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Results: 11 to 20 of 87

Publication Record


Function of death-associated protein 1 in proliferation, differentiation, and apoptosis of chicken satellite cells.
Shin J, McFarland DC, Strasburg GM, Velleman SG
(2013) Muscle Nerve 48: 777-90
MeSH Terms: Animals, Apoptosis, Apoptosis Regulatory Proteins, Cell Differentiation, Cell Proliferation, Cells, Cultured, Chickens, Genetic Vectors, Muscle Development, Muscle, Skeletal, Satellite Cells, Skeletal Muscle, Transfection
Show Abstract · Added March 3, 2014
INTRODUCTION - Muscle growth and regeneration are processes closely associated with proliferation, differentiation, and apoptosis of muscle cells. Death-associated protein 1 (DAP1) has been identified as a negative regulator of autophagy. Little is known about the function of DAP1 in the regulation of myogenesis and satellite cells.
METHODS - Chicken satellite cells were transfected with DAP1 cloned into the pCMS-enhanced green fluorescent protein vector or pcDNA3.1 vector, or a small interference RNA against the endogenous DAP1 gene. The cells were assayed for proliferation, differentiation, and apoptosis.
RESULTS - The overexpression of DAP1 increased proliferation, differentiation, and myotube diameter, but it had no effect on satellite cell apoptosis. In contrast, knockdown of DAP1 significantly decreased proliferation, differentiation, and number of nuclei per myotube, and it increased apoptosis of the cells.
CONCLUSION - DAP1 is required for regulating myogenesis and apoptosis of satellite cells, which may affect muscle mass accretion and regeneration, and ameliorate muscle sarcopenia.
Copyright © 2013 Wiley Periodicals, Inc.
0 Communities
1 Members
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12 MeSH Terms
N-cadherin regulates spatially polarized signals through distinct p120ctn and β-catenin-dependent signalling pathways.
Ouyang M, Lu S, Kim T, Chen CE, Seong J, Leckband DE, Wang F, Reynolds AB, Schwartz MA, Wang Y
(2013) Nat Commun 4: 1589
MeSH Terms: Actin Cytoskeleton, Animals, CHO Cells, Cadherins, Catenins, Cell Polarity, Chickens, Cricetinae, Embryo, Mammalian, Fibroblasts, Fluorescent Dyes, Integrins, Intercellular Junctions, Mice, Models, Biological, Phosphatidylinositol 3-Kinases, Protein Binding, RNA, Small Interfering, Rats, Recombinant Fusion Proteins, Signal Transduction, beta Catenin, rac GTP-Binding Proteins
Show Abstract · Added March 28, 2014
The spatial distribution of molecular signals within cells is crucial for cellular functions. Here, as a model to study the polarized spatial distribution of molecular activities, we used cells on micropatterned strips of fibronectin with one end free and the other end contacting a neighbouring cell. Phosphoinositide 3-kinase and the small GTPase Rac display greater activity at the free end, whereas myosin II light chain and actin filaments are enriched near the intercellular junction. Phosphoinositide 3-kinase and Rac polarization depend specifically on the N-cadherin-p120 catenin complex, whereas myosin II light chain and actin filament polarization depend on the N-cadherin-β-catenin complex. Integrins promote high phosphoinositide 3-kinase/Rac activities at the free end, and the N-cadherin-p120 catenin complex excludes integrin α5 at the junctions to suppress local phosphoinositide 3-kinase and Rac activity. We hence conclude that N-cadherin couples with distinct effectors to polarize phosphoinositide 3-kinase/Rac and myosin II light chain/actin filaments in migrating cells.
1 Communities
1 Members
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23 MeSH Terms
Both genome segments contribute to the pathogenicity of very virulent infectious bursal disease virus.
