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Migration of turkey muscle satellite cells is enhanced by the syndecan-4 cytoplasmic domain through the activation of RhoA.
Shin J, McFarland DC, Velleman SG
(2013) Mol Cell Biochem 375: 115-30
MeSH Terms: Animals, Avian Proteins, Cell Movement, Cells, Cultured, Enzyme Activation, Gene Knockdown Techniques, Male, Protein Kinase C-alpha, Protein Structure, Tertiary, RNA, Small Interfering, Satellite Cells, Skeletal Muscle, Syndecan-4, Turkey, rhoA GTP-Binding Protein
Show Abstract · Added March 3, 2014
Syndecan-4 (S4) is a cell membrane-associated heparan sulfate proteoglycan that forms oligomers in muscle satellite cells. The S4 oligomers activate protein kinase Cα (PKCα) through the S4 cytoplasmic domain and may regulate the activation of ras homolog gene family member A (RhoA), a signal transduction molecule down-stream of PKCα which is thought to influence cell migration. However, little is known about the function of the S4 cytoplasmic domain in satellite cell migration and RhoA activation. The objective of the current study was to determine the function of S4 and its cytoplasmic domain in cell migration and RhoA activation. To study the objective, clones of S4 and S4 without the cytoplasmic domain (S4C) were used in overexpression studies, and small interference RNAs targeting S4 or RhoA were used in knockdown studies. Satellite cell migration was increased by S4 overexpression, but decreased by the knockdown or deletion of the S4 cytoplasmic domain. The RhoA protein was activated by the overexpression of S4, but not with the deletion of the S4 cytoplasmic domain. The treatment of Rho activator II or the knockdown of RhoA also modulated satellite cell migration. Finally, co-transfection (S4 overexpression and RhoA knockdown) and rescue (the knockdown of S4 and the treatment with Rho activator II) studies demonstrated that S4-mediated satellite cell migration was regulated through the activation of RhoA. The cytoplasmic domain of S4 is required for cell migration and RhoA activation which will affect muscle fiber formation.
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14 MeSH Terms
Inhibition of RhoA signaling with increased Bves in trabecular meshwork cells.
Russ PK, Kupperman AI, Presley SH, Haselton FR, Chang MS
(2010) Invest Ophthalmol Vis Sci 51: 223-30
MeSH Terms: Avian Proteins, Blotting, Western, Cell Adhesion Molecules, Cell Line, Electric Impedance, Fluorescein, Fluorescent Antibody Technique, Indirect, Humans, Membrane Proteins, Microfilament Proteins, Muscle Proteins, Myosin Light Chains, Occludin, Permeability, Phosphoproteins, Phosphorylation, Signal Transduction, Tight Junctions, Trabecular Meshwork, Transfection, Zonula Occludens-1 Protein, rhoA GTP-Binding Protein
Show Abstract · Added May 27, 2014
PURPOSE - Blood vessel epicardial substance (Bves) is a novel adhesion molecule that regulates tight junction (TJ) formation. TJs also modulate RhoA signaling, which has been implicated in outflow regulation. Given that Bves has been reported in multiple ocular tissues, the authors hypothesize that Bves plays a role in the regulation of RhoA signaling in trabecular meshwork (TM) cells.
METHODS - Human TM cell lines NTM-5 and NTM-5 transfected to overexpress Bves (NTM-w) were evaluated for TJ formation, and levels of occludin, cingulin, and ZO-1 protein were compared. Assays of TJ function were carried out using diffusion of sodium fluorescein and transcellular electrical resistance (TER). Levels of activated RhoA were measured using FRET probes, and phosphorylation of myosin light chain (MLC-p), a downstream target of RhoA, was assessed by Western blot analysis.
RESULTS - Overexpression of Bves led to increased TJ formation in NTM-5 cells. Increased TJ formation was confirmed by increased occludin, cingulin, and ZO-1 protein. Functionally, NTM-w cells showed decreased permeability and increased TER compared with NTM-5 cells, consistent with increased TJ formation. NTM-w cells also exhibited decreased levels of active RhoA and lower levels of MLC-p than did NTM-5 cells. These findings support a TJ role in RhoA signaling.
