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The ubiquitin-selective chaperone Cdc48/p97 associates with Ubx3 to modulate monoubiquitylation of histone H2B.
Bonizec M, Hérissant L, Pokrzywa W, Geng F, Wenzel S, Howard GC, Rodriguez P, Krause S, Tansey WP, Hoppe T, Dargemont C
(2014) Nucleic Acids Res 42: 10975-86
MeSH Terms: Adenosine Triphosphatases, Cell Cycle Proteins, Cell Line, Cells, Cultured, Female, Histones, Humans, Male, Molecular Chaperones, Mutation, Myoblasts, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic, Ubiquitination, Valosin Containing Protein
Show Abstract · Added February 12, 2015
Cdc48/p97 is an evolutionary conserved ubiquitin-dependent chaperone involved in a broad array of cellular functions due to its ability to associate with multiple cofactors. Aside from its role in removing RNA polymerase II from chromatin after DNA damage, little is known about how this AAA-ATPase is involved in the transcriptional process. Here, we show that yeast Cdc48 is recruited to chromatin in a transcription-coupled manner and modulates gene expression. Cdc48, together with its cofactor Ubx3 controls monoubiquitylation of histone H2B, a conserved modification regulating nucleosome dynamics and chromatin organization. Mechanistically, Cdc48 facilitates the recruitment of Lge1, a cofactor of the H2B ubiquitin ligase Bre1. The function of Cdc48 in controlling H2B ubiquitylation appears conserved in human cells because disease-related mutations or chemical inhibition of p97 function affected the amount of ubiquitylated H2B in muscle cells. Together, these results suggest a prominent role of Cdc48/p97 in the coordination of chromatin remodeling with gene transcription to define cellular differentiation processes.
© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.
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16 MeSH Terms
Endothelial cells contribute to generation of adult ventricular myocytes during cardiac homeostasis.
Fioret BA, Heimfeld JD, Paik DT, Hatzopoulos AK
(2014) Cell Rep 8: 229-41
MeSH Terms: Animals, Antigens, Ly, Cell Lineage, Cells, Cultured, Coronary Vessels, Endothelial Cells, Endothelial Progenitor Cells, GATA4 Transcription Factor, Heart Ventricles, Homeostasis, Membrane Proteins, Mice, Myoblasts, Myocytes, Cardiac, Stem Cell Niche
Show Abstract · Added February 13, 2015
Cardiac tissue undergoes renewal with low rates. Although resident stem cell populations have been identified to support cardiomyocyte turnover, the source of the cardiac stem cells and their niche remain elusive. Using Cre/Lox-based cell lineage tracing strategies, we discovered that labeling of endothelial cells in the adult heart yields progeny that have cardiac stem cell characteristics and express Gata4 and Sca1. Endothelial-derived cardiac progenitor cells were localized in the arterial coronary walls with quiescent and proliferative cells in the media and adventitia layers, respectively. Within the myocardium, we identified labeled cardiomyocytes organized in clusters of single-cell origin. Pulse-chase experiments showed that generation of individual clusters was rapid but confined to specific regions of the heart, primarily in the right anterior and left posterior ventricular walls and the junctions between the two ventricles. Our data demonstrate that endothelial cells are an intrinsic component of the cardiac renewal process.
Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved.
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15 MeSH Terms
Matrix metalloproteinase-9 inhibition improves proliferation and engraftment of myogenic cells in dystrophic muscle of mdx mice.
Hindi SM, Shin J, Ogura Y, Li H, Kumar A
(2013) PLoS One 8: e72121
MeSH Terms: Animals, Cell Proliferation, Cells, Cultured, Graft Survival, Macrophages, Matrix Metalloproteinase 9, Matrix Metalloproteinase Inhibitors, Mice, Mice, Inbred C57BL, Mice, Inbred mdx, Mice, Knockout, Muscle, Skeletal, Muscular Dystrophy, Duchenne, Myoblasts, Phenotype, Primary Cell Culture, Receptors, Notch, Wnt Signaling Pathway
Show Abstract · Added March 3, 2014
Duchenne muscular dystrophy (DMD) caused by loss of cytoskeletal protein dystrophin is a devastating disorder of skeletal muscle. Primary deficiency of dystrophin leads to several secondary pathological changes including fiber degeneration and regeneration, extracellular matrix breakdown, inflammation, and fibrosis. Matrix metalloproteinases (MMPs) are a group of extracellular proteases that are involved in tissue remodeling, inflammation, and development of interstitial fibrosis in many disease states. We have recently reported that the inhibition of MMP-9 improves myopathy and augments myofiber regeneration in mdx mice (a mouse model of DMD). However, the mechanisms by which MMP-9 regulates disease progression in mdx mice remain less understood. In this report, we demonstrate that the inhibition of MMP-9 augments the proliferation of satellite cells in dystrophic muscle. MMP-9 inhibition also causes significant reduction in percentage of M1 macrophages with concomitant increase in the proportion of promyogenic M2 macrophages in mdx mice. Moreover, inhibition of MMP-9 increases the expression of Notch ligands and receptors, and Notch target genes in skeletal muscle of mdx mice. Furthermore, our results show that while MMP-9 inhibition augments the expression of components of canonical Wnt signaling, it reduces the expression of genes whose products are involved in activation of non-canonical Wnt signaling in mdx mice. Finally, the inhibition of MMP-9 was found to dramatically improve the engraftment of transplanted myoblasts in skeletal muscle of mdx mice. Collectively, our study suggests that the inhibition of MMP-9 is a promising approach to stimulate myofiber regeneration and improving engraftment of muscle progenitor cells in dystrophic muscle.
