IGF-I enhances α5β1 integrin expression and cell motility in human chondrosarcoma cells

2011 ◽  
Vol 226 (12) ◽  
pp. 3270-3277 ◽  
Author(s):  
Chi-Ming Wu ◽  
Te-Mao Li ◽  
Sheng-Feng Hsu ◽  
Yi-Chang Su ◽  
Shung-Te Kao ◽  
...  
Keyword(s):  
Cell Motility ◽  
Integrin Expression ◽  
Human Chondrosarcoma ◽  
Igf I ◽  
Α5β1 Integrin

HMGB-1 induces cell motility and α5β1 integrin expression in human chondrosarcoma cells

2012 ◽  
Vol 322 (1) ◽  
pp. 98-106 ◽  
Author(s):  
Chih-Hsin Tang ◽  
Yun-Ting Keng ◽  
Ju-Fang Liu
Keyword(s):  
Cell Motility ◽  
Integrin Expression ◽  
Human Chondrosarcoma ◽  
Α5β1 Integrin

IL-8 increases integrin expression and cell motility in human chondrosarcoma cells

2011 ◽  
Vol 112 (9) ◽  
pp. 2549-2557 ◽  
Author(s):  
Chun-Yi Lee ◽  
Chun-Yin Huang ◽  
Meng-Yi Chen ◽  
Ching-Yuang Lin ◽  
Horng-Chaung Hsu ◽  
...  
Keyword(s):  
Cell Motility ◽  
Integrin Expression ◽  
Human Chondrosarcoma

scholarly journals Amphiregulin enhances alpha6beta1 integrin expression and cell motility in human chondrosarcoma cells through Ras/Raf/MEK/ERK/AP-1 pathway

Oncotarget ◽  
2015 ◽  
Vol 6 (13) ◽  
pp. 11434-11446 ◽  
Author(s):  
Jui-Chieh Chen ◽  
Yu-Ju Chen ◽  
Chih-Yang Lin ◽  
Yi-Chin Fong ◽  
Chin-Jung Hsu ◽  
...  
Keyword(s):  
Cell Motility ◽  
Integrin Expression ◽  
Human Chondrosarcoma

scholarly journals Correction: Amphiregulin enhances alpha6beta1 integrin expression and cell motility in human chondrosarcoma cells through Ras/Raf/MEK/ERK/AP-1 pathway

Oncotarget ◽  
2017 ◽  
Vol 8 (15) ◽  
pp. 25830-25830
Author(s):  
Jui-Chieh Chen ◽  
Yu-Ju Chen ◽  
Chih-Yang Lin ◽  
Yi-Chin Fong ◽  
Chin-Jung Hsu ◽  
...  
Keyword(s):  
Cell Motility ◽  
Integrin Expression ◽  
Human Chondrosarcoma

scholarly journals Absence of the αvβ3 Integrin Dictates the Time-Course of Angiogenesis in the Hypoxic Central Nervous System: Accelerated Endothelial Proliferation Correlates with Compensatory Increases in α5β1 Integrin Expression

2010 ◽  
Vol 30 (5) ◽  
pp. 1031-1043 ◽  
Author(s):  
Longxuan Li ◽  
Jennifer V Welser ◽  
Richard Milner
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Time Course ◽  
Αvβ3 Integrin ◽  
Integrin Expression ◽  
Brain Endothelial Cells ◽  
Endothelial Proliferation ◽  
Β3 Integrin ◽  
Α5β1 Integrin