Escaffre O, Le Nouën C, Amelot M, Ambroggio X, Ogden KM, Guionie O, Toquin D, Müller H, Islam MR, Eterradossi N
(2013) J Virol 87: 2767-80
MeSH Terms: Amino Acid Sequence, Animals, Base Sequence, Birnaviridae Infections, Chick Embryo, Chickens, Infectious bursal disease virus, Molecular Dynamics Simulation, Poultry Diseases, Sequence Analysis, RNA, Spleen, Thymus Gland, Viral Structural Proteins
Show Abstract · Added April 26, 2017
Infectious bursal disease virus (IBDV) causes an economically significant disease of chickens worldwide. Very virulent IBDV (vvIBDV) strains have emerged and induce as much as 60% mortality. The molecular basis for vvIBDV pathogenicity is not understood, and the relative contributions of the two genome segments, A and B, to this phenomenon are not known. Isolate 94432 has been shown previously to be genetically related to vvIBDVs but exhibits atypical antigenicity and does not cause mortality. Here the full-length genome of 94432 was determined, and a reverse genetics system was established. The molecular clone was rescued and exhibited the same antigenicity and reduced pathogenicity as isolate 94432. Genetically modified viruses derived from 94432, whose vvIBDV consensus nucleotide sequence was restored in segment A and/or B, were produced, and their pathogenicity was assessed in specific-pathogen-free chickens. We found that a valine (position 321) that modifies the most exposed part of the capsid protein VP2 critically modified the antigenicity and partially reduced the pathogenicity of 94432. However, a threonine (position 276) located in the finger domain of the virus polymerase (VP1) contributed even more significantly to attenuation. This threonine is partially exposed in a hydrophobic groove on the VP1 surface, suggesting possible interactions between VP1 and another, as yet unidentified molecule at this amino acid position. The restored vvIBDV-like pathogenicity was associated with increased replication and lesions in the thymus and spleen. These results demonstrate that both genome segments influence vvIBDV pathogenicity and may provide new targets for the attenuation of vvIBDVs.
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13 MeSH Terms
A novel angiopoietin-derived peptide displays anti-angiogenic activity and inhibits tumour-induced and retinal neovascularization.
Palmer GM, Tiran Z, Zhou Z, Capozzi ME, Park W, Coletta C, Pyriochou A, Kliger Y, Levy O, Borukhov I, Dewhirst MW, Rotman G, Penn JS, Papapetropoulos A
(2012) Br J Pharmacol 165: 1891-1903
MeSH Terms: Angiogenesis Inhibitors, Angiopoietins, Animals, Cell Movement, Chickens, Chorioallantoic Membrane, Colorectal Neoplasms, Disease Models, Animal, Female, HCT116 Cells, Human Umbilical Vein Endothelial Cells, Humans, Mice, Mice, Nude, Neovascularization, Pathologic, Peptides, Rats, Rats, Sprague-Dawley, Retinal Neovascularization, Xenograft Model Antitumor Assays
Show Abstract · Added October 9, 2013
BACKGROUND AND PURPOSE - Pathological angiogenesis is associated with various human diseases, such as cancer, autoimmune diseases and retinopathy. The angiopoietin (Ang)-Tie2 system plays critical roles in several steps of angiogenic remodelling. Here, we have investigated the anti-angiogenic effect of a novel angiopoietin-derived peptide.
EXPERIMENTAL APPROACH - Using computational methods, we identified peptides from helical segments within angiopoietins, which were predicted to inhibit their activity. These peptides were tested using biochemical methods and models of angiogenesis. The peptide with best efficacy, A11, was selected for further characterization as an anti-angiogenic compound.
KEY RESULTS - The potent anti-angiogenic activity of A11 was demonstrated in a multicellular assay of angiogenesis and in the chorioallantoic membrane model. A11 bound to angiopoietins and reduced the binding of Ang-2 to Tie2. A11 was also significantly reduced vascular density in a model of tumour-induced angiogenesis. Its ability to inhibit Ang-2 but not Ang-1-induced endothelial cell migration, and to down-regulate Tie2 levels in tumour microvessels, suggests that A11 targets the Ang-Tie2 pathway. In a rat model of oxygen-induced retinopathy, A11 strongly inhibited retinal angiogenesis. Moreover, combination of A11 with an anti-VEGF antibody showed a trend for further inhibition of angiogenesis, suggesting an additive effect.
CONCLUSIONS AND IMPLICATIONS - Our results indicate that A11 is a potent anti-angiogenic compound, through modulation of the Ang-Tie2 system, underlining its potential as a therapeutic agent for the treatment of ocular and tumour neovascularization, as well as other pathological conditions that are dependent on angiogenesis.
© 2011 The Authors. British Journal of Pharmacology © 2011 The British Pharmacological Society.
1 Communities
1 Members
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20 MeSH Terms
Development of a spatially offset Raman spectroscopy probe for breast tumor surgical margin evaluation.
Keller MD, Vargis E, de Matos Granja N, Wilson RH, Mycek MA, Kelley MC, Mahadevan-Jansen A
(2011) J Biomed Opt 16: 077006
MeSH Terms: Animals, Breast Neoplasms, Carcinoma, Ductal, Breast, Chickens, Female, Humans, In Vitro Techniques, Mastectomy, Segmental, Models, Statistical, Monte Carlo Method, Optical Phenomena, Signal-To-Noise Ratio, Spectrum Analysis, Raman
Show Abstract · Added March 31, 2014
The risk of local recurrence for breast cancers is strongly correlated with the presence of a tumor within 1 to 2 mm of the surgical margin on the excised specimen. Previous experimental and theoretical results suggest that spatially offset Raman spectroscopy (SORS) holds much promise for intraoperative margin analysis. Based on simulation predictions for signal-to-noise ratio differences among varying spatial offsets, a SORS probe with multiple source-detector offsets was designed and tested. It was then employed to acquire spectra from 35 frozen-thawed breast tissue samples in vitro. Spectra from each detector ring were averaged to create a composite spectrum with biochemical information covering the entire range from the tissue surface to ∼2 mm below the surface, and a probabilistic classification scheme was used to classify these composite spectra as "negative" or "positive" margins. This discrimination was performed with 95% sensitivity and 100% specificity, or with 100% positive predictive value and 94% negative predictive value.
