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 6 of 6

Publication Record

Connections

CpG methylation at the USF-binding site mediates cell-specific transcription of human ascorbate transporter SVCT2 exon 1a.
Qiao H, May JM
(2011) Biochem J 440: 73-84
MeSH Terms: Azacitidine, CCAAT-Binding Factor, Cell Line, Cell Line, Tumor, CpG Islands, Decitabine, Dinucleoside Phosphates, Exons, Humans, Methylation, Promoter Regions, Genetic, Sodium-Coupled Vitamin C Transporters, Upstream Stimulatory Factors
Show Abstract · Added December 5, 2013
SVCT2 (sodium-vitamin C co-transporter 2) is the major transporter mediating vitamin C uptake in most organs. Its expression is driven by two promoters (CpG-poor exon 1a promoter and CpG-rich exon 1b promoter). In the present study, we mapped discrete elements within the proximal CpG-poor promoter responsible for exon 1a transcription. We identified two E boxes for USF (upstream stimulating factor) binding and one Y box for NF-Y (nuclear factor Y) binding. We show further that NF-Y and USF bind to the exon 1a promoter in a co-operative manner, amplifying the binding of each to the promoter, and is absolutely required for the full activity of the exon 1a promoter. The analysis of the CpG site located at the upstream USF-binding site in the promoter showed a strong correlation between expression and demethylation. It was also shown that exon 1a transcription was induced in cell culture treated with the demethylating agent decitabine. The specific methylation of this CpG site impaired both the binding of USF and the formation of the functional NF-Y-USF complex as well as promoter activity, suggesting its importance for cell-specific transcription. Thus CpG methylation at the upstream USF-binding site functions in establishing and maintaining cell-specific transcription from the CpG-poor SVCT2 exon 1a promoter.
1 Communities
0 Members
0 Resources
13 MeSH Terms
Regional expression of brain derived neurotrophic factor (BDNF) is correlated with dynamic patterns of promoter methylation in the developing mouse forebrain.
Dennis KE, Levitt P
(2005) Brain Res Mol Brain Res 140: 1-9
MeSH Terms: Animals, Base Sequence, Brain-Derived Neurotrophic Factor, DNA Methylation, DNA Primers, Dinucleoside Phosphates, Female, Gene Expression Regulation, Developmental, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Neuronal Plasticity, Organ Specificity, Pregnancy, Promoter Regions, Genetic, Prosencephalon
Show Abstract · Added April 7, 2010
Brain Derived Neurotrophic Factor (BDNF) plays an important role in brain development and plasticity. BDNF gene expression is known to be dynamically regulated during development, but the regulatory controls of normal differential expression are not well understood. Methylation of CpG dinucleotides within gene promoters is emerging as an important epigenetic control mechanism of transcription, and the BDNF complex promoter contains several CpG dinucleotides. We determined BDNF expression in the developing mouse forebrain and examined whether there were correlated patterns of methylation at CpG dinucleotides within the BDNF promoter. The data show that BDNF is dynamically expressed in the mouse forebrain and that expression is correlated with differential methylation specifically at CpG dinucleotides in eIV of the mouse BDNF promoter. These studies demonstrate that DNA methylation of this regulatory region may be an important mechanism controlling differential expression of BDNF during forebrain development.
0 Communities
1 Members
0 Resources
16 MeSH Terms
Inotropic effects of diadenosine tetraphosphate (AP4A) in human and animal cardiac preparations.