CONCLUSIONS - Increased Bves in TM cells leads to increased TJ formation with decreased RhoA activation and decreased MLC-p. This is the first report of a regulatory pathway upstream of RhoA in TM cells. In TM tissue, RhoA has been implicated in outflow regulation; thus, Bves may be a key regulatory molecule in aqueous outflow.
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22 MeSH Terms
Single molecule-sensitive probes for imaging RNA in live cells.
Santangelo PJ, Lifland AW, Curt P, Sasaki Y, Bassell GJ, Lindquist ME, Crowe JE
(2009) Nat Methods 6: 347-9
MeSH Terms: Actin-Related Protein 2, Actins, Animals, Avian Proteins, Bacterial Proteins, Biotin, Carbocyanines, Cell Line, Tumor, Cell Membrane Permeability, Cell Survival, Cells, Cultured, Chick Embryo, DNA-Binding Proteins, Fibroblasts, Fluorescent Dyes, Humans, Image Processing, Computer-Assisted, Microscopy, Confocal, Microscopy, Fluorescence, Molecular Probe Techniques, Oligonucleotide Probes, Poly(A)-Binding Proteins, RNA, RNA, Messenger, RNA-Binding Proteins, Respiratory Syncytial Virus, Human, Streptavidin, Streptolysins, T-Cell Intracellular Antigen-1
Show Abstract · Added August 6, 2012
To visualize native or non-engineered RNA in live cells with single-molecule sensitivity, we developed multiply labeled tetravalent RNA imaging probes (MTRIPs). When delivered with streptolysin O into living human epithelial cancer cells and primary chicken fibroblasts, MTRIPs allowed the accurate imaging of native mRNAs and a non-engineered viral RNA, of RNA co-localization with known RNA-binding proteins, and of RNA dynamics and interactions with stress granules.
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29 MeSH Terms
The mitochondrial genome sequence and molecular phylogeny of the turkey, Meleagris gallopavo.
Guan X, Silva P, Gyenai KB, Xu J, Geng T, Tu Z, Samuels DC, Smith EJ
(2009) Anim Genet 40: 134-41
MeSH Terms: Animals, Avian Proteins, Base Sequence, Chickens, Coturnix, DNA Primers, DNA, Mitochondrial, Evolution, Molecular, Genome, Mitochondrial, Phylogeny, Polymerase Chain Reaction, RNA, Ribosomal, RNA, Transfer, Species Specificity, Turkeys
Show Abstract · Added December 12, 2013
The mitochondrial genome (mtGenome) has been little studied in the turkey (Meleagris gallopavo), a species for which there is no publicly available mtGenome sequence. Here, we used PCR-based methods with 19 pairs of primers designed from the chicken and other species to develop a complete turkey mtGenome sequence. The entire sequence (16,717 bp) of the turkey mtGenome was obtained, and it exhibited 85% similarity to the chicken mtGenome sequence. Thirteen genes and 24 RNAs (22 tRNAs and 2 rRNAs) were annotated. An mtGenome-based phylogenetic analysis indicated that the turkey is most closely related to the chicken, Gallus gallus, and quail, Corturnix japonica. Given the importance of the mtGenome, the present work adds to the growing genomic resources needed to define the genetic mechanisms that underlie some economically significant traits in the turkey.
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15 MeSH Terms
Specific deletion of CMF1 nuclear localization domain causes incomplete cell cycle withdrawal and impaired differentiation in avian skeletal myoblasts.
