Only in Titles

           Search results for: Mouse Anti-Troponin-I (Cardiac) Proteins    

paperclip

#28924186   2017/09/19 Save this To Up

Interactome analysis reveals ZNF804A, a schizophrenia risk gene, as a novel component of protein translational machinery critical for embryonic neurodevelopment.

Recent genome-wide association studies identified over 100 genetic loci that significantly associate with schizophrenia (SZ). A top candidate gene, ZNF804A, was robustly replicated in different populations. However, its neural functions are largely unknown. Here we show in mouse that ZFP804A, the homolog of ZNF804A, is required for normal progenitor proliferation and neuronal migration. Using a yeast two-hybrid genome-wide screen, we identified novel interacting proteins of ZNF804A. Rather than transcriptional factors, genes involved in mRNA translation are highly represented in our interactome result. ZNF804A co-fractionates with translational machinery and modulates the translational efficiency as well as the mTOR pathway. The ribosomal protein RPSA interacts with ZNF804A and rescues the migration and translational defects caused by ZNF804A knockdown. RNA immunoprecipitation-RNAseq (RIP-Seq) identified transcripts bound to ZFP804A. Consistently, ZFP804A associates with many short transcripts involved in translational and mitochondrial regulation. Moreover, among the transcripts associated with ZFP804A, a SZ risk gene, neurogranin (NRGN), is one of ZFP804A targets. Interestingly, downregulation of ZFP804A decreases NRGN expression and overexpression of NRGN can ameliorate ZFP804A-mediated migration defect. To verify the downstream targets of ZNF804A, a Duolink in situ interaction assay confirmed genes from our RIP-Seq data as the ZNF804A targets. Thus, our work uncovered a novel mechanistic link of a SZ risk gene to neurodevelopment and translational control. The interactome-driven approach here is an effective way for translating genome-wide association findings into novel biological insights of human diseases.Molecular Psychiatry advance online publication, 19 September 2017; doi:10.1038/mp.2017.166.

1234 related Products with: Interactome analysis reveals ZNF804A, a schizophrenia risk gene, as a novel component of protein translational machinery critical for embryonic neurodevelopment.

Bone Morphogenetic Protei Amplite™ Luciferase Rep Amplite™ Luciferase Rep Amplite™ Luciferase Rep Amplite™ Gaussia Lucife Amplite™ Gaussia Lucife Amplite™ Renilla Lucife Amplite™ Renilla Lucife Amplite™ Renilla Lucife Recombinant Human ASF1A P Recombinant Human ASF1A P Recombinant Human ASF1A P

Related Pathways

paperclip

#28923350   2017/09/19 Save this To Up

Ascorbate starvation alters endoplasmic reticulum-resident enzymes in cardiac fibroblasts, priming them for increased procollagen secretion.

Since ascorbate is unnecessary for cell growth and survival, cardiac fibroblasts are routinely cultured without it. However, ascorbate is necessary for optimal collagen synthesis, so we hypothesized that its presence would influence cell phenotype. Cardiac fibroblasts cultured without ascorbate had increased intracellular levels of procollagens, with procollagen α1(III) showing the largest accumulation. Endoplasmic reticulum (ER)-resident proteins that are known to bind single-stranded procollagens were also elevated. These included the catalytic prolyl 4-hydroxylase subunits, lysyl hydroxylases, and hydroxylysyl galactosyltransferases, with prolyl 4-hydroxylase α1 and α2 (P4HA1 and P4HA2) demonstrating the largest increases. There were no differences in the levels of protein disulfide isomerase (P4HB/PDI) or the triple-helical procollagen chaperone, HSP47, with or without ascorbate. Results were similar with mouse and rat cardiac fibroblasts, suggesting a conserved response. Ascorbate-replete cells that were subsequently deprived of the vitamin lost the ability to secrete intact procollagen α1(I) within ~3days, approximately when intracellular procollagen α1(III) and P4HA1 levels began to rise. Upon ascorbate re-addition, starved fibroblasts initially secreted high levels of procollagen that gradually declined over ~4days, a pattern that was not universal as extra domain A (EDA)-fibronectin secretion was unchanged. Despite the necessity of the P4HA enzymes for triple-helical procollagen formation, they were not responsible for early increased secretion. However, in the absence of ascorbate, P4HA2 overexpression increased intracellular turnover of procollagens, suggesting that it may help clear accumulating procollagens from the ER. Cardiac fibroblasts change in the absence of ascorbate to cope with increased intracellular levels of procollagens. These changes occur slowly and can render the cells phenotypically altered for several days after ascorbate re-addition. These findings have direct implications for the study of cardiac fibroblasts in culture, and may help our understanding of the response of these cells to fluctuating nutrient levels in ischemic myocardium.

