Search results for: p21ARC




Aging-Associated Changes in Oxidative Stress Negatively Impacts the Urinary Bladder Urothelium.
Lower urinary tract symptoms are known to significantly increase with age, negatively impacting quality of life and self-reliance. The urothelium fulfills crucial tasks, serving as a barrier protecting the underlying bladder tissue from the harsh chemical composition of urine, and exhibits signaling properties via the release of mediators within the bladder wall that affect bladder functioning. Aging is associated with detrimental changes in cellular health, in part by increasing oxidative stress in the bladder mucosa, and more specifically the urothelium. This, in turn, may impact urothelial mitochondrial health and bioenergetics.Mathijs M de Rijk, Amanda Wolf-Johnston, Aura F Kullmann, Stephanie Taiclet, Anthony J Kanai, Sruti Shiva, Lori A Birder
1875 related Products with: Aging-Associated Changes in Oxidative Stress Negatively Impacts the Urinary Bladder Urothelium.
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The tomato Arp2/3 complex is required for resistance to the powdery mildew fungus Oidium neolycopersici.
The actin-related protein 2/3 complex (Arp2/3 complex), a key regulator of actin cytoskeletal dynamics, has been linked to multiple cellular processes, including those associated with response to stress. Herein, the Solanum habrochaites ARPC3 gene, encoding a subunit protein of the Arp2/3 complex, was identified and characterized. ShARPC3 encodes a 174-amino acid protein possessing a conserved P21-Arc domain. Silencing of ShARPC3 resulted in enhanced susceptibility to the powdery mildew pathogen Oidium neolycopersici (On-Lz), demonstrating a role for ShARPC3 in defence signalling. Interestingly, a loss of ShARPC3 coincided with enhanced susceptibility to On-Lz, a process that we hypothesize is the result of a block in the activity of SA-mediated defence signalling. Conversely, overexpression of ShARPC3 in Arabidopsis thaliana, followed by inoculation with On-Lz, showed enhanced resistance, including the rapid induction of hypersensitive cell death and the generation of reactive oxygen. Heterologous expression of ShARPC3 in the arc18 mutant of Saccharomyces cerevisiae (i.e., ∆arc18) resulted in complementation of stress-induced phenotypes, including high-temperature tolerance. Taken together, these data support a role for ShARPC3 in tomato through positive regulation of plant immunity in response to O. neolycopersici pathogenesis.Guangzheng Sun, Chanjing Feng, Jia Guo, Ancheng Zhang, Yuanliu Xu, Yang Wang, Brad Day, Qing Ma
2055 related Products with: The tomato Arp2/3 complex is required for resistance to the powdery mildew fungus Oidium neolycopersici.
1 ml100ug Lyophilized200 ug100ug Lyophilized100ug Lyophilized0.25 mg100ug Lyophilized
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Identification of salivary protein biomarkers for orthodontically induced inflammatory root resorption.
Orthodontically induced inflammatory root resorption (OIIRR) is one of the most prevalent and unavoidable consequence of orthodontic tooth movement. The aim of this study was to discover potential diagnostic protein biomarkers for detection of OIIRR in whole saliva (WS).Karolina Elżbieta Kaczor-Urbanowicz, Omer Deutsch, Batia Zaks, Guy Krief, Stella Chaushu, Aaron Palmon
2977 related Products with: Identification of salivary protein biomarkers for orthodontically induced inflammatory root resorption.
2ug5ug100μg10ìg100 mg5ug2ug5ug10 mg100ug2ug1 mg
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Role of End Binding Protein-1 in endothelial permeability response to barrier-disruptive and barrier-enhancing agonists.
Rapid changes in microtubule (MT) polymerization dynamics affect regional activity of small GTPases RhoA and Rac1, which play a key role in the regulation of actin cytoskeleton and endothelial cell (EC) permeability. This study tested the role of End Binding Protein-1 (EB1) in the mechanisms of increased and decreased EC permeability caused by thrombin and hepatocyte growth factor (HGF) and mediated by RhoA and Rac1 GTPases, respectively. Stimulation of human lung EC with thrombin inhibited peripheral MT growth, which was monitored by morphological and biochemical evaluation of peripheral MT and the levels of stabilized MT. In contrast, stimulation of EC with HGF promoted peripheral MT growth and protrusion of EB1-positive MT plus ends to the EC peripheral submembrane area. EB1 knockdown by small interfering RNA did not affect partial MT depolymerization, activation of Rho signaling, and permeability response to thrombin, but suppressed the HGF-induced endothelial barrier enhancement. EB1 knockdown suppressed HGF-induced activation of Rac1 and Rac1 cytoskeletal effectors cortactin and PAK1, impaired HGF-induced assembly of cortical cytoskeleton regulatory complex (WAVE-p21Arc-IQGAP1), and blocked HGF-induced enhancement of peripheral actin cytoskeleton and VE-cadherin-positive adherens junctions. Altogether, these data demonstrate a role for EB1 in coordination of MT-dependent barrier enhancement response to HGF, but show no involvement of EB1 in acute increase of EC permeability caused by the barrier disruptive agonist. The results suggest that increased peripheral EB1 distribution is a critical component of the Rac1-mediated pathway and peripheral cytoskeletal remodeling essential for agonist-induced EC barrier enhancement.Xinyong Tian, Tomomi Ohmura, Alok S Shah, Sophia Son, Yufeng Tian, Anna A Birukova
1983 related Products with: Role of End Binding Protein-1 in endothelial permeability response to barrier-disruptive and barrier-enhancing agonists.
