G-CSF increases Akt phosphorylaton and activation.

CXCR4 and CXCR7 are capable of activating the PI3K pathway via G-protein and β-arrestin. Blocking either receptor is sufficient to inhibit Akt phosphorylation, but co-stimulation does not indicate an additive effect.

TLR stimulation results in the phosphorylation of Akt by a p38α- and MK2/3-dependent manner.

ROS accumulation inhibits the PI3K pathway repressor, PTEN.

Inhibition of FoxO3a leads to a hyperphosphorylation of Akt.

Linkage of β1 integrins with some of their ligands leads to activation of PI3K through the direct interaction with the focal adhesion kinase (FAK) or Pyk2, depending on cell type.

CXCR4 and CXCR7 are capable of activating the PI3K pathway via G-protein and β-arrestin. Blocking either receptor is sufficient to inhibit Akt phosphorylation, but co-stimulation does not indicate an additive effect.

GSK3β-mediated phosphorylation leads to β-catenin ubiquitination and subsequent degradation via proteasome-dependent proteolysis.

TLR4 recognition of its ligand stimulates Myd88 recruitment, which leads to the activation of NF-kB.

The NF-kB pathway is activated by Myd88-dependent IL-1R signaling. Studies observing endothelial cells have noted that NF-kB activation requires PI3K, which is recruited through the interaction of p85 with IL-1R.

ROS activation of the NF-kB pathway requires ERK for IκBα phosphorylation and degradation.

ROS activation of the NF-kB pathway requires ERK for IκBα phosphorylation and degradation.

The NF-kB pathway is activated by Myd88-dependent IL-1R signaling. Studies observing endothelial cells have noted that NF-kB activation requires PI3K, which is recruited through the interaction of p85 with IL-1R.

The NF-kB pathway is activated by IL-1R signaling in a PI3K-dependent mechanism.

TLR1,2,4-10 recognition of their ligands stimulates Myd88 recruitment, which leads to the activation of NF-kB.

ROS accumulation results in increased activation of the NF-kB pathway. This activity is caused by two possible mechanisms: the promotion of disulfide-bonds formation favoring NEMO dimerization and S-gluthationylation of IKK-β.

FoxO3a inhibits transloation of the NF-kB subunit RelA.

The NF-kB pathway is activated by IL-1R signaling in a PI3K-dependent mechanism.

FoxO3a upregulates enzymes such as superoxide dismutase, glutathion peroxidases, and catalase which regulate ROS levels.

Stimulation with LPS increases intracellular ROS levels.

Mesenchymal stem cells treated with IL-1β upregulate intracellular ROS levels.

Gfi1 contains consensus sites for its own promoter region, suggestin cis regulation. These sites are conserved in mice, rates, and humans.

Gfi1 mRNA concentration increases after treatment with G-CSF. This increase is dependent on the integrity of the carboxil terminal region of the G-CSF receptor.

Gfi1 is upregulated after LPS stimulation of bone marrow and macrophages. Gfil regulates some NF-kB targets by binding to p65.

Treatment with IL-1α showed an increase in G-CSF expression. Since IL-1α and IL-1β bind and activate the same receptor, it is assumed that G-CSF can be induced in mesenchymal stem cells or other stromal components expressing IL-1R1.

G-CSF binding to its receptor increases Akt and Erk phosphorylaton and activation.

TLR stimulation results in the phosphorylation of Akt in serine 473.

ROS accumulation inhibits the PI3K pathway repressor, PTEN.

CXCL12 binding to CXCR4 enhances VLA-4 affinity to its ligands.

VLA-4 integrin binds to the integrin receptor VCAM-1.

FOXO transcription factors compete with T-cell factor for binding to β-catenin, which inhibits β-catenin/T-cell factor transcription activity.

GSK3β-mediated phosphorylation leads to β-catenin ubiquitination and subsequent degradation via proteasome-dependent proteolysis.

NFkB recruits IKKβ. IKKβ directly phosphorylates p65, promoting its nuclear translocation. This induces expression of Smurf1 and Smurf2 (Smad ubiquitin regulatorand factor1 and 2), which increase β-catenin degradation.

Akt activation leads to the phosphorylation and inactivation of GSK3β.