Cerebral angiogenesis is an important adaptive response to hypoxia. As the αvβ3 integrin is induced on angiogenic vessels in the ischemic central nervous system (CNS), and the suggested angiogenic role for this integrin in other systems, it is important to determine whether the αvβ3 integrin is an important mediator of cerebral angiogenesis. αvβ3 integrin expression was examined in a model of cerebral hypoxia, in which mice were subject to hypoxia (8% O2) for 0, 4, 7, or 14 days. Immunofluorescence and western blot analysis revealed that in the hypoxic CNS, αvβ3 integrin was strongly induced on angiogenic brain endothelial cells (BEC), along with its ligand vitronectin. In the hypoxia model, β3 integrin-null mice showed no obvious defect in cerebral angiogenesis. However, early in the angiogenic process, BEC in these mice showed an increased mitotic index that correlated closely with increased α5 integrin expression. In vitro experiments confirmed α5 integrin upregulation on β3 integrin-null BEC, which also correlated with increased BEC proliferation on fibronectin. These studies confirm hypoxic induction of αvβ3 integrin on angiogenic vessels, but suggest distinct roles for the BEC integrins αvβ3 and α5β1 in cerebral angiogenesis, with αvβ3 having a nonessential role, and α5β1 promoting BEC proliferation.

scholarly journals Concerted Activity of Tyrosine Phosphatase SHP-2 and Focal Adhesion Kinase in Regulation of Cell Motility

1999 ◽  
Vol 19 (4) ◽  
pp. 3125-3135 ◽  
Author(s):  
Santos Mañes ◽  
Emilia Mira ◽  
Concepción Gómez-Mouton ◽  
Zhizuang Joe Zhao ◽  
Rosa Ana Lacalle ◽  
...  
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Cell Motility ◽  
Focal Adhesion ◽  
Tyrosine Phosphatase ◽  
Mitogen Activated Protein Kinase ◽  
Wild Type ◽  
Igf I ◽  
Mitogen Activated Protein ◽  
Mcf 7

ABSTRACT The coordinated interplay of substrate adhesion and deadhesion is necessary for cell motility. Using MCF-7 cells, we found that insulin-like growth factor I (IGF-I) induces the adhesion of MCF-7 to vitronectin and collagen in a dose- and time-dependent manner, suggesting that IGF-I triggers the activation of different integrins. On the other hand, IGF-I promotes the association of insulin receptor substrate 1 with the focal adhesion kinase (FAK), paxillin, and the tyrosine phosphatase SHP-2, resulting in FAK and paxillin dephosphorylation. Abrogation of SHP-2 catalytic activity with a dominant-negative mutant (SHP2-C>S) abolishes IGF-I-induced FAK dephosphorylation, and cells expressing SHP2-C>S show reduced IGF-I-stimulated chemotaxis compared with either mock- or SHP-2 wild-type-transfected cells. This impairment of cell migration is recovered by reintroduction of a catalytically active SHP-2. Interestingly, SHP-2-C>S cells show a larger number of focal adhesion contacts than wild-type cells, suggesting that SHP-2 activity participates in the integrin deactivation process. Although SHP-2 regulates mitogen-activated protein kinase activity, the mitogen-activated protein kinase kinase inhibitor PD-98059 has only a marginal effect on MCF-7 cell migration. The role of SHP-2 as a general regulator of cell chemotaxis induced by other chemotactic agents and integrins is discussed.

Nitric oxide attenuates insulin- or IGF-I-stimulated aortic smooth muscle cell motility by decreasing H2O2 levels: essential role of cGMP

2004 ◽  
Vol 286 (6) ◽  
pp. H2103-H2112 ◽  
Author(s):  
Daming Zhuang ◽  
Alice-Corina Ceacareanu ◽  
Yi Lin ◽  
Bogdan Ceacareanu ◽  
Madhulika Dixit ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Peroxide ◽  
Smooth Muscle ◽  
Smooth Muscle Cell ◽  
Cell Motility ◽  
Muscle Cell ◽  
Aortic Smooth Muscle Cell ◽  
Aortic Smooth Muscle ◽  
Igf I ◽  
Necessary And Sufficient