1000 TESTS/0.65ml100ul100μg100ug Lyophilized100ug Lyophilized100ug Lyophilized96 tests1.00 flask100ug Lyophilized100ug Lyophilized3840 (in case - Racked - 100ug Lyophilized
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Effects of acute and repeated cocaine on markers for neural plasticity within the mesolimbic system in rats.
Repeated cocaine is known to induce morphological changes in dopaminergic circuits that are known to participate on cocaine-induced addictive changes.Nieves Rodriguez-Espinosa, Emilio Fernandez-Espejo
1436 related Products with: Effects of acute and repeated cocaine on markers for neural plasticity within the mesolimbic system in rats.
100 G250 mg100ug 1 G 1 G 50 UG
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Antiparkinsonian trophic action of glial cell line-derived neurotrophic factor and transforming growth factor β1 is enhanced after co-infusion in rats.
The objective was to analyze functional effects of the combination of GDNF and TGF-β1 in the retrograde model of Parkinsonism in rats, based on the intrastriatal infusion of 6-hydroxydopamine, which leads to protracted and progressive cell death in the substantia nigra. Hemiparkinsonian rats were implanted with osmotic minipumps 2 months after striatal lesion, pumps delivering GDNF alone (10 ng/day), TGF-β1 alone (2 ng/day), or a GDNF and TGF-β1 combination. The findings confirmed that GDNF alone has potent dopaminotrophic effects but they also revealed, for the first time, that GDNF and TGF-β1 co-infusion led to stronger trophic effects relative to the infusion of GDNF alone. TGF-β1 allowed further reducing dopamine receptor hypersensitivity, and potentiated GDNF-mediated effects. This cooperation could be accounted for by the recruitment of GFRα1 on striatal membranes, and by enhanced expression and activation of TH through augmented pSer31TH and pSer40TH. Co-infusion induced striatal sprouting, as revealed by augmentation of p21-Arc, stathmin, and synaptophysin, and led to a reliable recovery of phenotypic expression of TH in surviving nigral neurons. Functional recovery and improvement of TH signal in the nigrostriatal system were long-lasting and sustained, remaining after cessation of trophic infusion.Ramiro Gonzalez-Aparicio, Juan A Flores, Emilio Fernandez-Espejo
1695 related Products with: Antiparkinsonian trophic action of glial cell line-derived neurotrophic factor and transforming growth factor β1 is enhanced after co-infusion in rats.
0.1ml (1mg/ml)112ug2ug10 ug100ug100 µgKit100.00 ug4 Membranes/Box2ug
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Proteomic signatures in laryngeal squamous cell carcinoma.
Laryngeal cancer remains a worldwide health problem. The identification of biomarkers unique to laryngeal cancer may provide new insights into its pathogenesis, as well as provide potential targets for novel therapies and early detection. In order to identify potential biomarkers, we performed a proteomic analysis of laryngeal cancer specimens. Using two-dimensional differential in-gel electrophoresis and mass spectroscopy, protein expression profiles from two laryngeal carcinoma specimens and corresponding adjacent normal tissue were analyzed. The results of our analysis showed that the expression of a number of proteins was significantly altered in the tumor specimens when compared to matched normal controls. The differentially expressed proteins were identified, and they included stratifin, S100 calcium-binding protein A9, p21-ARC, stathmin, and enolase. With these findings, we have identified potential biomarkers which may contribute to the pathogenesis of laryngeal carcinoma, and which may be suitable as targets for novel therapeutic and/or diagnostic modalities.Duane A Sewell, Chao-Xing Yuan, Erle Robertson
1583 related Products with: Proteomic signatures in laryngeal squamous cell carcinoma.
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Interaction between Tiam1 and the Arp2/3 complex links activation of Rac to actin polymerization.