2146 related Products with: Ascorbate starvation alters endoplasmic reticulum-resident enzymes in cardiac fibroblasts, priming them for increased procollagen secretion.

stress-associated endopla GLP 1 ELISA Kit, Rat Gluc (7’-Benzyloxy-indolymet Breast invasive ductal ca Multiple lung carcinoma ( Indole 7 carboxaldehyde ( Indole 3 carboxaldehyde ( Indole 6 carboxaldehyde ( Indole 5 carboxaldehyde ( Indole 4 carboxaldehyde ( Anti-BMP-1 (Bone Morphoge Interleukin-34 IL34 (N-t

Related Pathways

paperclip

#28922986   2017/09/19 Save this To Up

Attenuation of doxorubicin-induced cardiotoxicity and genotoxicity by an indole based natural compound 3,3'-diindolylmethane (DIM) through activation of Nrf2/ARE signaling pathways and inhibiting apoptosis.

The most crucial complication related to doxorubicin (DOX) therapy is nonspecific cytotoxic effect on healthy normal cells. The clinical use of this broad-spectrum chemotherapeutic agent is restricted due to development of severe form of cardiotoxicity, myelosuppression and genotoxicity which interfere with therapeutic schedule, compromise treatment outcome and may lead to secondary malignancy. 3,3'-diindolylmethane (DIM) is a naturally occurring plant alkaloid formed by the hydrolysis of indolylmethyl glucosinolate (glucobrassicin). Therefore, the present study was undertaken to investigate the protective role of DIM against DOX-induced toxicity in mice. DOX was administered (5 mg/kg b.W, i.p.) and DIM was administered (25 mg/kg b.W p.o.) in concomitant and 15-day pretreatment schedule. Results showed that DIM significantly attenuated DOX-induced oxidative stress in the cardiac tissues by reducing the levels of free radicals and lipid peroxidation, and by enhancing the level of glutathione (reduced) and the activity of antioxidant enzymes. The chemoprotective potential of DIM was confirmed by histopathological evaluation of heart and bone marrow niche. Moreover, DIM considerably mitigated DOX-induced clastogenicity, DNA damage, apoptosis and myeloid hyperplasia in bone marrow niche. In addition, oral administration of DIM significantly (p<0.05) stimulated the Nrf2-mediated activation of antioxidant response element (ARE) pathway and promoted expression of ARE-driven cytoprotective proteins, HO-1, NQO1 and glutathione-S-transferase (GST). In connection with that, DIM significantly attenuated DOX-induced apoptosis by upregulation of Bcl-2 expression and downregulation of Bax and caspase-3 expression. Thus, this study suggests that DIM has promising chemoprotective efficacy against DOX-induced toxicity and indicates its future use as an adjuvant in chemotherapy.

1903 related Products with: Attenuation of doxorubicin-induced cardiotoxicity and genotoxicity by an indole based natural compound 3,3'-diindolylmethane (DIM) through activation of Nrf2/ARE signaling pathways and inhibiting apoptosis.

Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 AZD-3514 Mechanisms: Andr 17β-Acetoxy-2α-bromo-5 (5α,16β)-N-Acetyl-16-[2 (5α,16β)-N-Acetyl-16-ac 5α-N-Acetyl-2'H-androst- 5α-N-Acetyl-2'H-androst- 3-O-Acetyl 5,14-Androstad

Related Pathways

  •  
  • No related Items
paperclip

#28916335   2017/09/16 Save this To Up

Troxerutin abrogates mitochondrial oxidative stress and myocardial apoptosis in mice fed calorie-rich diet.

