Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 10 of 15

Publication Record

Connections

Resident progenitors, not exogenous migratory cells, generate the majority of visceral mesothelium in organogenesis.
Winters NI, Williams AM, Bader DM
(2014) Dev Biol 391: 125-32
MeSH Terms: Animals, Cell Differentiation, Cell Movement, Chick Embryo, Chimera, Embryonic Stem Cells, Epithelium, Gastrointestinal Tract, Heart, Organogenesis, Quail, Respiratory System
Show Abstract · Added September 28, 2015
Historically, analyses of mesothelial differentiation have focused on the heart where a highly migratory population of progenitors originating from a localized "extrinsic" source moves to and over the developing organ. This model long stood alone as the paradigm for generation of this cell type. Here, using chick/quail chimeric grafting and subsequent identification of mesothelial cell populations, we demonstrate that a different mechanism for the generation of mesothelia exists in vertebrate organogenesis. In this newly discovered model, mesothelial progenitors are intrinsic to organs of the developing digestive and respiratory systems. Additionally, we demonstrate that the early heart stands alone in its ability to recruit an entirely exogenous mesothelial cell layer during development. Thus, the newly identified "organ intrinsic" model of mesotheliogenesis appears to predominate while the long-studied cardiac model of mesothelial development may be the outlier.
Copyright © 2014 Elsevier Inc. All rights reserved.
1 Communities
1 Members
0 Resources
12 MeSH Terms
Comprehensive timeline of mesodermal development in the quail small intestine.
Thomason RT, Bader DM, Winters NI
(2012) Dev Dyn 241: 1678-94
MeSH Terms: Animals, Fluorescent Antibody Technique, Gene Expression Regulation, Developmental, Intestine, Small, Mesoderm, Microscopy, Fluorescence, Quail
Show Abstract · Added December 5, 2013
BACKGROUND - To generate the mature intestine, splanchnic mesoderm diversifies into six different tissue layers each with multiple cell types through concurrent and complex morphogenetic events. Hindering the progress of research in the field is the lack of a detailed description of the fundamental morphological changes that constitute development of the intestinal mesoderm.
RESULTS - We used immunofluorescence and morphometric analyses of wild-type and Tg(tie1:H2B-eYFP) quail embryos to establish a comprehensive timeline of mesodermal development in the avian intestine. The following landmark features were analyzed from appearance of the intestinal primordium through generation of the definitive structure: radial compartment formation, basement membrane dynamics, mesothelial differentiation, mesenchymal expansion and growth patterns, smooth muscle differentiation, and maturation of the vasculature. In this way, structural relationships between mesodermal components were identified over time.
CONCLUSIONS - This integrated analysis presents a roadmap for investigators and clinicians to evaluate diverse experimental data obtained at individual stages of intestinal development within the longitudinal context of intestinal morphogenesis.
Copyright © 2012 Wiley Periodicals, Inc.
2 Communities
1 Members
0 Resources
7 MeSH Terms
Technical note: a gene delivery system in the embryonic cells of avian species using a human adenoviral vector.
Shin J, Bae DR, Latshaw JD, Wick MP, Reddish JM, Lee K
(2009) J Anim Sci 87: 2791-5
MeSH Terms: Adenoviruses, Human, Animals, Cells, Cultured, Chickens, Gene Transfer Techniques, Genetic Vectors, Green Fluorescent Proteins, Quail
Show Abstract · Added March 3, 2014
Adenovirus (Ad) has been used in vivo and in vitro as a vector to carry a foreign gene for efficient gene delivery into various cell types and tissues of animals. The aim of the current study was to evaluate the Ad delivery system in primary avian cells. Primary cells isolated from the embryonic pectoralis major muscles of the chicken and quail were cultured and incubated with human recombinant Ad serotype 5 (Ad5) containing sequences encoding either the green fluorescence protein (GFP) gene alone, as a tracking marker, or both GFP and murine 3-hydroxyisobutyryl-CoA hydrolase (mHIBCH) as a target gene. The fluorescent GFP images showed the successful delivery of a target gene using Ad5 in the primary avian cultured cells. In addition, immunostaining of the myosin heavy chain (MyHC) in these cells indicated that a large population of the cells was myogenic. Colocalization of GFP-positive cells with MyHC staining was mostly found in MyHC-negative cells, indicating successful delivery of Ad5 into a large population of mononucleated cells. Furthermore, the current fluorescence study detected the dual expression of GFP and mHIBCH protein in GFP-positive cells. Finally, Western blot analysis confirmed that the Ad-mediated expression of mHIBCH protein was specific in primary cultures of avian myogenic cells and that the mHIBCH protein expression was continued for 15 d after infection in chicken primary cells. These data demonstrate that Ad5 is a feasible tool to express foreign genes in primary cultured cells of avian species, providing a new approach to study the function of genes of interest in muscle development and metabolism.
0 Communities
1 Members
0 Resources
8 MeSH Terms
Cloning of adipose triglyceride lipase complementary deoxyribonucleic acid in poultry and expression of adipose triglyceride lipase during development of adipose in chickens.