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18 MeSH Terms
Current stem cell delivery methods for myocardial repair.
Sheng CC, Zhou L, Hao J
(2013) Biomed Res Int 2013: 547902
MeSH Terms: Animals, Bone Marrow Cells, Cardiovascular Diseases, Embryonic Stem Cells, Humans, Myoblasts, Skeletal, Myocardial Infarction, Myocardium, Pluripotent Stem Cells, Regeneration, Stem Cell Transplantation, Stem Cells, Wound Healing
Show Abstract · Added September 16, 2013
Heart failure commonly results from an irreparable damage due to cardiovascular diseases (CVDs), the leading cause of morbidity and mortality in the United States. In recent years, the rapid advancements in stem cell research have garnered much praise for paving the way to novel therapies in reversing myocardial injuries. Cell types currently investigated for cellular delivery include embryonic stem cells (ESCs), induced pluripotent stem cells (iPSCs), and adult stem cell lineages such as skeletal myoblasts, bone-marrow-derived stem cells (BMSCs), mesenchymal stem cells (MSCs), and cardiac stem cells (CSCs). To engraft these cells into patients' damaged myocardium, a variety of approaches (intramyocardial, transendocardial, transcoronary, venous, intravenous, intracoronary artery and retrograde venous administrations and bioengineered tissue transplantation) have been developed and explored. In this paper, we will discuss the pros and cons of these delivery modalities, the current state of their therapeutic potentials, and a multifaceted evaluation of their reported clinical feasibility, safety, and efficacy. While the issues of optimal delivery approach, the best progenitor stem cell type, the most effective dose, and timing of administration remain to be addressed, we are highly optimistic that stem cell therapy will provide a clinically viable option for myocardial regeneration.
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13 MeSH Terms
Long isoform mouse selenoprotein P (Sepp1) supplies rat myoblast L8 cells with selenium via endocytosis mediated by heparin binding properties and apolipoprotein E receptor-2 (ApoER2).
Kurokawa S, Hill KE, McDonald WH, Burk RF
(2012) J Biol Chem 287: 28717-26
MeSH Terms: Animals, Cell Line, Chlorates, Endocytosis, Glutathione Peroxidase, LDL-Receptor Related Proteins, Low Density Lipoprotein Receptor-Related Protein-1, Lysosomes, Mice, Mice, Knockout, Myoblasts, Protein Isoforms, Rats, Receptors, LDL, Selenoproteins, Tumor Suppressor Proteins
Show Abstract · Added March 7, 2014
In vivo studies have shown that selenium is supplied to testis and brain by apoER2-mediated endocytosis of Sepp1. Although cultured cell lines have been shown to utilize selenium from Sepp1 added to the medium, the mechanism of uptake and utilization has not been characterized. Rat L8 myoblast cells were studied. They took up mouse Sepp1 from the medium and used its selenium to increase their glutathione peroxidase (Gpx) activity. L8 cells did not utilize selenium from Gpx3, the other plasma selenoprotein. Neither did they utilize it from Sepp1(Δ240-361), the isoform of Sepp1 that lacks the selenium-rich C-terminal domain. To identify Sepp1 receptors, a solubilized membrane fraction was passed over a Sepp1 column. The receptors apoER2 and Lrp1 were identified in the eluate by mass spectrometry. siRNA experiments showed that knockdown of apoER2, but not of Lrp1, inhibited (75)Se uptake from (75)Se-labeled Sepp1. The addition of protamine to the medium or treatment of the cells with chlorate also inhibited (75)Se uptake. Blockage of lysosome acidification did not inhibit uptake of Sepp1 but did prevent its digestion and thereby utilization of its selenium. These results indicate that L8 cells take up Sepp1 by an apoER2-mediated mechanism requiring binding to heparin sulfate proteoglycans. The presence of at least part of the selenium-rich C-terminal domain of Sepp1 is required for uptake. RT-PCR showed that mouse tissues express apoER2 in varying amounts. It is postulated that apoER2-mediated uptake of long isoform Sepp1 is responsible for selenium distribution to tissues throughout the body.