Vahlensieck U, Bokník P, Gombosová I, Huke S, Knapp J, Linck B, Lüss H, Müller FU, Neumann J, Deng MC, Scheld HH, Jankowski H, Schlüter H, Zidek W, Zimmermann N, Schmitz W
(1999) J Pharmacol Exp Ther 288: 805-13
MeSH Terms: Animals, Calcium, Calcium Channels, Cells, Cultured, Dinucleoside Phosphates, Drug Interactions, Guinea Pigs, Heart, Heart Atria, Heart Ventricles, Humans, In Vitro Techniques, Male, Myocardial Contraction, Myocardium, Platelet Aggregation Inhibitors, Xanthines
Show Abstract · Added May 27, 2014
Diadenosine tetraphosphate (AP4A) is an endogenous compound and exerts diverse physiological effects in animal systems. However, the effects of AP4A on inotropy in ventricular cardiac preparations have not yet been studied. The effects of AP4A on force of contraction (FOC) were studied in isolated electrically driven guinea pig and human cardiac preparations. Furthermore, the effects of AP4A on L-type calcium current and [Ca]i were studied in isolated guinea pig ventricular myocytes. In guinea pig left atria, AP4A (0.1-100 microM) reduced FOC maximally by 36.5 +/- 4.3%. In guinea pig papillary muscles, AP4A (100 microM) alone was ineffective, but reduced isoproterenol-stimulated FOC maximally by 29.3 +/- 3.4%. The negative inotropic effects of AP4A in atria and papillary muscles were abolished by the A1-adenosine receptor antagonist 1, 3-dipropyl-cyclopentylxanthine. In guinea pig ventricular myocytes, AP4A (100 microM) attenuated isoproterenol-stimulated L-type calcium current and [Ca]i. In human atrial and ventricular preparations, AP4A (100 microM) alone increased FOC to 158.3 +/- 12.4% and 167.5 +/- 25.1%, respectively. These positive inotropic effects were abolished by the P2-purinoceptor antagonist suramin. On the other hand, AP4A (100 microM) reduced FOC by 27.2 +/- 7.4% in isoproterenol-stimulated human ventricular trabeculae. The latter effect was abolished by 1,3-dipropyl-cyclopentylxanthine. In summary, after beta adrenergic stimulation AP4A exerts negative inotropic effects in animal and human ventricular preparations via stimulation of A1-adenosine receptors. In contrast, AP4A alone can exert positive inotropic effects via P2-purinoceptors in human ventricular myocardium. Thus, P2-purinoceptor stimulation might be a new positive inotropic principle in the human myocardium.
0 Communities
1 Members
0 Resources
17 MeSH Terms
Low frequency of p57KIP2 mutation in Beckwith-Wiedemann syndrome.
Lee MP, DeBaun M, Randhawa G, Reichard BA, Elledge SJ, Feinberg AP
(1997) Am J Hum Genet 61: 304-9
MeSH Terms: Beckwith-Wiedemann Syndrome, Chromosomes, Human, Pair 11, CpG Islands, Cyclin-Dependent Kinase Inhibitor p57, Cyclin-Dependent Kinases, DNA Methylation, DNA Mutational Analysis, Dinucleoside Phosphates, Female, Frameshift Mutation, Gene Frequency, Genetic Heterogeneity, Genomic Imprinting, Humans, Infant, KCNQ Potassium Channels, KCNQ1 Potassium Channel, Male, Nuclear Proteins, Pedigree, Potassium Channels, Potassium Channels, Voltage-Gated
Show Abstract · Added September 19, 2013
Beckwith-Wiedemann syndrome (BWS) is an autosomal dominant disorder of increased prenatal growth and predisposition to embryonal cancers such as Wilms tumor. BWS is thought to involve one or more imprinted genes, since some patients show paternal uniparental disomy, and others show balanced germ-line chromosomal rearrangements involving the maternal chromosome. We previously mapped BWS, by genetic linkage analysis, to 11p15.5, which we and others also found to contain several imprinted genes; these include the gene for insulin-like growth factor II (IGF2) and H19, which show abnormal imprint-specific expression and/or methylation in 20% of BWS patients, and p57KIP2, a cyclin-dependent kinase inhibitor, which we found showed biallelic expression in one of nine BWS patients studied. In addition, p57KIP2 was recently reported to show mutations in two of nine BWS patients. We have now analyzed the entire coding sequence and intron-exon boundaries of p57KIP2 in 40 unrelated BWS patients. Of these patients, only two (5%) showed mutations, both involving frameshifts in the second exon. In one case, the mutation was transmitted to the proband's mother, who was also affected, from the maternal grandfather, suggesting that p57KIP2 is not imprinted in at least some affected tissues at a critical stage of development and that haploinsufficiency due to mutation of either parental allele may cause at least some features of BWS. The low frequency of p57KIP2 mutations, as well as our recent discovery of disruption of the K(v)LQT1 gene in patients with chromosomal rearrangements, suggest that BWS can involve disruption of multiple independent 11p15.5 genes.
