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#28951871   2017/09/27 Save this To Up

Recombinant Vaccinia Viruses Coding Transgenes of Apoptosis-Inducing Proteins Enhance Apoptosis But Not Immunogenicity of Infected Tumor Cells.

Genetic modifications of the oncolytic vaccinia virus (VV) improve selective tumor cell infection and death, as well as activation of antitumor immunity. We have engineered a double recombinant VV, coding human GM-CSF, and apoptosis-inducing protein apoptin (VV-GMCSF-Apo) for comparing with the earlier constructed double recombinant VV-GMCSF-Lact, coding another apoptosis-inducing protein, lactaptin, which activated different cell death pathways than apoptin. We showed that both these recombinant VVs more considerably activated a set of critical apoptosis markers in infected cells than the recombinant VV coding GM-CSF alone (VV-GMCSF-dGF): these were phosphatidylserine externalization, caspase-3 and caspase-7 activation, DNA fragmentation, and upregulation of proapoptotic protein BAX. However, only VV-GMCSF-Lact efficiently decreased the mitochondrial membrane potential of infected cancer cells. Investigating immunogenic cell death markers in cancer cells infected with recombinant VVs, we demonstrated that all tested recombinant VVs were efficient in calreticulin and HSP70 externalization, decrease of cellular HMGB1, and ATP secretion. The comparison of antitumor activity against advanced MDA-MB-231 tumor revealed that both recombinants VV-GMCSF-Lact and VV-GMCSF-Apo efficiently delay tumor growth. Our results demonstrate that the composition of GM-CSF and apoptosis-inducing proteins in the VV genome is very efficient tool for specific killing of cancer cells and for activation of antitumor immunity.

1742 related Products with: Recombinant Vaccinia Viruses Coding Transgenes of Apoptosis-Inducing Proteins Enhance Apoptosis But Not Immunogenicity of Infected Tumor Cells.

Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant Human HGF [fr Recombinant Human HGF [fr Recombinant Human HGF [fr Recombinant Human IL-4 [f Recombinant Human IL-6 (I Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Human OPG TNF

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#27233218   2016/07/10 Save this To Up

Up-regulation of activating transcription factor 4 induces severe loss of dopamine nigral neurons in a rat model of Parkinson's disease.

Activating transcription factor 4 (ATF4) is a member of the PERK signaling pathway, which directly binds endoplasmic reticulum stress target genes and plays a crucial role in both adaptations to stress and activation of apoptosis. Previous publications demonstrated conflicting evidence on the role of ATF4 in the pathogenesis of neurodegenerative disorders. In this study, we used recombinant adeno-associate virus (rAAV)-mediated gene transfer to investigate if the sustained up-regulation of ATF4 launches a pro-survival or pro-death trend in the dopamine (DA) cells of the substantia nigra pars compacta in a rat model of Parkinson-like neurodegeneration induced by human alpha-synuclein (αS) overexpression. We showed that ATF4 does not protect nigral DA neurons against an αS-induced pathology. Moreover, the rAAV-mediated overexpression of ATF4 resulted in severe nigra-striatal degeneration via activation of caspases 3/7.

1491 related Products with: Up-regulation of activating transcription factor 4 induces severe loss of dopamine nigral neurons in a rat model of Parkinson's disease.

Beta Amyloid (42) ELISA K Beta Amyloid (40) ELISA K Beta Amyloid (1 40) ELISA Beta Amyloid (1 40) ELISA Growth Factor (Human) Ant Liver disease spectrum ti Kidney disease spectrum ( Breast disease spectrum t Breast disease spectrum t Cervical intraepithelial Lung disease spectrum tis DNA (cytosine 5) methyltr

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#27230238   2016/05/27 Save this To Up

RhBMP-2 Activates Hippo Signaling through RASSF1 in Esophageal Cancer Cells.

Despite that recombinant human bone morphogenetic protein-2 (rhBMP-2) has been reported as a stimulatory effecter of cancer cell growth because of its characteristic like morphogen, the biological functions of rhBMP-2 in human esophageal cancer cells are unknown. The purpose of this study was to investigate whether rhBMP-2 has an inhibitory effect on the growth of human esophageal squamous carcinoma cells (ESCC). RhBMP-2 significantly inhibited proliferation of ESCC cells in a dose-dependent manner in the MTT assay. Cell cycle arrest at the G1 phase was induced 24 h after rhBMP2 treatment. RhBMP-2 also reduced cyclin D1, cyclin-dependent kinase (CDK) 4 and CDK 6 activities, and stimulated p-Smad1/5/8, p53, and p21 levels at 12 h. In contrast, rhBMP-2 diminished poly (ADP-ribose) polymerase (PARP) protein expression levels and activated cleaved PARP, cleaved caspase-7, and cleaved-caspase 9 levels in ESCC cells. In addition, rhBMP-2 increased MST1, MOB1, and p-YAP protein levels and the RASSF1 binds Mst1 more upon treatment with rhBMP2. The induced p-YAP expression in TE-8 and TE-12 cells by rhBMP-2 was reversed by the RASSF1 knockdown. In vivo study, rhBMP-2 decreased tumor volume following subcutaneous implantation and showed higher radiologic score (less bony destruction) after femoral implantation compared to those in a control group. These results suggest that rhBMP-2 inhibits rather than activates proliferation of human esophageal cancer cells which is mediated through activating the hippo signaling pathway.