0 Communities
2 Members
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13 MeSH Terms
Matrix sublimation/recrystallization for imaging proteins by mass spectrometry at high spatial resolution.
Yang J, Caprioli RM
(2011) Anal Chem 83: 5728-34
MeSH Terms: Animals, Brain, Brain Chemistry, Chickens, Crystallization, Histological Techniques, Liver, Mice, Proteins, Rats, Sensitivity and Specificity, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Show Abstract · Added March 3, 2020
We have employed matrix deposition by sublimation for protein image analysis on tissue sections using a hydration/recrystallization process that produces high-quality MALDI mass spectra and high-spatial-resolution ion images. We systematically investigated different washing protocols, the effect of tissue section thickness, the amount of sublimated matrix per unit area, and different recrystallization conditions. The results show that an organic solvent rinse followed by ethanol/water rinses substantially increased sensitivity for the detection of proteins. Both the thickness of the tissue section and the amount of sinapinic acid sublimated per unit area have optimal ranges for maximal protein signal intensity. Ion images of mouse and rat brain sections at 50, 20, and 10 μm spatial resolution are presented and are correlated with hematoxylin and eosin (H&E)-stained optical images. For targeted analysis, histology-directed imaging can be performed using this protocol where MS analysis and H&E staining are performed on the same section.
0 Communities
1 Members
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MeSH Terms
Intravital imaging of embryonic and tumor neovasculature using viral nanoparticles.
Leong HS, Steinmetz NF, Ablack A, Destito G, Zijlstra A, Stuhlmann H, Manchester M, Lewis JD
(2010) Nat Protoc 5: 1406-17
MeSH Terms: Animals, Chickens, Comovirus, Embryo Culture Techniques, Embryo, Mammalian, Embryo, Nonmammalian, Endothelium, Vascular, Fabaceae, Fluorescent Dyes, Mice, Microinjections, Microscopy, Confocal, Microscopy, Fluorescence, Nanoparticles, Nanotechnology, Neoplasms
Show Abstract · Added December 30, 2013
Viral nanoparticles are a novel class of biomolecular agents that take advantage of the natural circulatory and targeting properties of viruses to allow the development of therapeutics, vaccines and imaging tools. We have developed a multivalent nanoparticle platform based on the cowpea mosaic virus (CPMV) that facilitates particle labeling at high density with fluorescent dyes and other functional groups. Compared with other technologies, CPMV-based viral nanoparticles are particularly suited for long-term intravital vascular imaging because of their biocompatibility and retention in the endothelium with minimal side effects. The stable, long-term labeling of the endothelium allows the identification of vasculature undergoing active remodeling in real time. In this study, we describe the synthesis, purification and fluorescent labeling of CPMV nanoparticles, along with their use for imaging of vascular structure and for intravital vascular mapping in developmental and tumor angiogenesis models. Dye-labeled viral nanoparticles can be synthesized and purified in a single day, and imaging studies can be conducted over hours, days or weeks, depending on the application.
0 Communities
1 Members
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16 MeSH Terms
An initial map of chromosomal segmental copy number variations in the chicken.
Wang X, Nahashon S, Feaster TK, Bohannon-Stewart A, Adefope N
(2010) BMC Genomics 11: 351
MeSH Terms: Animals, Chickens, Chromosomes, DNA Copy Number Variations, Dogs, Female, Genomics, Humans, Male, Mice, Polymerase Chain Reaction, Rats, Reproducibility of Results
Show Abstract · Added October 23, 2013
BACKGROUND - Chromosomal segmental copy number variation (CNV) has been recently recognized as a very important source of genetic variability. Some CNV loci involve genes or conserved regulatory elements. Compelling evidence indicates that CNVs impact genome functions. The chicken is a very important farm animal species which has also served as a model for biological and biomedical research for hundreds of years. A map of CNVs in chickens could facilitate the identification of chromosomal regions that segregate for important agricultural and disease phenotypes.
