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: 221 to 225 of 225

Publication Record


A 20-nucleotide element in the intestinal fatty acid binding protein gene modulates its cell lineage-specific, differentiation-dependent, and cephalocaudal patterns of expression in transgenic mice.
Simon TC, Roberts LJ, Gordon JI
(1995) Proc Natl Acad Sci U S A 92: 8685-9
MeSH Terms: Animals, Base Sequence, Carrier Proteins, Cell Differentiation, Fatty Acid-Binding Protein 7, Fatty Acid-Binding Proteins, Gene Expression Regulation, Developmental, Head, Immunohistochemistry, Intestines, Male, Mice, Mice, Transgenic, Microscopy, Confocal, Microscopy, Immunoelectron, Molecular Sequence Data, Myelin P2 Protein, Neoplasm Proteins, Nerve Tissue Proteins, Nuclear Proteins, Protein Binding, Regulatory Sequences, Nucleic Acid, Suppression, Genetic, Tail, Transcriptional Activation
Show Abstract · Added December 10, 2013
A sequence of epithelial cell proliferation, allocation to four principal lineages, migration-associated differentiation, and cell loss occurs along the crypt-villus axis of the mouse intestine. The sequence is completed in a few days and is recapitulated throughout the life-span of the animal. We have used an intestine-specific fatty acid binding protein gene, Fabpi, as a model for studying regulation of gene expression in this unique developmental system. Promoter mapping studies in transgenic mice identified a 20-bp cis-acting element (5'-AGGTGGAAGCCATCACACTT-3') that binds small intestinal nuclear proteins and participates in the control of Fabpi's cephalocaudal, differentiation-dependent, and cell lineage-specific patterns of expression. Immunocytochemical studies using confocal and electron microscopy indicate that it does so by acting as a suppressor of gene expression in the distal small intestine/colon, as a suppressor of gene activation in proliferating and nonproliferating cells located in the crypts of Lieberk├╝hn, and as a suppressor of expression in the growth factor and defensin-producing Paneth cell lineage. The 20-bp domain has no obvious sequence similarities to known transcription factor binding sites. The three functions modulated by this compact element represent the types of functions required to establish and maintain the intestine's remarkably complex spatial patterns of gene expression. The transgenes described in this report also appear to be useful in characterizing the crypt's stem cell hierarchy.
0 Communities
1 Members
0 Resources
25 MeSH Terms
Phenotypic determinants of adenovirus E1A gene autoregulation: variable region between conserved coding domains 2 and 3.
Hamid R, Cogan JD, Jones SN, Tibbetts C
(1995) Virology 213: 666-70
MeSH Terms: Adenovirus E1A Proteins, Adenoviruses, Human, Amino Acid Sequence, Base Sequence, Conserved Sequence, DNA, Viral, Gene Expression Regulation, Viral, Genes, Viral, HeLa Cells, Humans, Molecular Sequence Data, Phenotype, Promoter Regions, Genetic, Transcriptional Activation
Show Abstract · Added March 5, 2014
Different serotypes and evolutionary variants of human adenoviruses exhibit distinctive patterns of positive and negative autoregulation of the viral E1A gene. An autoregulatory E1A promoter mutation of the adenovirus type 3 (Ad3) E1A gene renders Ad3hr15 incapable of growth in normally permissive cells. The promoter mutation is complemented in trans by E1A products of the heterologous helper adenovirus type 5 (Ad5). Second-site revertants of Ad3hr15 restore viability with high levels of E1A gene expression. The revertant E1A genotypes retain the mutant E1A promoter and have small in-frame deletions in the nonconserved region between the repression- and activation-associated conserved domains CR2 and CR3. Plasmid expression vectors were constructed as 12S and 13S cDNA forms of revertant E1A genes. These were used in cotransfection experiments with a reporter gene plasmid under transcriptional control of the mutant Ad3hr15 E1A promoter. The repression of the Ad3hr15 E1A promoter by helper Ad5 or revertant 12S E1A cDNA was consistently greater than that effected wild-type Ad3 12S cDNAs expression. Significantly greater levels of positive transactivation were observed in cotransfections with 13S cDNAs of Ad5 or with the 13S E1A cDNA of Ad3hr15 revertants, compared to the transactivation observed with the mutant-encoded wild-type Ad3 13S E1A cDNA. The Ad5 helper and dI-revertant phenotype of Ad3hr15 appear to be related to transactivation activities of coexpressed E1A genes. The nonconserved region which separates the conserved coding regions CR2 and CR3 of the type 3 E1A gene acts to attenuate E1A-mediated repression and transactivation of transcription.
0 Communities
1 Members
0 Resources
14 MeSH Terms
In vitro inhibition of dihydropyridine oxidation and aflatoxin B1 activation in human liver microsomes by naringenin and other flavonoids.