1228 related Products with: RhBMP-2 Activates Hippo Signaling through RASSF1 in Esophageal Cancer Cells.

High density esophageal c Esophageal cancer tissue Esophageal cancer test ti Esophageal cancer test ti AKT PKB Signaling Phospho ErbB Her Signaling Phosph ERK Signaling Phospho-Spe IGF-1R Signaling Phospho- NF-kB II Phospho-Specific Lung cancer tissue array, Colon cancer and normal t Prostate cancer, adjacent

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#26884715   2016/02/17 Save this To Up

Caspase-3/7-mediated Cleavage of β2-spectrin is Required for Acetaminophen-induced Liver Damage.

The ubiquitously expressed β2-spectrin (β2SP, SPTBN1) is the most common non-erythrocytic member of the β-spectrin gene family. Loss of β2-spectrin leads to defects in liver development, and its haploinsufficiency spontaneously leads to chronic liver disease and the eventual development of hepatocellular cancer. However, the specific role of β2-spectrin in liver homeostasis remains to be elucidated. Here, we reported that β2-spectrin was cleaved by caspase-3/7 upon treatment with acetaminophen which is the main cause of acute liver injury. Blockage of β2-spectrin cleavage robustly attenuated β2-spectrin-specific functions, including regulation of the cell cycle, apoptosis, and transcription. Cleaved fragments of β2-spectrin were physiologically active, and the N- and C-terminal fragments retained discrete interaction partners and activity in transcriptional regulation and apoptosis, respectively. Cleavage of β2-spectrin facilitated the redistribution of the resulting fragments under conditions of liver damage induced by acetaminophen. In contrast, downregulation of β2-spectrin led to resistance to acetaminophen-induced cytotoxicity, and its insufficiency in the liver promoted suppression of acetaminophen-induced liver damage and enhancement of liver regeneration.

2569 related Products with: Caspase-3/7-mediated Cleavage of β2-spectrin is Required for Acetaminophen-induced Liver Damage.

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#26755661   2016/03/21 Save this To Up

Axon guidance molecule semaphorin3A is a novel tumor suppressor in head and neck squamous cell carcinoma.

Semaphorin3A (SEMA3A), an axon guidance molecule in the nervous system, plays an inhibitory role in oncogenesis. Here, we investigated the expression pattern and biological roles of SEMA3A in head and neck squamous cell carcinoma (HNSCC) by gain-of-function assays using adenovirus transfection and recombinant human SEMA3A protein. In addition, we explored the therapeutic efficacy of SEMA3A against HNSCC in vivo. We found that lower expression of SEMA3A correlated with shorter overall survival and had independent prognostic importance in patients with HNSCC. Both genetic and recombinant SEMA3A protein inhibited cell proliferation and colony formation and induced apoptosis, accompanied by decreased cyclin E, cyclin D, CDK2, CDK4 and CDK6 and increased P21, P27, activated caspase-5 and caspase-7. Moreover, over-expression of SEMA3A suppressed migration, invasion and epithelial-to-mesenchymal transition due in part to the inhibition of NF-κB and SNAI2 in HNSCC cell lines. Furthermore, intratumoral SEMA3A delivery significantly stagnated tumor growth in a xenograft model. Taken together, our results indicate that SEMA3A serves as a tumor suppressor during HNSCC tumorigenesis and a new target for the treatment of HNSCC.

1552 related Products with: Axon guidance molecule semaphorin3A is a novel tumor suppressor in head and neck squamous cell carcinoma.

Head and neck squamous ce Multiple head and neck sq Lung squamous cell carcin Skin malignant tumor tiss Cervix squamous cell carc Esophagus squamous cell c Esophagus squamous cell c Esophageal squamous cell Esophagus squamous cell c Esophageal squamous cell Multiple head and neck tu Head and neck squamous ca

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#26457789   2015/11/28 Save this To Up

Pro-nerve growth factor in the ovary and human granulosa cells.

