Interactions of the integrin subunit β1A with protein kinase B/Akt, p130Cas and paxillin contribute to regulation of radiation survival

Seidler, Julia; Durzok, R; Brakebusch, Cord; Cordes, Nils

doi:10.1016/j.radonc.2005.06.018

Cited by 25 publications

(22 citation statements)

References 24 publications

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“…p130cas may mediate propofol-and pressure-stimulated phagocytosis. p130cas (a Crk-associated substrate) is a docking protein involved in regulation of the actin cytoskeleton and cell migration (1,20,45,48). Some studies suggest that p130cas may be involved in bacterial or apoptotic cell phagocytosis by macrophages (6,18,49).…”

Section: Resultsmentioning

confidence: 99%

“…The docking protein p130cas is an adaptor that promotes protein-protein interaction, facilitates focal adhesion complex formation along with FAK and Src, and mediates integrin signal transduction, leading to migration, proliferation, and survival of various cell types (17,45,48). p130cas is required for Salmonella typhimurium invasion into host cells (49), and the secreted virulent protein of Yersinia, YopH, binds to p130cas as a substrate (6).…”

Section: Discussionmentioning

confidence: 99%

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Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABA_A receptor and dysregulation of p130cas phosphorylation

Shiratsuchi

Kouatli

et al. 2009

American Journal of Physiology-Cell Physiology

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Surgical stress and anesthesia result in systemic immunosuppression. Propofol, a commonly used anesthetic agent, alters immune cell functions. Previously, we demonstrated that extracellular pressure increases macrophage phagocytosis. We hypothesized that propofol might influence pressure-induced macrophage phagocytosis in monocytes from patients undergoing surgery. Pressure (20 mmHg above ambient pressure) augmented phagocytosis in monocytes from non-propofol-anesthetized patients but reduced phagocytosis in monocytes from propofol-anesthetized patients. In vitro, propofol stimulated phagocytosis but reversed pressure-induced phagocytosis in THP-1 macrophages and monocytes from healthy volunteers. The GABAA receptor antagonists picrotoxin and SR-95531 did not affect basal THP-1 phagocytosis or prevent pressure-stimulated phagocytosis. However, picrotoxin and SR-95531 negated the inhibitory effect of pressure in propofol-treated cells without altering propofol-induced phagocytosis. Phosphorylation of the adaptor protein p130cas was inversely related to phagocytosis: it was inhibited by pressure or propofol but increased by pressure + propofol compared with propofol alone. Reduction of p130cas by small interfering RNA in THP-1 macrophages increased basal phagocytosis and prevented pressure and propofol effects. In conclusion, propofol may alter macrophage responses to pressure via the GABAA receptor and p130cas, whereas pressure also acts via p130cas but independently of GABAA receptors. p130cas may be an important target for modulation of macrophage function in anesthetized patients.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABA_A receptor and dysregulation of p130cas phosphorylation

Shiratsuchi

Kouatli

et al. 2009

American Journal of Physiology-Cell Physiology

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“…In lung adenocarcinoma A549 and SKMES1 cells, x-ray irradiation also induces expression of functional integrin β1 [9]. Furthermore, a signal through the cytoplasmic domains of integrin β1 contributes to cell survival after irradiation [10].…”

Section: Introductionmentioning

confidence: 99%

Integrin β1-dependent invasive migration of irradiation-tolerant human lung adenocarcinoma cells in 3D collagen matrix

Ishihara

Haga

Yasuda

et al. 2010

Biochemical and Biophysical Research Communications

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Radiotherapy is one of the effective therapies used for treating various malignant tumors.However, the emergence of tolerant cells after irradiation remains problematic due to their high metastatic ability, sometimes indicative of poor prognosis. In this study, we showed that subcloned human lung adenocarcinoma cells (A549P-3) that are irradiation-tolerant indicate high invasive activity in vitro, and exhibit an integrin β1 activity-dependent migratory pattern.In collagen gel overlay assay, majority of the A549P-3 cells displayed round morphology and low migration activity, whereas a considerable number of A549P-3IR cells surviving irradiation displayed a spindle morphology and high migration rate. Blocking integrin β1 activity reduced the migration rate of A549P-3IR cells and altered the cell morphology allowing them to assume a round shape. These results suggest that the A549P-3 cells surviving irradiation acquire a highly invasive integrin β1-dependent phenotype, and integrin β1 might be a potentially effective therapeutic target in combination with radiotherapy.

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“…In great similarity to adherent growing cells (Zhang et al, 2002;Cordes and van Beuningen, 2003;Seidler et al, 2005), these events confer resistance to genotoxic agents such as ionizing radiation or drugs like bleomycin, etoposide or fludarabine.…”

Section: Introductionmentioning

confidence: 99%

Integrin-linked kinase interacts with caspase-9 and -8 in an adhesion-dependent manner for promoting radiation-induced apoptosis in human leukemia cells

et al. 2006

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Integrin-mediated adhesion of leukemia cells to extracellular matrix proteins reduces apoptosis following radiation-induced genotoxic injury. To evaluate the role of integrin-linked kinase (ILK) in this process, HL60 human acute promyelocytic leukemia cells were stably transfected with ILK wild-type or kinase-hyperactive overexpression vectors. Suspension or fibronectin (FN) adhesion cultures were irradiated with X-rays and processed for measurement of apoptosis, mitochondrial transmembrane potential and caspase activation. Adhesion to FN pronouncedly reduced radiation-induced apoptosis of HL60 cells and vector controls. Intriguingly, overexpressed ILK enhanced apoptosis after irradiation by combined activation of caspase-3 through caspase-8 and -9 in irradiated FN cultures. Irradiation of ILK suspension cultures lacked caspase-8 activation, but showed serial cleavage of caspase-9, -3 and poly (ADPribose) polymerase. These findings further characterize the cell death-promoting function of ILK in DNAdamaged cells. Moreover, ILK might represent a potential therapeutic target for innovative chemo-and radiooncological approaches in hematological malignancies.

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Interactions of the integrin subunit β1A with protein kinase B/Akt, p130Cas and paxillin contribute to regulation of radiation survival

Cited by 25 publications

References 24 publications

Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABA_A receptor and dysregulation of p130cas phosphorylation

Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABA_A receptor and dysregulation of p130cas phosphorylation

Integrin β1-dependent invasive migration of irradiation-tolerant human lung adenocarcinoma cells in 3D collagen matrix

Integrin-linked kinase interacts with caspase-9 and -8 in an adhesion-dependent manner for promoting radiation-induced apoptosis in human leukemia cells

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Interactions of the integrin subunit β1A with protein kinase B/Akt, p130Cas and paxillin contribute to regulation of radiation survival

Cited by 25 publications

References 24 publications

Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABAA receptor and dysregulation of p130cas phosphorylation

Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABAA receptor and dysregulation of p130cas phosphorylation

Integrin β1-dependent invasive migration of irradiation-tolerant human lung adenocarcinoma cells in 3D collagen matrix

Integrin-linked kinase interacts with caspase-9 and -8 in an adhesion-dependent manner for promoting radiation-induced apoptosis in human leukemia cells

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Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABA_A receptor and dysregulation of p130cas phosphorylation

Propofol inhibits pressure-stimulated macrophage phagocytosis via the GABA_A receptor and dysregulation of p130cas phosphorylation