Mitochondrial oxidative stress plays a major role in the pathogenesis of myocardial apoptosis in metabolic syndrome (MS) patients. In this study, we investigated the effect of troxerutin (TX), an antioxidant on mitochondrial oxidative stress and apoptotic markers in heart of mice fed fat and fructose-rich diet. Adult male Mus musculus mice were fed either control diet or high fat, high fructose diet (HFFD) for 60 days to induce MS. Mice from each dietary group were divided into two on the 16th day and were either treated or untreated with TX (150 mg/kg bw, p.o) for the next 45 days. At the end of the study, mitochondrial reactive oxygen species (ROS) generation, oxidative stress markers, levels of intracellular calcium, cardiolipin content, cytochrome c release and apoptotic markers were examined in the myocardium. HFFD-feeding resulted in diminution of antioxidants and increased ROS production, lipid peroxidation and oxidatively modified adducts of 8-OHG, 4-HNE and 3-NT. Further increase in Ca(2+) levels, low levels of calcium transporters and decrease in cardiolipin content were noted. Changes in the mitochondrial structure were observed by electron microscopy. Furthermore, cytochrome c release, increase in proapoptotic proteins (APAF-1, BAX, caspases-9 and-3) and decrease in antiapoptotic protein (BCL-2) in HFFD-fed mice suggest myocardial apoptosis. These changes were significantly restored by TX supplementation. TX administration effectively attenuated cardiac apoptosis and exerted a protective role by increasing antioxidant potential and by improving mitochondrial function. Thus, TX could be a promising therapeutic candidate for treating cardiac disease in MS patients.

1800 related Products with: Troxerutin abrogates mitochondrial oxidative stress and myocardial apoptosis in mice fed calorie-rich diet.

OXI TEK (Oxidative Stress Anti beta3 AR Human, Poly 8 Isoprostane oxidative s Apoptosis antibody array Apoptosis Phospho-Specifi Cancer Apoptosis Phospho- Apoptosis (Human) Antibod Apoptosis (Human) Antibod Transcription factors: O Ready to use Apoptosis In Rabbit Anti-Human Apoptos Anti-ARID2(AT-rich intera

Related Pathways

paperclip

#28915917   2017/09/16 Save this To Up

Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function.

Myopathies encompass a wide variety of acquired and hereditary disorders. The pathomechanisms include structural and functional changes affecting, e.g., myofiber metabolism and contractile properties. In this study, we observed increased passive tension (PT) of skinned myofibers from patients with myofibrillar myopathy (MFM) caused by FLNC mutations (MFM-filaminopathy) and limb-girdle muscular dystrophy type-2A due to CAPN3 mutations (LGMD2A), compared to healthy control myofibers. Because the giant protein titin determines myofiber PT, we measured its molecular size and the titin-to-myosin ratio, but found no differences between myopathies and controls. All-titin phosphorylation and site-specific phosphorylation in the PEVK region were reduced in myopathy, which would be predicted to lower PT. Electron microscopy revealed extensive ultrastructural changes in myofibers of various hereditary myopathies and also suggested massive binding of proteins to the sarcomeric I-band region, presumably heat shock proteins (HSPs), which can translocate to elastic titin under stress conditions. Correlative immunofluorescence and immunoelectron microscopy showed that two small HSPs (HSP27 and αB-crystallin) and the ATP-dependent chaperone HSP90 translocated to the titin springs in myopathy. The small HSPs, but not HSP90, were upregulated in myopathic versus control muscles. The titin-binding pattern of chaperones was regularly observed in Duchenne muscular dystrophy (DMD), LGMD2A, MFM-filaminopathy, MFM-myotilinopathy, titinopathy, and inclusion body myopathy due to mutations in valosin-containing protein, but not in acquired sporadic inclusion body myositis. The three HSPs also associated with elastic titin in mouse models of DMD and MFM-filaminopathy. Mechanical measurements on skinned human myofibers incubated with exogenous small HSPs suggested that the elevated PT seen in myopathy is caused, in part, by chaperone-binding to the titin springs. Whereas this interaction may be protective in that it prevents sarcomeric protein aggregation, it also has detrimental effects on sarcomere function. Thus, we identified a novel pathological phenomenon common to many hereditary muscle disorders, which involves sarcomeric alterations.

2218 related Products with: Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function.

FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Interleukin-34 IL34 (N-t Interleukin-34 IL34 anti Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon HIV1 integrase antibody, Shiga Toxin 1 antibody, M

Related Pathways

paperclip

#28914030   2017/09/15 Save this To Up

[Preliminary investigation on mechanism of Naoxintong capsule's preventive treatment of cardio-cerebrovascular disease based on serum proteomics].