Lee K, Shin J, Latshaw JD, Suh Y, Serr J
(2009) Poult Sci 88: 620-30
MeSH Terms: Adipose Tissue, Amino Acid Sequence, Animals, Base Composition, Chickens, Cloning, Molecular, DNA, Complementary, Gene Expression Regulation, Developmental, Lipase, Molecular Sequence Data, Quail, Turkeys
Show Abstract · Added March 3, 2014
Increasing the breakdown of stored fat in adipose tissue leads to reducing fat content, enhancing feed efficiency and, consequently, decreasing the production cost of poultry. The processes of lipolysis are not completely understood, and the proteins involved in this process need to be identified. An adipose triglyceride lipase (ATGL), recently identified in several species, has not been studied in avian species. We have cloned the full-length coding sequences of ATGL cDNA for the chicken, turkey, and quail. Sequence comparisons among mammals and these avian species showed that the avian ATGL have 2 conserved domains, the patatin domain and the hydrophobic domain. The patatin domain contains lipase activity, and the hydrophobic domain exhibits lipid droplet binding. The high levels of chicken, turkey, and quail ATGL mRNA and protein are exclusively found in subcutaneous and abdominal adipose tissues. In addition, chicken ATGL (gATGL) is mainly expressed in the fractionated adipocytes compared with stromal-vascular cells that mostly contain preadipocytes (P < 0.001). Furthermore, ontogeny of gATGL mRNA and protein expression in adipose tissue showed induction of gATGL immediately after hatching before access to food (P < 0.05), suggesting that an energy deficit due to posthatching starvation may increase breakdown of stored fat via increasing gATGL expression in adipose tissue. Our studies showed that expression of the chicken ATGL is adipose specific and regulated developmentally, suggesting that a possible modulation of ATGL expression would regulate fat deposition in avian species.
0 Communities
1 Members
0 Resources
12 MeSH Terms
CMF1-Rb interaction promotes myogenesis in avian skeletal myoblasts.
Robertson JB, Zhu T, Nasreen S, Kilkenny D, Bader D, Dees E
(2008) Dev Dyn 237: 1424-33
MeSH Terms: Animals, Cell Cycle, Cell Differentiation, Cell Line, Cell Proliferation, Chromosomal Proteins, Non-Histone, Contractile Proteins, Humans, Mice, Microfilament Proteins, Muscle Development, Muscle Proteins, Muscle, Skeletal, MyoD Protein, Myoblasts, Myocytes, Cardiac, Myogenic Regulatory Factor 5, Myogenin, Protein Binding, Quail, Retinoblastoma Protein
Show Abstract · Added May 29, 2014
CMF1 protein is expressed in developing striated muscle before the expression of contractile proteins, and depletion of CMF1 in myoblasts results in inability to express muscle-specific proteins. Previous studies of CMF1 identify a functional Rb-binding domain, which is conserved in the murine and human homologues. Here, we show that CMF1 binds Rb family members, while a CMF1 protein with deletion of the Rb-binding domain (Rb-del CMF1) does not. Myogenic cell lines over-expressing Rb-del CMF1 proliferate normally, but exhibit markedly impaired differentiation, including dramatically reduced contractile proteins gene expression and failure to fuse into myotubes. Furthermore, by quantitative real-time polymerase chain reaction, MyoD and Myf5 mRNA levels are comparable to wild-type, while myogenin and contractile protein mRNA levels are significantly attenuated. These data demonstrate that CMF1 regulates myocyte differentiation by interaction with Rb family members to induce expression of myogenic regulatory factors.
0 Communities
1 Members
0 Resources
21 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, Cercopithecus aethiops, Chickens, 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.
1 Communities
1 Members
0 Resources
22 MeSH Terms
Autocrine regulation of norepinephrine transporter expression.
Ren ZG, Pörzgen P, Zhang JM, Chen XR, Amara SG, Blakely RD, Sieber-Blum M
(2001) Mol Cell Neurosci 17: 539-50
MeSH Terms: Animals, Autocrine Communication, Carrier Proteins, Cell Movement, Cells, Cultured, Chick Embryo, Cloning, Molecular, DNA, Complementary, Gene Expression Regulation, Developmental, In Vitro Techniques, Molecular Sequence Data, Neurons, Neurotrophin 3, Norepinephrine, Norepinephrine Plasma Membrane Transport Proteins, Quail, RNA, Messenger, Sequence Homology, Amino Acid, Sympathomimetics, Symporters, Transforming Growth Factor beta, Transforming Growth Factor beta1
Show Abstract · Added July 10, 2013
The norepinephrine transporter (NET) is a neurotransmitter scavenger and site of drug action in noradrenergic neurons. The aim of this study was to identify mechanisms that regulate NET expression during the development of quail (q) sympathetic neuroblasts, which develop from neural crest stem cells. Neurotrophin-3 (NT-3) and transforming growth factor beta1 (TGF-beta1) cause an increase of qNET mRNA levels in neural crest cells. When combined, the growth factors are additive in increasing qNET mRNA levels. Both NT-3 and TGF-beta1 are synthesized by neural crest cells. Onset of NET expression precedes the onset of neural crest stem cell emigration from the neural tube. In older embryos, qNET is expressed by several crest-derived and noncrest tissues. The data show that qNET expression in presumptive sympathetic neurons is initiated early in embryonic development by growth factors that are produced by neural crest cells themselves. Moreover, the results support our previous observations that norepinephrine transport contributes to the regulation of the differentiation of neural crest stem cells into sympathetic neurons.