Pro-nerve growth factor must be cleaved to generate mature NGF, which was suggested to be a factor involved in ovarian physiology and pathology. Extracellular proNGF can induce cell death in many tissues. Whether extracellular proNGF exists in the ovary and may play a role in the death of follicular cells or atresia was unknown.

1946 related Products with: Pro-nerve growth factor in the ovary and human granulosa cells.

Epidermal Growth Factor ( Epidermal Growth Factor ( Human Insulin-like Growth Human Insulin-like Growth Human Nerve Growth Factor Macrophage Colony Stimula Macrophage Colony Stimula Growth Factor (Human) Ant Goat Anti-Human Fibroblas Human Insulin-like Growth Epidermal Growth Factor ( Epidermal Growth Factor (

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#26317656   2015/08/31 Save this To Up

An Engineered Split Intein for Photoactivated Protein Trans-Splicing.

Protein splicing is mediated by inteins that auto-catalytically join two separated protein fragments with a peptide bond. Here we engineered a genetically encoded synthetic photoactivatable intein (named LOVInC), by using the light-sensitive LOV2 domain from Avena sativa as a switch to modulate the splicing activity of the split DnaE intein from Nostoc punctiforme. Periodic blue light illumination of LOVInC induced protein splicing activity in mammalian cells. To demonstrate the broad applicability of LOVInC, synthetic protein systems were engineered for the light-induced reassembly of several target proteins such as fluorescent protein markers, a dominant positive mutant of RhoA, caspase-7, and the genetically encoded Ca2+ indicator GCaMP2. Spatial precision of LOVInC was demonstrated by targeting activity to specific mammalian cells. Thus, LOVInC can serve as a general platform for engineering light-based control for modulating the activity of many different proteins.

2723 related Products with: An Engineered Split Intein for Photoactivated Protein Trans-Splicing.

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#26268696   2015/09/04 Save this To Up

TMEM33: a new stress-inducible endoplasmic reticulum transmembrane protein and modulator of the unfolded protein response signaling.

Endoplasmic reticulum (ER) stress leads to activation of the unfolded protein response (UPR) signaling cascade and induction of an apoptotic cell death, autophagy, oncogenesis, metastasis, and/or resistance to cancer therapies. Mechanisms underlying regulation of ER transmembrane proteins PERK, IRE1α, and ATF6α/β, and how the balance of these activities determines outcome of the activated UPR, remain largely unclear. Here, we report a novel molecule transmembrane protein 33 (TMEM33) and its actions in UPR signaling. Immunoblotting and northern blot hybridization assays were used to determine the effects of ER stress on TMEM33 expression levels in various cell lines. Transient transfections, immunofluorescence, subcellular fractionation, immunoprecipitation, and immunoblotting were used to study the subcellular localization of TMEM33, the binding partners of TMEM33, and the expression of downstream effectors of PERK and IRE1α. Our data demonstrate that TMEM33 is a unique ER stress-inducible and ER transmembrane molecule, and a new binding partner of PERK. Exogenous expression of TMEM33 led to increased expression of p-eIF2α and p-IRE1α and their known downstream effectors, ATF4-CHOP and XBP1-S, respectively, in breast cancer cells. TMEM33 overexpression also correlated with increased expression of apoptotic signals including cleaved caspase-7 and cleaved PARP, and an autophagosome protein LC3II, and reduced expression of the autophagy marker p62. TMEM33 is a novel regulator of the PERK-eIE2α-ATF4 and IRE1-XBP1 axes of the UPR signaling. Therefore, TMEM33 may function as a determinant of the ER stress-responsive events in cancer cells.

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stress-associated endopla Transmembrane protein 147 transmembrane emp24 prote Rabbit Anti-Rat Androgen Goat Anti- Transmembrane CD40 Ligand protein CD40 Recombinant Human Androge Glial Fibrillary Acidic Glial Fibrillary Acidic Glial Fibrillary Acidic Acyl CoA binding Protein G protein subunit alpha 1

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#26057632   2015/09/15 Save this To Up

Distinct effects of TRAIL on the mitochondrial network in human cancer cells and normal cells: role of plasma membrane depolarization.