RESULTS - Ninety six CNVs were identified in three lines of chickens (Cornish Rock broiler, Leghorn and Rhode Island Red) using whole genome tiling array. These CNVs encompass 16 Mb (1.3%) of the chicken genome. Twenty six CNVs were found in two or more animals. Whereas most small sized CNVs reside in none coding sequences, larger CNV regions involve genes (for example prolactin receptor, aldose reductase and zinc finger proteins). These results suggest that chicken CNVs potentially affect agricultural or disease related traits.
CONCLUSION - An initial map of CNVs for the chicken has been described. Although chicken genome is approximately one third the size of a typical mammalian genome, the pattern of chicken CNVs is similar to that of mammals. The number of CNVs detected per individual was also similar to that found in dogs, mice, rats and macaques. A map of chicken CNVs provides new information on genetic variations for the understanding of important agricultural traits and disease.
0 Communities
2 Members
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13 MeSH Terms
Molecular morphology of the chick heart visualized by MALDI imaging mass spectrometry.
Grey AC, Gelasco AK, Section J, Moreno-Rodriguez RA, Krug EL, Schey KL
(2010) Anat Rec (Hoboken) 293: 821-8
MeSH Terms: Animals, Biochemistry, Biomarkers, Chickens, Coronary Vessels, Endocardium, Heart, Heart Septum, Heart Valves, Image Processing, Computer-Assisted, Myocardium, Paraffin Embedding, Proteins, Proteomics, Species Specificity, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tissue Fixation
Show Abstract · Added May 27, 2014
Utilization of MALDI-MS (matrix-assisted laser desorption/ionization mass spectrometry) for tissue imaging is a relatively new proteomic technique that simultaneously maps the spatial distribution of multiple proteins directly within a single frozen tissue section. Here, we report the development of a methodology to apply MALDI tissue imaging to chick heart tissue sections acquired from fixed and paraffin-embedded samples. This protocol produces molecular images that can be related to the high-quality histological tissue sections. Perfused term chick hearts were fixed in acidic ethanol and embedded in paraffin wax. Tissue sections (15 microm) were collected onto conductive slides, deparaffinized with xylene, and transitioned into water with graded ethanol washes and allowed to air dry. In separate experiments, three different MALDI matrices were applied to chick heart tissue sections through repeated cycles from a glass nebulizer. Tissue sections were then analyzed by MALDI mass spectrometry using a raster step-size of 75-100 microm, and molecular images for specific m/z ratios reconstituted. MALDI tissue imaging revealed spatially resolved protein signals within single heart sections that are specific to structures or regions of the heart, for example, vessels, valves, endocardium, myocardium, or septa. Moreover, no prior knowledge of protein expression is required as is the case for immunohistochemistry and in situ hybridization methodologies. The ability to simultaneously localize a large number of unique protein signals within a single tissue section, with good preservation of histological features, provides cardiovascular researchers a new tool to give insight into the molecular mechanisms underlying normal and pathological conditions.
0 Communities
1 Members
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17 MeSH Terms
Performance metrics for liquid chromatography-tandem mass spectrometry systems in proteomics analyses.
Rudnick PA, Clauser KR, Kilpatrick LE, Tchekhovskoi DV, Neta P, Blonder N, Billheimer DD, Blackman RK, Bunk DM, Cardasis HL, Ham AJ, Jaffe JD, Kinsinger CR, Mesri M, Neubert TA, Schilling B, Tabb DL, Tegeler TJ, Vega-Montoto L, Variyath AM, Wang M, Wang P, Whiteaker JR, Zimmerman LJ, Carr SA, Fisher SJ, Gibson BW, Paulovich AG, Regnier FE, Rodriguez H, Spiegelman C, Tempst P, Liebler DC, Stein SE
(2010) Mol Cell Proteomics 9: 225-41
MeSH Terms: Animals, Chickens, Chromatography, Liquid, Egg Proteins, Laboratories, Proteome, Proteomics, Reproducibility of Results, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Software, Tandem Mass Spectrometry
Show Abstract · Added August 21, 2013
A major unmet need in LC-MS/MS-based proteomics analyses is a set of tools for quantitative assessment of system performance and evaluation of technical variability. Here we describe 46 system performance metrics for monitoring chromatographic performance, electrospray source stability, MS1 and MS2 signals, dynamic sampling of ions for MS/MS, and peptide identification. Applied to data sets from replicate LC-MS/MS analyses, these metrics displayed consistent, reasonable responses to controlled perturbations. The metrics typically displayed variations less than 10% and thus can reveal even subtle differences in performance of system components. Analyses of data from interlaboratory studies conducted under a common standard operating procedure identified outlier data and provided clues to specific causes. Moreover, interlaboratory variation reflected by the metrics indicates which system components vary the most between laboratories. Application of these metrics enables rational, quantitative quality assessment for proteomics and other LC-MS/MS analytical applications.
0 Communities
3 Members
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12 MeSH Terms