Naoxintong capsule has beneficial effects for activating blood circulation, dispersing blood stasis and dredging collateral. It is widely used in the treatment of coronary heart disease, angina pectoris, stroke and cardiovascular disease. However, the pharmacodynamic basis and possible mechanism of its preventive effects are not clear. In this study, 10 male and 10 female C57BL/6 mice were used, and were randomly divided into the control group (saline) and Naoxintong group. Adaptively fed for 7 days in common conditions, mice were given Naoxintong capsule or saline for 3 days via intragastric administration. Serum was collected from 6 mice in each group 1 h after the last administration. Serum proteins were prepared to do two-dimensional gel electrophoresis. Then image analysis and mass spectrometry detection were carried out to screen and identify the differentially expressed proteins and make bioinformatics analysis. It was found that 24 differentially expressed proteins between Naoxintong group and control group. Compared with the control group, 12 proteins were increased, and 12 were decreased. The proteins were involved in apoptosis signal pathway and vascular endothelial growth factor signal transduction pathway, in which vasohibin-1 is a negative feedback regulation factor in angiogenesis. Western blot showed that the expression of vasohibin-1 in Naoxintong group was reduced, which is consistent with the result in two-dimensional electrophoresis. Serum proteins expression is different between Naoxintong and control groups. The targets of these differentially expressed proteins include endothelial cells, inflammatory cells and platelets. The changes on proteins showed that Naoxintong capsule may ameliorate coronary heart disease and ischemic cerebrovascular disease, and provide potential biological markers to prevent ischemic disease.

2499 related Products with: [Preliminary investigation on mechanism of Naoxintong capsule's preventive treatment of cardio-cerebrovascular disease based on serum proteomics].

c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl RAP2C, member of RAS onco DIABETIC DISEASES-Glycate DIABETIC DISEASES Glycate Bcl-2 Oncoprotein; Clone Bcl-2 Oncoprotein; Clone c-erbB-2 Oncoprotein c-erbB-2 Oncoprotein c-erbB-3 Oncoprotein; Cl c-erbB-3 Oncoprotein; Cl

Related Pathways

paperclip

#28904224   2017/09/14 Save this To Up

Targeted inhibition of Gq signaling induces airway relaxation in mouse models of asthma.

Obstructive lung diseases are common causes of disability and death worldwide. A hallmark feature is aberrant activation of Gq protein-dependent signaling cascades. Currently, drugs targeting single G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors (GPCRs) are used to reduce airway tone. However, therapeutic efficacy is often limited, because various GPCRs contribute to bronchoconstriction, and chronic exposure to receptor-activating medications results in desensitization. We therefore hypothesized that pharmacological Gq inhibition could serve as a central mechanism to achieve efficient therapeutic bronchorelaxation. We found that the compound FR900359 (FR), a membrane-permeable inhibitor of Gq, was effective in silencing Gq signaling in murine and human airway smooth muscle cells. Moreover, FR both prevented bronchoconstrictor responses and triggered sustained airway relaxation in mouse, pig, and human airway tissue ex vivo. Inhalation of FR in healthy wild-type mice resulted in high local concentrations of the compound in the lungs and prevented airway constriction without acute effects on blood pressure and heart rate. FR administration also protected against airway hyperreactivity in murine models of allergen sensitization using ovalbumin and house dust mite as allergens. Our findings establish FR as a selective Gq inhibitor when applied locally to the airways of mice in vivo and suggest that pharmacological blockade of Gq proteins may be a useful therapeutic strategy to achieve bronchorelaxation in asthmatic lung disease.

2142 related Products with: Targeted inhibition of Gq signaling induces airway relaxation in mouse models of asthma.

Mouse Anti-Lipoprotein Li Sterile filtered mouse s Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon HIV1 integrase antibody, Goat Anti-Mouse SAR1, (in Goat Anti-Mouse Rab17 (mo Goat Anti-Mouse IA2, (int Goat Anti-Human, Mouse HI Goat Anti-Human FTO (Mous Goat Anti-Human, Mouse EB Goat Anti-Mouse, Rat DLL1

Related Pathways

paperclip

#28901173   2017/09/13 Save this To Up

Cyclin D2 is a critical mediator of exercise-induced cardiac hypertrophy.