Dees E, Robertson JB, Zhu T, Bader D
(2006) Exp Cell Res 312: 3000-14
MeSH Terms: Amino Acid Sequence, Animals, Avian Proteins, COS Cells, Cell Cycle, Cell Differentiation, Cell Nucleus, Cell Proliferation, Chickens, Chlorocebus aethiops, Conserved Sequence, Cytoplasm, Gene Expression, HeLa Cells, Humans, Molecular Sequence Data, Myoblasts, Skeletal, Nuclear Localization Signals, Quail, RNA, Messenger, Sequence Deletion, Transfection
Show Abstract · Added September 28, 2015
CMF1 is a protein expressed in embryonic striated muscle with onset of expression preceding that of contractile proteins. Disruption of CMF1 in myoblasts disrupts muscle-specific protein expression. Preliminary studies indicate both nuclear and cytoplasmic distribution of CMF1 protein, suggesting functional roles in both cellular compartments. Here we examine the nuclear function of CMF1, using a newly characterized antibody generated against the CMF1 nuclear localization domain and a CMF1 nuclear localization domain-deleted stable myocyte line. The antibody demonstrates nuclear distribution of the CMF1 protein both in vivo and in cell lines, with clustering of CMF1 protein around chromatin during mitosis. In more differentiated myocytes, the protein shifts to the cytoplasm. The CMF1 NLS-deleted cell lines have markedly impaired capacity to differentiate. Specifically, these cells express less contractile protein than wild-type or full-length CMF1 stably transfected cells, and do not fuse properly into multinucleate syncytia with linear nuclear alignment. In response to low serum medium, a signal to differentiate, CMF1 NLS-deleted cells enter G0, but continue to express proliferation markers and will reenter the cell cycle when stimulated by restoring growth medium. These data suggest that CMF1 is involved in regulation the transition from proliferation to differentiation in embryonic muscle.
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22 MeSH Terms
Bves modulates epithelial integrity through an interaction at the tight junction.
Osler ME, Chang MS, Bader DM
(2005) J Cell Sci 118: 4667-78
MeSH Terms: Animals, Avian Proteins, Biological Transport, Cadherins, Calcium, Cell Adhesion, Cell Adhesion Molecules, Cell Line, Cell Membrane, Chickens, Dogs, Epithelial Cells, Golgi Apparatus, Humans, Membrane Proteins, Muscle Proteins, Mutagenesis, Occludin, Phorbol Esters, Phosphoproteins, Protein Binding, Tight Junctions, Zonula Occludens-1 Protein
Show Abstract · Added September 28, 2015
We first identified Bves (blood vessel/epicardial substance) as a transmembrane protein that localized to the lateral compartment of the epithelial epicardium. Bves traffics to sites of cell-cell contact in cultured epicardial cells and promotes adhesion following transfection into non-adherent fibroblastic L-cells, reminiscent of a cell adhesion molecule. Currently, no function for Bves in relation to epithelial cell adhesion has been identified. We hypothesize that Bves plays a role at cell junctions to establish and/or modulate cell adhesion or cell-cell interactions in epithelial cell types. In this study, we demonstrate that Bves regulates epithelial integrity and that this function may be associated with a role at the tight junction (TJ). We report that Bves localizes with ZO-1 and occludin, markers of the TJ, in polarized epithelial cell lines and in vivo. We find that the behavior of Bves following low Ca2+ challenge or TPA treatment mimics that observed for ZO-1 and is distinct from adherens junction proteins such as E-cadherin. Furthermore, GST pull-down experiments show an interaction between ZO-1 and the intracellular C-terminal tail of Bves. Finally, we demonstrate that Bves modulates tight junction integrity, as indicated by the loss of transepithelial resistance and junction protein localization at the membrane following Bves knock-down in cultured cells. This study is the first to identify a function for Bves in epithelia and supports the hypothesis that Bves contributes to establishment and/or maintenance of epithelial cell integrity.
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23 MeSH Terms
Bves is expressed in the epithelial components of the retina, lens, and cornea.