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16 MeSH Terms
The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-β-dependent signaling, and inhibits TGF-β-dependent fibrotic response in skeletal muscles.
Cabello-Verrugio C, Santander C, Cofré C, Acuña MJ, Melo F, Brandan E
(2012) J Biol Chem 287: 6773-87
MeSH Terms: Animals, CHO Cells, Cell Line, Cricetinae, Decorin, Endocytosis, Fibrosis, Glyburide, Humans, Leucine, Low Density Lipoprotein Receptor-Related Protein-1, Male, Mice, Mice, Inbred C57BL, Muscle, Skeletal, Myoblasts, Skeletal, Protein Structure, Tertiary, Signal Transduction, Transforming Growth Factor beta
Show Abstract · Added June 23, 2012
Decorin is a small proteoglycan, composed of 12 leucine-rich repeats (LRRs) that modulates the activity of transforming growth factor type β (TGF-β) and other growth factors, and thereby influences proliferation and differentiation in a wide array of physiological and pathological processes, such as fibrosis, in several tissues and organs. Previously we described two novel modulators of the TGF-β-dependent signaling pathway: LDL receptor-related protein (LRP-1) and decorin. Here we have determined the regions in decorin that are responsible for interaction with LRP-1 and are involved in TGF-β-dependent binding and signaling. Specifically, we used decorin deletion mutants, as well as peptides derived from internal LRR regions, to determine the LRRs responsible for these decorin functions. Our results indicate that LRR6 and LRR5 participate in the interaction with LRP-1 and TGF-β as well as in its dependent signaling. Furthermore, the internal region (LRR6i), composed of 11 amino acids, is responsible for decorin binding to LRP-1 and subsequent TGF-β-dependent signaling. Furthermore, using an in vivo approach, we also demonstrate that the LRR6 region of decorin can inhibit TGF-β mediated action in response to skeletal muscle injury.
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19 MeSH Terms
Berberine protects against high fat diet-induced dysfunction in muscle mitochondria by inducing SIRT1-dependent mitochondrial biogenesis.
Gomes AP, Duarte FV, Nunes P, Hubbard BP, Teodoro JS, Varela AT, Jones JG, Sinclair DA, Palmeira CM, Rolo AP
(2012) Biochim Biophys Acta 1822: 185-95
MeSH Terms: AMP-Activated Protein Kinases, Animals, Berberine, Cell Line, Diet, High-Fat, Glucose, Hormones, Hyperglycemia, Insulin Resistance, Male, Mice, Mitochondria, Mitochondria, Muscle, Muscle, Skeletal, Myoblasts, NAD, Obesity, Organelle Biogenesis, Phosphorylation, Rats, Rats, Sprague-Dawley, Sirtuin 1
Show Abstract · Added April 25, 2013
Berberine (BBR) has recently been shown to improve insulin sensitivity in rodent models of insulin resistance. Although this effect was explained partly through an observed activation of AMP-activated protein kinase (AMPK), the upstream and downstream mediators of this phenotype were not explored. Here, we show that BBR supplementation reverts mitochondrial dysfunction induced by High Fat Diet (HFD) and hyperglycemia in skeletal muscle, in part due to an increase in mitochondrial biogenesis. Furthermore, we observe that the prevention of mitochondrial dysfunction by BBR, the increase in mitochondrial biogenesis, as well as BBR-induced AMPK activation, are blocked in cells in which SIRT1 has been knocked-down. Taken together, these data reveal an important role for SIRT1 and mitochondrial biogenesis in the preventive effects of BBR on diet-induced insulin resistance.
Copyright © 2011 Elsevier B.V. All rights reserved.
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22 MeSH Terms
Reprogramming of mesenchymal stem cells by the synovial sarcoma-associated oncogene SYT-SSX2.