0 Communities
1 Members
0 Resources
22 MeSH Terms
Deletions of a differentially methylated CpG island at the SNRPN gene define a putative imprinting control region.
Sutcliffe JS, Nakao M, Christian S, Orstavik KH, Tommerup N, Ledbetter DH, Beaudet AL
(1994) Nat Genet 8: 52-8
MeSH Terms: Angelman Syndrome, Autoantigens, Base Sequence, Chromosomes, Human, Pair 15, Dinucleoside Phosphates, Fathers, Genomic Imprinting, Humans, Molecular Sequence Data, Prader-Willi Syndrome, Ribonucleoproteins, Small Nuclear, Sequence Deletion, snRNP Core Proteins
Show Abstract · Added February 20, 2014
To determine the molecular basis of Prader-Willi syndrome (PWS) and Angelman syndrome (AS), we have isolated new transcripts from chromosome 15q11-q13. Two novel transcripts located within 300 kilobases telomeric to the small nuclear ribonucleoprotein-associated polypeptide N gene (SNRPN) were paternally expressed in cultured cells, along with SNRPN, defining a large imprinted transcriptional domain. In three PWS patients (two sibs), small deletions remove a differentially methylated CpG island containing a newly described 5' exon alpha of SNRPN, and cause loss of expression for the three imprinted transcripts and altered methylation over hundreds of kilobases. The smallest PWS deletion is familial and asymptomatic with maternal transmission. Our data imply the presence of a paternal imprinting control region near exon alpha.
0 Communities
1 Members
0 Resources
13 MeSH Terms
Structure of a duplex oligodeoxynucleotide containing propanodeoxyguanosine opposite a two-base deletion in the (CpG)3 frame shift hotspot of Salmonella typhimurium hisD3052 determined by 1H NMR and restrained molecular dynamics.
Weisenseel JP, Moe JG, Reddy GR, Marnett LJ, Stone MP
(1995) Biochemistry 34: 50-64
MeSH Terms: Base Sequence, Deoxyguanosine, Dinucleoside Phosphates, Frameshift Mutation, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Oligodeoxyribonucleotides, Repetitive Sequences, Nucleic Acid, Salmonella typhimurium, Sequence Deletion, Solutions
Show Abstract · Added March 5, 2014
Structural refinement from solution 1H NMR data was performed on the 5'-d[ATCGC(PdG)-CGGCATG]-3'.5'-d[CATGCCGCGAT]-3' duplex, in which the adducted oligodeoxynucleotide containing the exocyclic lesion 1,N2-propano-2'-deoxyguanosine (PdG) was annealed with the complementary strand which contained a CpG deletion. The resulting duplex required PdG and one adjacent cytosine to be unpaired. A total of 352 distances were utilized to restrain molecular dynamics calculations, of which 264 were NOE-derived. These distances were calculated using complete relaxation matrix methods from hybrid matrices, which were comprised of the experimentally determined distances and additional distances derived from either A-form or B-form DNA. A simulated annealing protocol combined with the distance restraints was able to refine a single structure with an average rms deviation of < 1.35 A. The accuracy of the refined structure was assessed using full relaxation matrix calculations, which gave good agreement with measured NOE intensities. PdG was found to be stacked into the helix below base pair C3.G18, whereas C5 was found to be unpaired and extruded toward the major groove and parallel to base pair G6.C17. This created a localized bend in the DNA helix of approximately 20-35 degrees at the junction between PdG and C5. The bending corroborated previous assays performed on this modified sequence [Moe, J. G., Reddy, G. R., Marnett, L. J., & Stone, M. P. (1994) Chem. Res. Toxicol. 7, 319-328].
0 Communities
1 Members
0 Resources
13 MeSH Terms