Ripley AN, Chang MS, Bader DM
(2004) Invest Ophthalmol Vis Sci 45: 2475-83
MeSH Terms: Animals, Avian Proteins, Cell Adhesion Molecules, Cell Differentiation, Cell Line, Chick Embryo, Cornea, Epithelial Cells, Eye Proteins, Fluorescent Antibody Technique, Indirect, Humans, Lens, Crystalline, Membrane Proteins, Mice, Muscle Proteins, Regeneration, Retina, Reverse Transcriptase Polymerase Chain Reaction, Wound Healing
Show Abstract · Added September 28, 2015
PURPOSE - To demonstrate the expression pattern and subcellular localization of Bves/Pop1a protein, a newly identified cell adhesion molecule, during eye development and corneal regeneration.
METHODS - Staged embryonic and adult eyes were assayed using fluorescence immunohistochemistry to detect the Bves protein. A human corneal epithelial (HCE) cell line was used as a model to examine Bves localization during corneal growth and regeneration, with and without antisense morpholino treatment.
RESULTS - The data detail the expression and localization of Bves protein before, during, and after differentiation of the eye. In these analyses, Bves was localized to an apical-lateral position in the initial epithelial primordia of the eye. Later, Bves became localized to specific cell types and subcellular domains in the retina, lens, and cornea, indicating changes in Bves expression in the differentiated eye. Finally, an in vitro model of corneal wound healing showed that Bves staining was missing at the epithelial surface during cellular migration across the wound, but it reappeared at points of cell contact during the reinitiation of epithelial continuity. When epithelial sheets were treated with Bves antisense morpholinos to inhibit Bves function, disruption of epithelial integrity was observed. After injury, similar treatment resulted in an acceleration of cell movement at the wound surface but regeneration of an intact epithelium was ultimately impeded.
CONCLUSIONS - Taken together, these studies suggest that Bves is expressed in epithelial elements of the developing eye and may have a role in corneal epithelial growth and regeneration.
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19 MeSH Terms
Bves expression during avian embryogenesis.
Osler ME, Bader DM
(2004) Dev Dyn 229: 658-67
MeSH Terms: Amino Acid Sequence, Animals, Avian Proteins, Blotting, Western, Cell Adhesion, Cell Adhesion Molecules, Chick Embryo, DNA Primers, Epidermal Cells, Epithelium, Gastrula, Gene Expression Regulation, Developmental, Immunohistochemistry, Intestines, Molecular Sequence Data, Muscle Proteins, Muscles, Reverse Transcriptase Polymerase Chain Reaction, Skin, Time Factors
Show Abstract · Added September 28, 2015
Bves (blood vessel/epicardial substance) is a transmembrane protein postulated to play a role in cell adhesion. While it is clear that Bves and gene products of the same family are expressed in adult striated muscle cells, the distribution of these proteins during development has not been critically examined. An understanding of the expression pattern of Bves is essential for a determination of protein function and its role in embryogenesis. In this study, we present an expression analysis of Bves during chick gastrulation and germ layer formation. Our data show that Bves is expressed in epithelia of all three germ layers early in development. Furthermore, Bves protein is observed in epithelial tissues during organogenesis, specifically the developing epidermis, the gut endoderm, and the epicardium of the heart. These data support the hypothesis that Bves may play a role in cell adhesion and movement of epithelia during early embryogenesis.
Copyright 2004 Wiley-Liss, Inc.
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20 MeSH Terms
Members of the large Maf transcription family regulate insulin gene transcription in islet beta cells.