A number of signaling pathways underlying pathological cardiac hypertrophy have been identified. However, few studies have probed the functional significance of these signaling pathways in the context of exercise or physiological pathways. Exercise studies were performed on females from six different genetic mouse models that have been shown to exhibit alterations in pathological cardiac adaptation and hypertrophy. These include mice expressing constitutively active glycogen synthase kinase-3β (GSK-3βS9A), an inhibitor of CaMK II (AC3-I), both GSK-3βS9A and AC3-I (GSK-3βS9A/AC3-I), constitutively active Akt (myrAkt), mice deficient in MAPK/ERK kinase kinase-1 (MEKK1(-/-)), and mice deficient in cyclin D2 (cyclin D2(-/-)). Voluntary wheel running performance was similar to NTG littermates for five of the mouse lines. Exercise induced significant cardiac growth in all mouse models except the cyclin D2(-/-) mice. Cardiac function was not impacted in the cyclin D2(-/-) mice and studies using a phospho-antibody array identified six proteins with increased phosphorylation (greater than 150%) and nine proteins with decreased phosphorylation (greater than 33% decrease) in the hearts of exercised cyclin D2(-/-) mice compared to exercised NTG littermate controls. Our results demonstrate that unlike the other hypertrophic signaling molecules tested here, cyclin D2 is an important regulator of both pathologic and physiological hypertrophy. Impact statement This research is relevant as the hypertrophic signaling pathways tested here have only been characterized for their role in pathological hypertrophy, and not in the context of exercise or physiological hypertrophy. By using the same transgenic mouse lines utilized in previous studies, our findings provide a novel and important understanding for the role of these signaling pathways in physiological hypertrophy. We found that alterations in the signaling pathways tested here had no impact on exercise performance. Exercise induced cardiac growth in all of the transgenic mice except for the mice deficient in cyclin D2. In the cyclin D2 null mice, cardiac function was not impacted even though the hypertrophic response was blunted and a number of signaling pathways are differentially regulated by exercise. These data provide the field with an understanding that cyclin D2 is a key mediator of physiological hypertrophy.

1133 related Products with: Cyclin D2 is a critical mediator of exercise-induced cardiac hypertrophy.

Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia Rabbit Anti-Nkx2.5 Cardia

Related Pathways

paperclip

#28899419   2017/09/13 Save this To Up

Increased plasma lipid levels exacerbate muscle pathology in the mdx mouse model of Duchenne muscular dystrophy.

Duchenne muscular dystrophy (DMD) is caused by loss of dystrophin expression and leads to severe ambulatory and cardiac function decline. However, the dystrophin-deficient mdx murine model of DMD only develops a very mild form of the disease. Our group and others have shown vascular abnormalities in animal models of MD, a likely consequence of the fact that blood vessels express the same dystrophin-associated glycoprotein complex (DGC) proteins as skeletal muscles.

2030 related Products with: Increased plasma lipid levels exacerbate muscle pathology in the mdx mouse model of Duchenne muscular dystrophy.

Multiple organ tumor tiss Sterile filtered mouse s Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon HIV1 integrase antibody, Goat Anti-Mouse SAR1, (in Goat Anti-Mouse Rab17 (mo Goat Anti-Mouse IA2, (int Goat Anti-Human, Mouse HI Goat Anti-Human FTO (Mous Goat Anti-Human, Mouse EB Goat Anti-Mouse, Rat DLL1

Related Pathways

paperclip

#28892929   2017/09/12 Save this To Up

Connective Tissue Growth Factor Transgenic Mouse Develops Cardiac Hypertrophy, Lean Body Mass and Alopecia.

Connective Tissue Growth Factor (CTGF/CCN2) is one of the six members of cysteine-rich, heparin-binding proteins, secreted as modular protein and recognised to play a major function in cell processes such as adhesion, migration, proliferation and differentiation as well as chondrogenesis, skeletogenesis, angiogenesis and wound healing. The capacity of CTGF to interact with different growth factors lends an important role during early and late development, especially in the anterior region of the embryo. CTGF Knockout (KO) mice have several craniofacial defects and bone miss shaped due to an impairment of the vascular system development during chondrogenesis.

1587 related Products with: Connective Tissue Growth Factor Transgenic Mouse Develops Cardiac Hypertrophy, Lean Body Mass and Alopecia.

Human Connective Tissue G Human, Connective Tissue Mouse Insulin-like Growth Mouse Nerve Growth Factor Mouse Fibroblast Growth F Mouse Fibroblast Growth F Mouse Vascular Endothelia Mouse Fibroblast Growth F Mouse Vascular Endothelia Mouse Epidermal Growth Fa Mouse Platelet Derived Gr Mouse Platelet Derived Gr

Related Pathways