting Protein ◽  
Jnk Signaling ◽  
Mitogen Activated Protein

ABSTRACT The c-Jun NH2-terminal kinase (JNK)-interacting protein (JIP) group of scaffold proteins (JIP1, JIP2, and JIP3) can interact with components of the JNK signaling pathway and potently activate JNK. Here we describe the identification of a fourth member of the JIP family. The primary sequence of JIP4 is most closely related to that of JIP3. Like other members of the JIP family of scaffold proteins, JIP4 binds JNK and also the light chain of the microtubule motor protein kinesin-1. However, the function of JIP4 appears to be markedly different from other JIP proteins. Specifically, JIP4 does not activate JNK signaling. In contrast, JIP4 serves as an activator of the p38 mitogen-activated protein (MAP) kinase pathway by a mechanism that requires the MAP kinase kinases MKK3 and MKK6. The JIP4 scaffold protein therefore appears to be a new component of the p38 MAP kinase signaling pathway.

scholarly journals Mitogen-Activated Protein Kinase-Dependent Interleukin-1α Intracrine Signaling Is Modulated by YopP during Yersinia enterocolitica Infection

2011 ◽  
Vol 80 (1) ◽  
pp. 289-297 ◽  
Author(s):  
Rumu Bose ◽  
Josephine Thinwa ◽  
Paola Chaparro ◽  
Youmin Zhong ◽  
Santanu Bose ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Yersinia Enterocolitica ◽  
Nuclear Translocation ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Virulence Plasmid ◽  
Content Type ◽  
Mitogen Activated Protein ◽  
Interleukin 1Α

ABSTRACTYersinia enterocoliticais a food-borne pathogen that preferentially infects the Peyer's patches and mesenteric lymph nodes, causing an acute inflammatory reaction. Even thoughY. enterocoliticainduces a robust inflammatory response during infection, the bacterium has evolved a number of virulence factors to limit the extent of this response. We previously demonstrated that interleukin-1α (IL-1α) was critical for the induction of gut inflammation characteristic ofY. enterocoliticainfection. More recently, the known actions of IL-1α are becoming more complex because IL-1α can function both as a proinflammatory cytokine and as a nuclear factor. In this study, we tested the ability ofY. enterocoliticato modulate intracellular IL-1α-dependent IL-8 production in epithelial cells. Nuclear translocation of pre-IL-1α protein and IL-1α-dependent secretion of IL-8 into the culture supernatant were increased during infection with a strain lacking the 70-kDa virulence plasmid compared to the case during infection with the wild type, suggesting thatYersiniaouter proteins (Yops) might be involved in modulating intracellular IL-1α signaling. Infection of HeLa cells with a strain lacking theyopPgene resulted in increased nuclear translocation of pre-IL-1α and IL-1α-dependent secretion of IL-8 similar to what is observed with bacteria lacking the virulence plasmid. YopP is a protein acetylase that inhibits mitogen-activated protein kinase (MAP kinase)- and NF-κB-dependent signal transduction pathways. Nuclear translocation of pre-IL-1α and IL-1α-dependent secretion of IL-8 in response toYersinia enterocoliticainfection were dependent on extracellular signal-regulated kinase (ERK) and p38 MAP kinase signaling but independent of NF-κB. These data suggest thatY. enterocoliticainhibits intracellular pre-IL-1α signaling and subsequent proinflammatory responses through inhibition of MAP kinase pathways.

scholarly journals p38 Mitogen-Activated Protein Kinase-Dependent and -Independent Signaling of mRNA Stability of AU-Rich Element-Containing Transcripts

2003 ◽  
Vol 23 (2) ◽  
pp. 425-436 ◽  
Author(s):  
Mathias A. E. Frevel ◽  
Tala Bakheet ◽  
Aristobolo M. Silva ◽  
John G. Hissong ◽  
Khalid S. A. Khabar ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Cdna Array ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Mrna Turnover ◽  
Mrna Levels ◽  
Mrna Stabilization ◽  
Mrna Induction ◽  
Mitogen Activated Protein

ABSTRACT Adenylate/uridylate-rich element (ARE)-mediated mRNA turnover is an important regulatory component of gene expression for innate and specific immunity, in the hematopoietic system, in cellular growth regulation, and for many other cellular processes. This diversity is reflected in the distribution of AREs in the human genome, which we have established as a database of more than 900 ARE-containing genes that may utilize AREs as a means of controlling cellular mRNA levels. The p38 mitogen-activated protein kinase (MAP kinase) pathway has been implicated in regulating the stability of nine ARE-containing transcripts. Here we explored the entire spectrum of ARE-containing genes for p38-dependent regulation of ARE-mediated mRNA turnover with a custom cDNA array containing probes for 950 ARE mRNAs. The human monocytic cell line THP-1 treated with lipopolysaccharide (LPS) was used as a reproducible cellular model system that allowed us to precisely control the conditions of mRNA induction and decay in the absence and presence of the p38 inhibitor SB203580. This approach allowed us to establish an LPS-induced ARE mRNA expression profile in human monocytes and determine the half-lives of 470 AU-rich mRNAs. Most importantly, we identified 42 AU-rich genes, previously unrecognized, that show p38-dependent mRNA stabilization. In addition to a number of cytokines, several interesting novel AU-rich transcripts likely to play a role in macrophage activation by LPS exhibited p38-dependent transcript stabilization, including macrophage-specific colony-stimulating factor 1, carbonic anhydrase 2, Bcl2, Bcl2-like 2, and nuclear factor erythroid 2-like 2. Finally, the identification of the p38-dependent upstream activator MAP kinase kinase 6 as a member of this group identifies a positive feedback loop regulating macrophage signaling via p38 MAP kinase-dependent transcript stabilization.

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