Matsuoka TA, Zhao L, Artner I, Jarrett HW, Friedman D, Means A, Stein R
(2003) Mol Cell Biol 23: 6049-62
MeSH Terms: Amino Acid Sequence, Animals, Avian Proteins, Binding Sites, Cells, Cultured, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Homeodomain Proteins, Humans, Hydrogen-Ion Concentration, Insulin, Islets of Langerhans, Lectins, C-Type, Macromolecular Substances, Maf Transcription Factors, Large, MafB Transcription Factor, Mass Spectrometry, Mice, Molecular Sequence Data, Multigene Family, Nuclear Proteins, Oncogene Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-maf, Receptors, Immunologic, Sequence Homology, Amino Acid, Trans-Activators, Transcription Factors, Transcription, Genetic
Show Abstract · Added December 10, 2013
The C1/RIPE3b1 (-118/-107 bp) binding factor regulates pancreatic-beta-cell-specific and glucose-regulated transcription of the insulin gene. In the present study, the C1/RIPE3b1 activator from mouse beta TC-3 cell nuclear extracts was purified by DNA affinity chromatography and two-dimensional gel electrophoresis. C1/RIPE3b1 binding activity was found in the roughly 46-kDa fraction at pH 7.0 and pH 4.5, and each contained N- and C-terminal peptides to mouse MafA as determined by peptide mass mapping and tandem spectrometry. MafA was detected in the C1/RIPE3b1 binding complex by using MafA peptide-specific antisera. In addition, MafA was shown to bind within the enhancer region (-340/-91 bp) of the endogenous insulin gene in beta TC-3 cells in the chromatin immunoprecipitation assay. These results strongly suggested that MafA was the beta-cell-enriched component of the RIPE3b1 activator. However, reverse transcription-PCR analysis demonstrated that mouse islets express not only MafA but also other members of the large Maf family, specifically c-Maf and MafB. Furthermore, immunohistochemical studies revealed that at least MafA and MafB were present within the nuclei of islet beta cells and not within pancreas acinar cells. Because MafA, MafB, and c-Maf were each capable of specifically binding to and activating insulin C1 element-mediated expression, our results suggest that all of these factors play a role in islet beta-cell function.
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30 MeSH Terms
Use of avian retroviral vectors to introduce transcriptional regulators into mammalian cells for analyses of tumor maintenance.
Pao W, Klimstra DS, Fisher GH, Varmus HE
(2003) Proc Natl Acad Sci U S A 100: 8764-9
MeSH Terms: Animals, Avian Leukosis Virus, Avian Proteins, Doxycycline, Genes, ras, Genetic Complementation Test, Genetic Vectors, Mice, Mice, Knockout, Mice, Nude, Mice, Transgenic, Neoplasms, Experimental, Receptors, Virus, Trans-Activators
Show Abstract · Added March 24, 2014
A key issue in cancer biology is whether genetic lesions involved in tumor initiation or progression are required for tumor maintenance. This question can be addressed with mouse models that conditionally express oncogenic transgenes, i.e., under the control of tetracycline (tet)-dependent transcriptional regulators. We have developed a system for studying tumor maintenance by using avian retroviral [i.e., replication-competent avian leukosis virus long terminal repeat with splice acceptor (RCAS)] vectors to deliver the reverse tet transcriptional transactivator (rtTA) gene to somatic mammalian cells. rtTA can regulate any transgene in which the protein coding sequence is preceded by a tet-operator (tet-o); RCAS viruses infect only cells engineered to express ectopically the avian retroviral receptor, TVA. One vector, RCAS-rtTA-IRES-GFP, also encodes GFP to identify infected cells. Infection of cells from beta-actin TVA transgenic mice with this vector permits efficient regulation of tet-responsive transgenes. Sarcomas arise when p53-deficient murine embryonic fibroblasts carrying beta-actin TVA and tet-o-K-ras4bG12D transgenes are infected with RCAS-rtTA-IRES-GFP and introduced into nude mice treated with the tet analog, doxycycline (dox); when dox is withdrawn, K-ras4bG12D levels fall, cells undergo apoptosis, and tumors regress. Regression can be prevented by means of a genetic complementation assay in which tumors are superinfected before dox withdrawal with other RCAS viruses, such as those carrying an active allele of K-ras. Many TVA and tet-regulated transgenic mice have been generated; thus, this method for somatic cell-specific and temporally controlled gene expression may have broad applications for the study of oncogenesis and tumor maintenance, as well as other cell functions and development.
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14 MeSH Terms