Garcia CB, Shaffer CM, Alfaro MP, Smith AL, Sun J, Zhao Z, Young PP, VanSaun MN, Eid JE
(2012) Oncogene 31: 2323-34
MeSH Terms: Cell Differentiation, Cell Line, Cell Lineage, Cell Transformation, Neoplastic, Gene Knockdown Techniques, Humans, Mesenchymal Stem Cells, Myoblasts, Neurons, Oncogene Proteins, Fusion, Receptor, Fibroblast Growth Factor, Type 2, Sarcoma, Synovial
Show Abstract · Added March 5, 2014
Cell identity is determined by its gene expression programs. The ability of a cell to change its identity and produce cell types outside its lineage is achieved by the activity of transcription controllers capable of reprogramming differentiation gene networks. The synovial sarcoma (SS)-associated protein, SYT-SSX2, reprograms myogenic progenitors and human bone marrow-derived mesenchymal stem cells (BMMSCs) by dictating their commitment to a pro-neural lineage. It fulfills this function by directly targeting an extensive array of neural-specific genes as well as genes of developmental pathway mediators. Concomitantly, the ability of both myoblasts and BMMSCs to differentiate into their normal myogenic and adipogenic lineages was compromised. SS is believed to arise in mesenchymal stem cells where formation of the t(X/18) translocation product, SYT-SSX, constitutes the primary event in the cancer. SYT-SSX is therefore believed to initiate tumorigenesis in its target stem cell. The data presented here allow a glimpse at the initial events that likely occur when SYT-SSX2 is first expressed, and its dominant function in subverting the nuclear program of the stem cell, leading to its aberrant differentiation, as a first step toward transformation. In addition, we identified the fibroblast growth factor receptor gene, Fgfr2, as one occupied and upregulated by SYT-SSX2. Knockdown of FGFR2 in both BMMSCs and SS cells abrogated their growth and attenuated their neural phenotype. These results support the notion that the SYT-SSX2 nuclear function and differentiation effects are conserved throughout sarcoma development and are required for its maintenance beyond the initial phase. They also provide the stem cell regulator, FGFR2, as a promising candidate target for future SS therapy.
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12 MeSH Terms
Goodpasture antigen-binding protein (GPBP) directs myofibril formation: identification of intracellular downstream effector 130-kDa GPBP-interacting protein (GIP130).
Revert-Ros F, López-Pascual E, Granero-Moltó F, Macías J, Breyer R, Zent R, Hudson BG, Saadeddin A, Revert F, Blasco R, Navarro C, Burks D, Saus J
(2011) J Biol Chem 286: 35030-43
MeSH Terms: Animals, Basement Membrane, Blood Proteins, Carrier Proteins, Cell Line, Collagen, DNA-Binding Proteins, Gene Expression Regulation, Intracellular Signaling Peptides and Proteins, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Myoblasts, Myofibrils, Phosphorylation, Protein-Serine-Threonine Kinases, Recombinant Proteins
Show Abstract · Added February 25, 2014
Goodpasture antigen-binding protein-1 (GPBP-1) is an exportable non-conventional Ser/Thr kinase that regulates glomerular basement membrane collagen organization. Here we provide evidence that GPBP-1 accumulates in the cytoplasm of differentiating mouse myoblasts prior to myosin synthesis. Myoblasts deficient in GPBP-1 display defective myofibril formation, whereas myofibrils assemble with enhanced efficiency in those overexpressing GPBP-1. We also show that GPBP-1 targets the previously unidentified GIP130 (GPBP-interacting protein of 130 kDa), which binds to myosin and promotes its myofibrillar assembly. This report reveals that GPBP-1 directs myofibril formation, an observation that expands its reported role in supramolecular organization of structural proteins to the intracellular compartment.
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19 MeSH Terms
Glutathionylation acts as a control switch for uncoupling proteins UCP2 and UCP3.
Mailloux RJ, Seifert EL, Bouillaud F, Aguer C, Collins S, Harper ME
(2011) J Biol Chem 286: 21865-75
MeSH Terms: Animals, Cells, Cultured, Cysteine, Glutathione, Ion Channels, Mice, Mice, Knockout, Mice, Transgenic, Mitochondrial Proteins, Models, Biological, Myoblasts, Oxidative Stress, Protein Processing, Post-Translational, Reactive Oxygen Species, Thymus Gland, Uncoupling Protein 2, Uncoupling Protein 3
Show Abstract · Added July 23, 2020
The mitochondrial uncoupling proteins 2 and 3 (UCP2 and -3) are known to curtail oxidative stress and participate in a wide array of cellular functions, including insulin secretion and the regulation of satiety. However, the molecular control mechanism(s) governing these proteins remains elusive. Here we reveal that UCP2 and UCP3 contain reactive cysteine residues that can be conjugated to glutathione. We further demonstrate that this modification controls UCP2 and UCP3 function. Both reactive oxygen species and glutathionylation were found to activate and deactivate UCP3-dependent increases in non-phosphorylating respiration. We identified both Cys(25) and Cys(259) as the major glutathionylation sites on UCP3. Additional experiments in thymocytes from wild-type and UCP2 null mice demonstrated that glutathionylation similarly diminishes non-phosphorylating respiration. Our results illustrate that UCP2- and UCP3-mediated state 4 respiration is controlled by reversible glutathionylation. Altogether, these findings advance our understanding of the roles UCP2 and UCP3 play in modulating metabolic efficiency, cell signaling, and oxidative stress processes.
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MeSH Terms