Akt phosphorylates FoxO3a, causing its cytoplasmic localization and down-regulation of its target genes.

ERK phosphorylates FoxO3a, causing its inactivation and subsequent degradation via MDM2.

β-catenin interacts directly with FoxO1, FoxO3a, and FoxO3 to increase its transcriptional activity.

ROS accumulation stimulates FOXO localization, increasing the expression of ROS-regulating enzymes such as catalase.

Cx43 Cx43_M activates itself.

TLR_M is activated by ITLR.

The PI3K/Akt pathway regulates the maturation of IL-1β through the inhibition of caspase-1. The PI3K/Akt pathway also up-regulates antagonist molecules for the IL-1β receptor, preventing IL-1β signaling.

The PI3K/Akt pathway upregulates antagonist molecules for the IL-1β receptor, preventing IL-1β signaling.

IL-1β contains binding sites for NF-κB pathway elements.

ROS- dependent signaling upregulates pro-IL-1β transcription and IL-1β exportation in macrophage stimulated with LPS.

ROS accumulation in mesenchymal stem cells increases IL-1β expression and secretion.

From the analysis of the IL-1β promoter region in rainbow trout, IL-1β appears to contain consensus sites for NF-κB, NF-IL6, AP1, AP4, CHOP/CEBPa, SP1, PU.1, and Gfi1. NF-κB binding sites have been confirmed in humans and mice.

ITLR activates itself.

CXCR7 is an alternative CXCL12 receptor that has higher binding affinity than CXCR4.

The promoter region of CXCR7 contains three consensus sites for NF-κB binding.

G-CSF promotes the phosphorylation of Akt and ERK1/2.

Mesenchymal stem cells treated with LPS increased ERK phosphorylation by 40%.

Oxidative stress promotes the phosphorylation and activation of ERK1/2.

Phosphorylation of ERK1/2 after CXCL12-CXCR4 binding is prevented by PI3K-inhibitor treatment.

Cells from Gfi1-/- mice showed a decreased activation of the ERK pathway.

G-CSF promotes the phosphorylation of Akt and ERK1/2.

GSK3β prevents LPS-inducted ERK1/2 phosphorylation.

CXCR4 binding to CXCR7, promotes ERK1/2 phosphorylation and activation.

Oxidative stress activates MAP kinases, increasing ERK1/2 phosphorylation.

Interaction between VLA-4 and its ligand leads to the up-regulation of the ERK pathway.

Phosphorylation of ERK1/2 after CXCL12-CXCR4 binding is prevented by PI3K-inhibitor treatment.

FoxO3a increases Spred2 expression, which prevents ERK phosphorylation.

TLR_H is activated by ITLR.

Cx43 gap junctions mediate the conduction of calcium ions, allowing for intercelular contact. This in turn enables MSC to secrete CXCL12.

G-CSF promotes the degradation of CXCL12 mRNA by the increase of metalloproteinase-9.

β-catenin inhibits CXCL12 transcription by binding to the promotor region.

Activation of the NF-kB pathway down-regulates CXCL12 expression through an unknown mechanism that utilizes RelB.

Akt phosphorylates FoxO3a, causing its cytoplasmic localization and down-regulation of its target genes.

β-catenin interacts directly with FoxO1, FoxO3a, and FoxO3 to increase its transcriptional activity.

ROS accumulation stimulates FOXO localization, increasing the expression of ROS-regulating enzymes such as catalase.

ERK phosphorylates FoxO3a, causing its inactivation and subsequent degradation via MDM2.

Stimulation with LPS increases intracellular ROS levels.

FoxO3a upregulates enzymes such as superoxide dismutase and catalase which regulate ROS levels.

Mesenchymal stem cells treated with IL-1β upregulate intracellular ROS levels.

Akt activates leads to the phosphorylation and inactivation of GSK3β.

Treatment with a specific PI3K inhibitor implicated that the PI3KAkt_M pathway is involved in the up-regulation of VCAM-1 expression.

NF-κB up-regulaties VCAM-1 expression, likely through directly binding to NF-κB sites in the promoter region of the VCAM-1 gene.

Treatment with the canonical Wnt pathway ligand, Wnt3a, down-regulation of VCAM-1 expression.