Role of gelsolin in cell proliferation and invasion of human hepatocellular carcinoma cells

Deng, Bingbing; Fang, Jie; Zhang, Xiaofei; Qu, Lei; Cao, Zhongwei; Wang, Bin

doi:10.1016/j.gene.2015.06.083

Cited by 21 publications

(16 citation statements)

References 29 publications

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“…Inhibition of EZR expression reduced adhesiveness in colorectal cancer cells [43]. GSN knockdown decreased cell viability and tumor cell invasion, whereas GSN overexpression correlates with proliferative and invasive capacities [44]. BSG promotes cell–cell adhesion, and its downregulation altered the actin/Spectrin network [45].…”

Section: Discussionmentioning

confidence: 99%

Rapamycin regulates autophagy and cell adhesion in induced pluripotent stem cells

et al. 2016

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BackgroundCellular reprogramming is a stressful process, which requires cells to engulf somatic features and produce and maintain stemness machineries. Autophagy is a process to degrade unwanted proteins and is required for the derivation of induced pluripotent stem cells (iPSCs). However, the role of autophagy during iPSC maintenance remains undefined.MethodsHuman iPSCs were investigated by microscopy, immunofluorescence, and immunoblotting to detect autophagy machinery. Cells were treated with rapamycin to activate autophagy and with bafilomycin to block autophagy during iPSC maintenance. High concentrations of rapamycin treatment unexpectedly resulted in spontaneous formation of round floating spheres of uniform size, which were analyzed for differentiation into three germ layers. Mass spectrometry was deployed to reveal altered protein expression and pathways associated with rapamycin treatment.ResultsWe demonstrate that human iPSCs express high basal levels of autophagy, including key components of APMKα, ULK1/2, BECLIN-1, ATG13, ATG101, ATG12, ATG3, ATG5, and LC3B. Block of autophagy by bafilomycin induces iPSC death and rapamycin attenuates the bafilomycin effect. Rapamycin treatment upregulates autophagy in iPSCs in a dose/time-dependent manner. High concentration of rapamycin reduces NANOG expression and induces spontaneous formation of round and uniformly sized embryoid bodies (EBs) with accelerated differentiation into three germ layers. Mass spectrometry analysis identifies actin cytoskeleton and adherens junctions as the major targets of rapamycin in mediating iPSC detachment and differentiation.ConclusionsHigh levels of basal autophagy activity are present during iPSC derivation and maintenance. Rapamycin alters expression of actin cytoskeleton and adherens junctions, induces uniform EB formation, and accelerates differentiation. IPSCs are sensitive to enzyme dissociation and require a lengthy differentiation time. The shape and size of EBs also play a role in the heterogeneity of end cell products. This research therefore highlights the potential of rapamycin in producing uniform EBs and in shortening iPSC differentiation duration.Electronic supplementary materialThe online version of this article (doi:10.1186/s13287-016-0425-x) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Rapamycin regulates autophagy and cell adhesion in induced pluripotent stem cells

et al. 2016

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“…The RAW264.7 cells were cultured in Dulbecco’s Modified Eagle Medium (Life Technologies, Inc, Gaithersburg, MD, USA) containing 10% fetal bovine serum (Life Technologies), 100 U/ml of penicillin G, and 100 µg/ml streptomycin at 37 °C in a water-saturated atmosphere of 5% CO 2 [20]. …”

Section: Methodsmentioning

confidence: 99%

Gelsolin Inhibits the Inflammatory Process Induced by LPS

Cheng

Liu

et al. 2017

Cell Physiol Biochem

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Background/Aims: Endotoxemia is a life-threatening situation that signifies a key challenge in the field of intensive care medicine. Proinflammatory mediators produced by macrophages play a key role in endotoxemia. Gelsolin (GSN) is involved in the process of inflammation. Methods: IL-6 and TNF-α in the supernatant were measured with an ELISA kit. NO production was assessed by measurement of nitrite concentration with the Griess assay. si-RNA directed against GSN (si-GSN) was transfected by Lipofectamine. Results: LPS decreased the levels of GSN. Recombinant GSN inhibited the cytokines induced by LPS and rescued mice from LPS-induced death, and si-GSN increased death in the LPS-pretreated mice. Conclusion: GSN exhibited a protective role in endotoxemia.

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“…9 Accumulating evidence indicates a link between gelsolin and tumor progression. For instance, Deng et al 10 reported that gelsolin is upregulated in human hepatocellular carcinoma (HCC) tissues, and overexpression of gelsolin promotes the proliferation and invasion of HCC cells. An adverse correlation between gelsolin expression and patient survival was noted in NSCLC, [11][12][13] implying an important role for gelsolin in tumor progression.…”

Section: Introductionmentioning

confidence: 99%

Gelsolin Promotes Radioresistance in Non–Small Cell Lung Cancer Cells Through Activation of Phosphoinositide 3-Kinase/Akt Signaling

Zhao

Wang

et al. 2016

Technol Cancer Res Treat

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Gelsolin is an actin-binding protein and acts as an important regulator of cell survival. This study aimed to determine the function of gelsolin in the radioresistance of non-small cell lung cancer cells. We examined the expression of gelsolin in radioresistant A549 and H460 cells and their parental cells. The effects of gelsolin overexpression and knockdown on the clonogenic survival and apoptosis of non-small cell lung cancer cells after irradiation were studied. The involvement of phosphoinositide 3-kinase/Akt signaling in the action of gelsolin was checked. We found that gelsolin was significantly upregulated in radioresistant A549 and H460 cells. Overexpression of gelsolin significantly (P < .05) increased the number of colonies from irradiated A549 and H460 cells compared to transfection of empty vector. In contrast, knockdown of gelsolin significantly (P < .05) suppressed colony formation after irradiation. Gelsolin-overexpressing cells displayed reduced apoptosis in response to irradiation, which was coupled with decreased levels of cleaved caspase-3 and poly adenosine diphosphate-ribose polymerase. Ectopic expression of gelsolin significantly (P < .05) enhanced the phosphorylation of Akt compared to nontransfected cells. Pretreatment with the phosphoinositide 3-kinase inhibitor LY294002 (20 mmol/L) significantly decreased clonogenic survival and enhanced apoptosis in gelsolin-overexpressing A549 and H460 cells after irradiation. Taken together, gelsolin upregulation promotes radioresistance in non-small cell lung cancer cells, at least partially, through activation of phosphoinositide 3-kinase/Akt signaling.

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Role of gelsolin in cell proliferation and invasion of human hepatocellular carcinoma cells

Cited by 21 publications

References 29 publications

Rapamycin regulates autophagy and cell adhesion in induced pluripotent stem cells

Rapamycin regulates autophagy and cell adhesion in induced pluripotent stem cells

Gelsolin Inhibits the Inflammatory Process Induced by LPS

Gelsolin Promotes Radioresistance in Non–Small Cell Lung Cancer Cells Through Activation of Phosphoinositide 3-Kinase/Akt Signaling

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