The Rac-specific GEF (guanine-nucleotide exchange factor) Tiam1 (T-lymphoma invasion and metastasis 1) regulates migration, cell-matrix and cell-cell adhesion by modulating the actin cytoskeleton through the GTPase, Rac1. Using yeast two-hybrid screening and biochemical assays, we found that Tiam1 interacts with the p21-Arc [Arp (actin-related protein) complex] subunit of the Arp2/3 complex. Association occurred through the N-terminal pleckstrin homology domain and the adjacent coiled-coil region of Tiam1. As a result, Tiam1 co-localizes with the Arp2/3 complex at sites of actin polymerization, such as epithelial cell-cell contacts and membrane ruffles. Deletion of the p21-Arc-binding domain in Tiam1 impairs its subcellular localization and capacity to activate Rac1, suggesting that binding to the Arp2/3 complex is important for the function of Tiam1. Indeed, blocking Arp2/3 activation with a WASP (Wiskott-Aldrich syndrome protein) inhibitor leads to subcellular relocalization of Tiam1 and decreased Rac activation. Conversely, functionally active Tiam1, but not a GEF-deficient mutant, promotes activation of the Arp2/3 complex and its association with cytoskeletal components, indicating that Tiam1 and Arp2/3 are mutually dependent for their correct localization and signalling. Our data suggests a model in which the Arp2/3 complex acts as a scaffold to localize Tiam1, and thereby Rac activity, which are both required for activation of the Arp2/3 complex and further Arp2/3 recruitment. This 'self-amplifying' signalling module involving Tiam1, Rac and the Arp2/3 complex could thus drive actin polymerization at specific sites in cells that are required for dynamic morphological changes.Jean Paul Ten Klooster, Eva E Evers, Lennert Janssen, Laura M Machesky, Frits Michiels, Peter Hordijk, John G Collard
2906 related Products with: Interaction between Tiam1 and the Arp2/3 complex links activation of Rac to actin polymerization.
100 mg10 mg500 MG3840 (in case - Racked - 25 G5mg
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Characterization of Arp2/3 complex in chicken tissues.
Arp2/3 protein complex consists of seven subunits (Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20-Arc and p16-Arc) in apparent 1:1 stoichiometry. This complex has been shown to promote the formation of Y-branch structures of F-actin in cultured cells. We generated specific antibodies against chicken Arp2, Arp3, and p34-Arc to analyze the distribution of these subunits in chicken tissues. In whole samples of brain and gizzard, antibodies against each recombinant protein reacted with single bands of predicted molecular mass based on their cDNA sequences of the antigens. Anti-p34-Arc antibody detected at least two neighboring spots in 2D-PAGE, which might suggest the existence of isoforms or modified forms. Arp2/3 complex bound to an F-actin affinity column from gizzard extract. However, Arp2/3 complex did not tightly bind major actin cytoskeleton because the complex was extracted easily when gizzard smooth muscle was homogenized in PBS. Immunoblot analysis of various tissues revealed that the amounts of Arp2/3 subunits were lower in striated muscle than in non-muscle and smooth muscle tissues. Amounts and ratio of the three subunits varied in tissues, as estimated by quantitative immunoblotting. With immunofluorescence microscopy, we also observed localization of Arp3 and p34-Arc in frozen sections of gizzard with different staining patterns around blood vessels. These results suggest that the Arp2/3 complex exists also in places where rapid actin polymerization does not occur, and that a part of the subunits may exist in different forms from the complex containing the seven subunits in some tissues.Asako G Terasaki, Keiko Morikawa, Hiroshi Suzuki, Kohji Oshima, Kazuyo Ohashi
2583 related Products with: Characterization of Arp2/3 complex in chicken tissues.
10mg1 g25 g 25 MG
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Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub.
The Arp2/3 complex is critical for nucleation and crosslinking of actin filaments. To gain insight into its subunit topology and assembly pathway, we systematically examined interactions among subunits of human Arp2/3 complex by yeast two-hybrid assays. It was shown that p20-Arc was able to interact with p21-Arc, p34-Arc, and p16-Arc, respectively. In contrast, p41-Arc only interacted with p20-Arc/p16-Arc heterodimer. In addition, we found that structural integrity was important for association between p20-Arc and p21-Arc, while the N-terminal half of p34-Arc was dispensable for its binding to p20-Arc. Our data suggest a key role of p20-Arc and a multistep pathway for the complex formation.X Zhao, Z Yang, M Qian, X Zhu
2124 related Products with: Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub.
1 kit(96 Wells)30ug100ug Lyophilized1 kit(96 Wells)1 kit(96 Wells)100μl0.1 mg100ug Lyophilized100 ul100μl100ug Lyophilized
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