Insulin and insulin-like growth factor I (IGF-I) both play important roles in vascular remodeling. Moreover, nitric oxide (NO) is well established as a counterregulatory agent that opposes the actions of several vascular agonists, in part by decreasing smooth muscle motility. We tested the hypothesis that NO blocks insulin or IGF-I-induced rat aortic smooth muscle cell motility via a mechanism involving the attenuation of agonist-induced elevation of hydrogen peroxide levels and cGMP as mediator. Insulin or IGF-I induced an increase of hydrogen peroxide levels and cell motility. Both effects were blocked by catalase or diphenyleneiodonium, indicating that hydrogen peroxide elevation is necessary for induction of cell motility. Two NO donors mimicked the effects of catalase, indicating that NO decreases cell motility by suppressing agonist-induced elevation of hydrogen peroxide. A cGMP analogue mimicked the effect of NO, whereas a guanyl cyclase inhibitor blocked the effect of NO on hydrogen peroxide levels, indicating that elevation of cGMP is both necessary and sufficient to account for the reduction of hydrogen peroxide levels. A NO donor as well as a cGMP analogue attenuated insulin-stimulated NADPH activity, indicating that NO decreases hydrogen peroxide levels by inhibiting the generation of superoxide, via a cGMP-mediated mechanism. Finally, exogenous hydrogen peroxide increased cell motility and reversed the inhibitory effect of cGMP. These results support the view that NO plays an antioxidant role via reduction of hydrogen peroxide in cultured rat aortic smooth muscle cells and that this effect is both necessary and sufficient to account for its capacity to decrease cell motility.

scholarly journals IGF-I stimulates chemotaxis of human neuroblasts. Involvement of type 1 IGF receptor, IGF binding proteins, phosphatidylinositol-3 kinase pathway and plasmin system

2000 ◽  
Vol 165 (1) ◽  
pp. 123-131 ◽  
Author(s):  
A Puglianiello ◽  
D Germani ◽  
P Rossi ◽  
S Cianfarani
Keyword(s):  
Cell Migration ◽  
Cell Motility ◽  
Igf Binding Proteins ◽  
Neuroblast Migration ◽  
Igf I ◽  
Igf Binding ◽  
Igf Receptor ◽  
Kinase Pathway

SH-SY5Y human neuroblastoma cells express IGF receptors, IGFs and IGF binding proteins (IGFBPs), and provide a model for studying the role of the IGF system in human neuronal development. We investigated the effect of IGF-I and des(1-3)IGF-I on the motility of SH-SY5Y cells by a cell migration assay based on the assessment of the number of cells which migrated across 8 microm pore size membranes and around an agarose drop. IGF-I and des(1-3)IGF-I stimulated neuroblast chemotaxis in a dose-dependent manner. Treatment of cells with these agents for 24 h resulted in a significant increase (IGF-I by 70% and des(1-3)IGF-I by 90%; P<0. 0001) in cell motility relative to control conditions. Addition of monoclonal antibody against type 1 IGF receptor (alpha-IR3), significantly (P<0.05) reduced the cell motility induced by IGF-I (by 30%) and des(1-3)IGF-I (by 70%). Wortmannin, a specific inhibitor of phosphatidylinositol (PI)-3 kinase intracellular signalling, also reduced the IGF-stimulated cell migration (by over 40%, P<0.01), indicating a key role of the PI-3 kinase pathway in mediating the IGF effect on neuroblast migration. Finally, cell treatment with plasminogen (PLG) markedly enhanced neuroblast migration (by over 200%, P<0.01), whereas incubation with the PLG inhibitor 4-(2-aminoethyl)-benzenesulphonyl fluoride reduced cell motility (by 80%, P<0.01), thus suggesting an involvement of PLG-dependent IGFBP proteolysis in the regulation of neuroblast motility. In conclusion, IGF-I is a potent stimulator of neuroblast migration through the activation of type 1 IGF receptor and the PI-3 kinase intracellular pathway. IGFBPs and the plasmin system seem to play a role in cell motility, although the nature and the extent of their involvement has yet to be elucidated.

Sign in / Sign up

Export Citation Format

Share Document