Apo2 ligand/tumor necrosis factor-related apoptosis-inducing ligand (Apo2L/TRAIL) is a promising anticancer drug due to its tumor-selective cytotoxicity. Here we report that TRAIL exhibits distinct effects on the mitochondrial networks in malignant cells and normal cells. Live-cell imaging revealed that multiple human cancer cell lines and normal cells exhibited two different modes of mitochondrial responses in response to TRAIL and death receptor agonists. Mitochondria within tumor cells became fragmented into punctate and clustered in response to toxic stimuli. The mitochondrial fragmentation was observed at 4 h, then became more pronounced over time, and associated with apoptotic cell death. In contrast, mitochondria within normal cells such as melanocytes and fibroblasts became only modestly truncated, even when they were treated with toxic stimuli. Although TRAIL activated dynamin-related protein 1 (Drp1)-dependent mitochondrial fission, inhibition of this process by Drp1 knockdown or with the Drp1 inhibitor mdivi-1, potentiated TRAIL-induced apoptosis, mitochondrial fragmentation, and clustering. Moreover, mitochondrial reactive oxygen species (ROS)-mediated depolarization accelerated mitochondrial network abnormalities in tumor cells, but not in normal cells, and TRAIL caused higher levels of mitochondrial ROS accumulation and depolarization in malignant cells than in normal cells. Our findings suggest that tumor cells are more prone than normal cells to oxidative stress and depolarization, thereby being more vulnerable to mitochondrial network abnormalities and that this vulnerability may be relevant to the tumor-targeting killing by TRAIL.

1299 related Products with: Distinct effects of TRAIL on the mitochondrial network in human cancer cells and normal cells: role of plasma membrane depolarization.

Plasma Membrane GFP Tag H Epidermal Growth Factor ( Epidermal Growth Factor ( Macrophage Colony Stimula Macrophage Colony Stimula anti CD38 Hematopoietic p Human Small Intestine Mic Human Large Intestine Mic Human Internal Mammary Ar GFP Expressing Human Inte Octyl â D 1 thioglucopyr Anti C Reactive Protein A

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#25882870   2015/08/10 Save this To Up

Involvement of smad2 and Erk/Akt cascade in TGF-β1-induced apoptosis in human gingival epithelial cells.

Periodontitis is the most prevalent infectious disease caused by periodontopathic bacteria and is also a chronic inflammatory disease. Gingival crevicular fluid (GCF) is an inflammatory exudate that seeps into the gingival crevices or periodontal pockets around teeth with inflamed gingiva, and contains various materials including leukocytes and cytokines. Since gingival epithelial cells, which form a barrier against bacterial challenges, are affected by GCF, cytokines or other materials contained within GCF are engaged in the maintenance and disruption of the epithelial barrier. Accordingly, its compositional pattern has been employed as a reliable objective index of local inflammation. Transforming growth factor β1 (TGF-β1) levels in GCF were previously shown to be markedly higher in patients with periodontitis than in healthy subject. However, it currently remains unclear how TGF-β1 affects gingival epithelial cell growth or apoptosis; therefore, elucidating the mechanism responsible may lead to a deeper understanding of pathogenic periodontitis. In the present study, the human gingival epithelial cell line, OBA9 cells were stimulated with recombinant TGF-β1. Apoptosis-related protein levels were determined by Western blotting. Caspase-3/7 activity was measured with a Caspase-Glo assay kit. Surviving and apoptotic cells were detected using an MTS assay and TUNEL staining, respectively. TGF-βRI siRNA and smad2 siRNA were transfected into cells using the lipofectamine RNAiMAX reagent. TGF-β1 elevated caspase-3 activity and the number of TUNEL-positive apoptotic cells in OBA9 cells. Furthermore, while the levels of the pro-apoptotic proteins Bax, Bak, Bim, and Bad were increased in OBA9 cells stimulated with TGF-β1, the TGF-β1 treatment also decreased the levels of anti-apoptotic proteins such as Bcl-2 and Bcl-xL in a time-dependent manner. Additionally, TGF-β1 up-regulated the protein levels of cleaved caspase-9. These results indicated that TGF-β1-induced apoptosis was involved in a mitochondria-related intrinsic pathway. TGF-β1 phosphorylated smad2 in OBA9 cells and this phosphorylation was clearly reduced by SB431542 (a TGF-β type I receptor inhibitor). Consistent with this result, SB431542 or smad2 siRNA-induced reductions in smad2 protein expression levels attenuated TGF-β1-induced apoptosis. On the other hand, the ligation of TGF-β1 on its receptor also stimulated the phosphorylation of Erk and Akt, which are smad2-independent pathways. However, the inhibition of Erk/Akt signaling pathways by U0126, a MEK-Erk inhibitor and LY294002, a PI3Kinase-Akt inhibitor, augmented TGF-β1-induced apoptosis in OBA9 cells. Taken together, the results of present study demonstrated that TGF-β1 activated both the smad2 and Erk/Akt cascades via its receptor on gingival epithelial cells, even though these two pathways have opposite roles in cell death and survival, and the culmination of these signaling events induced mitochondria-dependent apoptosis in gingival epithelial cells. Based on the results of the present study, we herein proposed for the first time, that TGF-β1 is a novel target cytokine for monitoring the progression of periodontal disease.

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