Integrin-linked Kinase Controls Neurite Outgrowth in N1E-115 Neuroblastoma Cells

Ishii, Toshiaki; Satoh, Eiki; Nishimura, Masakazu

doi:10.1074/jbc.m105198200

Cited by 53 publications

(56 citation statements)

References 44 publications

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“…Almost nothing is known about the relationship between ILK and p38 MAPK. In N1E-115 cells, p38 MAPK activation was reported to be involved in ILK-mediated signal transduction leading to integrin-dependent neurite outgrowth (Ishii et al, 2001). In other studies utilizing wild-type embryonic kidney organ cultures and IMCD cells transfected with mutants that were proposed to alter the kinase activity of ILK, ILK was shown to be required for BMP7-induced branching morphogenesis and a dominant-negative ILK decreased BMP7-dependent phosphorylation of p38 MAPK and phospho-ATF2.…”

Section: Discussionmentioning

confidence: 94%

Integrin-linked kinase regulates p38 MAPK-dependent cell cycle arrest in ureteric bud development

Smeeton

Zhang

Bulus³

et al. 2010

Development

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SUMMARYThe integrin-linked kinase (ILK), pinch and parvin ternary complex connects the cytoplasmic tails of 1 integrins to the actin cytoskeleton. We recently showed that constitutive expression of ILK and alpha parvin in both the ureteric bud and the metanephric mesenchyme of the kidney is required for kidney development. In this study, we define the selective role of ILK in the ureteric bud of the mouse kidney in renal development by deleting it in the ureteric cell lineage before the onset of branching morphogenesis (E10.5). Although deleting ILK resulted in only a moderate decrease in branching, the mice died at 8 weeks of age from obstruction due to the unprecedented finding of intraluminal collecting duct cellular proliferation. ILK deletion in the ureteric bud resulted in the inability of collecting duct cells to undergo contact inhibition and to activate p38 mitogen-activated protein kinase (MAPK) in vivo and in vitro. p38 MAPK activation was not dependent on the kinase activity of ILK. Thus, we conclude that ILK plays a crucial role in activating p38 MAPK, which regulates cell cycle arrest of epithelial cells in renal tubulogenesis.

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Section: Discussionmentioning

confidence: 94%

Integrin-linked kinase regulates p38 MAPK-dependent cell cycle arrest in ureteric bud development

Smeeton

Zhang

Bulus³

et al. 2010

Development

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“…Transient activation of p38 MAP kinase is critical for both growth factor-mediated and integrin-mediated neurite outgrowth (4,15,16). p38 MAP kinase, however, is also implicated in the mediation of apoptosis of four separate experiments.…”

Section: Discussionmentioning

confidence: 99%

Calcineurin Contributes to the Enhancing Effect of Adenosine on Nerve Growth Factor-Induced Neurite Outgrowth via the Decreased Duration of p38 Mitogen-Activated Protein Kinase Phosphorylation

et al. 2004

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Abstract. Adenosine enhances nerve growth factor (NGF)-induced neurite outgrowth in PC12 cells. We found that adenosine increases NGF-induced phosphorylation of extracellular signalregulated kinase (ERK), but decreases the duration of phosphorylation of p38 mitogen-activated protein (MAP) kinase. Therefore, we further examined the involvement of protein phosphatase in these effects of adenosine. FK506, a specific calcineurin inhibitor, inhibited the enhancing effect of adenosine on the NGF-induced neurite outgrowth and increased the duration of p38 MAP kinase phosphorylation without affecting ERK phosphorylation. These results suggest that adenosine decreases the duration of p38 MAP kinase via calcineurin activation, which contributes to the enhancement of NGF-induced neurite outgrowth.

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“…46 Because MAP kinase serves as a downstream effector of ␤1 integrin, 47 this fibronectin receptor, which is clustered in focal adhesion sites, could recruit ILK, and this, in turn, could regulate MAP kinase activity. 48 Thus, by this additional mechanism, Erk (p42/44), p38, and JNK could control the cell cycle as well as cellular proliferation, and alterations in these mechanisms could induce apoptosis.…”

Section: Discussionmentioning

confidence: 99%

Involvement of integrin-linked kinase in carbon tetrachloride–induced hepatic fibrosis in rats

et al. 2006

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Integrin-linked kinase (ILK) is a multidomain focal adhesion protein implicated in signal transduction between integrins and growth factor receptors. Although its expression is upregulated in pulmonary and renal fibrosis, its role in the development of hepatic fibrosis remains to be determined. Therefore, we considered it important to investigate whether ILK is involved in activation of hepatic stellate cells and thus plays a role in the development of hepatic fibrosis. Immunohistochemical analysis of liver sections obtained from rats with CCl 4 -induced cirrhosis revealed increased expression and colocalization of ILK and alpha-smooth muscle actin in hepatic stellate cells in perisinusoidal areas. In addition, hepatic stellate cells isolated from fibrotic livers expressed high levels of ILK and alpha-smooth muscle actin, and their expression was sustained in culture. In contrast, hepatic stellate cells (HSCs) isolated from normal rat liver did not express ILK, but its expression was increased when the cells were activated in culture. Our studies also showed that ILK is involved in the phosphorylation of ERK 1/2, p38 MAPK, JNK, and PKB and that selective inhibition of ILK expression by siRNA results in a significant decrease in their phosphorylation. These changes were accompanied by significant inhibition of cell spreading and migration without affecting cell proliferation. In conclusion, ILK plays a key role in HSC activation and could be a possible target for antifibrogenic therapy. (HEPATOLOGY 2006;44:612-622.)

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Integrin-linked Kinase Controls Neurite Outgrowth in N1E-115 Neuroblastoma Cells

Cited by 53 publications

References 44 publications

Integrin-linked kinase regulates p38 MAPK-dependent cell cycle arrest in ureteric bud development

Integrin-linked kinase regulates p38 MAPK-dependent cell cycle arrest in ureteric bud development

Calcineurin Contributes to the Enhancing Effect of Adenosine on Nerve Growth Factor-Induced Neurite Outgrowth via the Decreased Duration of p38 Mitogen-Activated Protein Kinase Phosphorylation

Involvement of integrin-linked kinase in carbon tetrachloride–induced hepatic fibrosis in rats

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