Guengerich FP, Kim DH
(1990) Carcinogenesis 11: 2275-9
MeSH Terms: Aflatoxins, Chamomile, Chromatography, High Pressure Liquid, Dihydropyridines, Felodipine, Flavanones, Flavins, Flavonoids, Gene Expression Regulation, Hesperidin, Humans, In Vitro Techniques, Kaempferols, Microsomes, Liver, Oils, Volatile, Plants, Medicinal, Quercetin, Transcriptional Activation
Show Abstract · Added March 5, 2014
Recent in vivo studies in humans have shown a dramatic effect of grapefruit juice in blocking the oxidation of dihydropyridine calcium channel blockers. The flavonoid naringin is the most abundant natural product specific for grapefruit and related citrus--the aglycone naringenin, known to be readily formed from naringin in humans, was found to inhibit the oxidation of the dihydropyridines nifedipine and felodipine in human liver microsomal preparations. These observations were of interest in light of the knowledge that the same human liver cytochrome P450 (IIIA4) appears to be a major catalyst in both nifedipine oxidation and aflatoxin B1 activation. Several flavones inhibited the in vitro activation of aflatoxin B1 in a system employing umuC gene activation due to DNA damage in Salmonella typhimurium TA1535/pSK1002, with naringenin being as effective as any. The high concentration of derivatives of naringenin in certain citrus fruits may be of relevance to cancer chemoprevention involving those carcinogens that are activated by cytochrome P-450IIIA4.
0 Communities
1 Members
0 Resources
18 MeSH Terms
Transcriptional and posttranscriptional activation of urokinase plasminogen activator gene expression in metastatic tumor cells.
Henderson BR, Tansey WP, Phillips SM, Ramshaw IA, Kefford RF
(1992) Cancer Res 52: 2489-96
MeSH Terms: 9,10-Dimethyl-1,2-benzanthracene, Amino Acid Sequence, Animals, DNA, Down-Regulation, Enzyme Activation, Female, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Neoplastic, Mammary Neoplasms, Experimental, Molecular Sequence Data, RNA, Messenger, Rats, Rats, Inbred F344, Transcription, Genetic, Transcriptional Activation, Urokinase-Type Plasminogen Activator
Show Abstract · Added March 10, 2014
Urokinase plasminogen activator (uPA) is a serine protease which has frequently been implicated in the process of tumor cell invasion and metastasis. The degree of expression and mode(s) of regulation of the uPA gene in metastatic compared with nonmetastatic tumor cells have not yet been addressed. We have cloned and sequenced a full-length rat uPA complementary DNA and utilized Northern blot analysis to report that the uPA gene is expressed at levels 3.5- to 70-fold higher in metastatic cell lines than in nonmetastatic cell lines derived from two independent rat mammary adenocarcinomas. Nuclear run-on assays and RNA half-life estimations indicated that metastatic MAT 13762 rat mammary adenocarcinoma cells expressed 3.5-fold higher levels of uPA RNA than a nonmetastatic derivative (J-clone), due to a combined increase in uPA gene transcription and cytoplasmic RNA stability. By contrast, uPA RNA (and enzyme) levels were elevated by up to 70-fold in metastatic clones of dimethylbenz(a)anthracene-induced rat mammary adenocarcinoma (DMBA-8) due to predominantly posttranscriptional mechanisms. Moreover, treatment of nonmetastatic DMBA-8 cell lines with protein synthesis inhibitors led to an increase in nuclear and cytoplasmic uPA RNA levels, without altering the rate of uPA gene transcription. These results suggest that in addition to gene transcription, posttranscriptional events localized in the nucleus and cytoplasm are key determinants of uPA gene activation in rat mammary adenocarcinomas.
0 Communities
1 Members
0 Resources
17 MeSH Terms
Mini-Oct and Oct-2c: two novel, functionally diverse murine Oct-2 gene products are differentially expressed in the CNS.
Stoykova AS, Sterrer S, Erselius JR, Hatzopoulos AK, Gruss P
(1992) Neuron 8: 541-58
MeSH Terms: Amino Acid Sequence, Animals, Base Sequence, Central Nervous System, Cloning, Molecular, DNA, DNA-Binding Proteins, Gene Expression Regulation, Genes, Male, Mice, Molecular Sequence Data, Nucleic Acid Hybridization, Octamer Transcription Factor-2, RNA Splicing, RNA, Messenger, Repressor Proteins, Restriction Mapping, Testis, Trans-Activators, Transcription Factors, Transcriptional Activation
Show Abstract · Added June 11, 2010
We report that two novel alternatively spliced products of the murine Oct-2 gene encode Mini-Oct (Oct-2d), a protein consisting of almost only the POU domain, and Oct-2c, a protein lacking the last 12 amino acids of Oct-2a. Ectopic expression in HeLa cells shows that Oct-2c is a transactivator, whereas Mini-Oct fails to transactivate if the octamer motif is in a promoter position next to TATA box. Mini-Oct can repress the transcriptional signal generated by endogenous octamer factors in F9 cells. It seems that Mini-Oct has the potential to serve as a transcriptional modulator for genes regulated by different octamer-binding factors. In situ hybridization reveals that Mini-Oct expression follows the general pattern of other known Oct-2 transcripts. However, it is absent from the Purkinje cell layer in the cerebellum of adult mice, and strong expression is observed in the developing nasal neuroepithelium and primary spermatids. Differential expression patterns of the Oct-2 transcripts with different transactivation/repression capacities of the encoded proteins may have a specific role in gene expression in the developing nervous system and in adult brain.
0 Communities
1 Members
0 Resources
22 MeSH Terms