Copyright 2001 Academic Press.
1 Communities
1 Members
0 Resources
22 MeSH Terms
Analysis of CMF1 reveals a bone morphogenetic protein-independent component of the cardiomyogenic pathway.
Pabón-Peña LM, Goodwin RL, Cise LJ, Bader D
(2000) J Biol Chem 275: 21453-9
MeSH Terms: Amino Acid Sequence, Animals, Avian Proteins, Bone Morphogenetic Proteins, Cell Differentiation, Cell Division, Chick Embryo, Chickens, Chromosomal Proteins, Non-Histone, Cloning, Molecular, Embryo, Nonmammalian, Embryonic Induction, Gene Expression Regulation, Developmental, Heart, Microfilament Proteins, Molecular Sequence Data, Muscle Proteins, Quail, Restriction Mapping
Show Abstract · Added September 28, 2015
Disruption of the CMF1 function in anterior mesoderm inhibits cardiac myogenesis in avian embryos. In the present study, we show that CMF1 is a member of an emerging family of proteins that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 kDa), dynamic subcellular distribution, and potential functions in cell division and differentiation. The current data suggest that CMF1 is a unique member of this family by virtue of its restricted protein expression and variant subcellular distribution. Immunochemical analysis demonstrates that CMF1 protein is expressed in cardiogenic cells prior to the activation of cardiac structural gene products. In addition, we show that expression of CMF1 is not dependent on the bone morphogenetic protein (BMP) signaling pathway during development. Still, CMF1 cannot direct cardiomyogenesis in the absence of such factors as NKX-2.5. Taken with our previous data, this study suggests that CMF1 is a BMP-independent component of the cardiomyogenic pathway.
1 Communities
1 Members
0 Resources
19 MeSH Terms
Antibodies directed against the chicken type II TGFbeta receptor identify endothelial cells in the developing chicken and quail.
Brown CB, Drake CJ, Barnett JV
(1999) Dev Dyn 215: 79-85
MeSH Terms: Animals, Blotting, Western, Chick Embryo, Endothelium, Quail, Transforming Growth Factor beta
Show Abstract · Added February 21, 2016
Due to the availability of the endothelial cell marker QH1, experiments using quail embryos have traditionally been used to trace the endothelial cell lineage and describe the morphologic events of vessel formation. A comparable marker in the chicken has not been available. Here we report that antibodies raised against the extracellular domain of the chicken type II TGFbeta receptor (TBRII) preferentially identify endothelial cells in the chick. Endothelial cells can first be identified in the 6-somite chick embryo by TBRII expression. TBRII expression in 12- and 22-somite chick and quail embryos was found to directly correlate with the endothelial QH1 staining pattern in quail. This preferential labeling of endothelial cells persists until at least embryonic day 10 in the chick. These data indicate that antibodies to TBRII are an effective marker of endothelial cells in chick and provide useful reagents for the evaluation of vascular patterning.
0 Communities
1 Members
0 Resources
6 MeSH Terms
bves: A novel gene expressed during coronary blood vessel development.
Reese DE, Zavaljevski M, Streiff NL, Bader D
(1999) Dev Biol 209: 159-71
MeSH Terms: Actins, Amino Acid Sequence, Animals, Aorta, Avian Proteins, Blotting, Northern, Blotting, Western, Cell Adhesion Molecules, Chick Embryo, Coronary Vessels, Gene Library, Mice, Molecular Sequence Data, Muscle Proteins, Muscle, Smooth, Muscle, Smooth, Vascular, Myocardium, Pericardium, Quail, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Time Factors, Tissue Distribution
Show Abstract · Added September 28, 2015
We have used a subtractive method to clone novel messages enriched in the heart. Here we show that one such message, bves (blood vessel/epicardial substance) is a novel protein that is highly conserved between chicken and mouse. The bves message is detected at high levels in early chick hearts. Using anti-Bves antibodies, we show expression in cells of the proepicardial organ, migrating epicardium, epicardial-derived mesenchyme, and smooth muscle of the developing intracardiac arterial system, including the coronary arteries. Our data suggest that Bves is an early marker of developing vascular smooth muscle cells. In addition, the expression pattern of Bves protein reveals the patterning of intracardiac vascular smooth muscle and possible insights into the cellular regulation of smooth muscle differentiation during vasculogenesis.
Copyright 1999 Academic Press.
1 Communities
1 Members
0 Resources
23 MeSH Terms