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Results: 3521 to 3530 of 3554

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TAP1 mutant mice are deficient in antigen presentation, surface class I molecules, and CD4-8+ T cells.
Van Kaer L, Ashton-Rickardt PG, Ploegh HL, Tonegawa S
(1992) Cell 71: 1205-14
MeSH Terms: Animals, Base Sequence, CD4 Antigens, CD8 Antigens, Cell Line, Chimera, Gene Expression Regulation, Genes, MHC Class I, Mice, Mice, Transgenic, Molecular Sequence Data, T-Lymphocytes
Show Abstract · Added December 10, 2013
The transporter associated with the antigen processing 1 (TAP1) gene encodes a subunit for a transporter, presumed to be involved in the delivery of peptides across the endoplasmic reticulum membrane to class I molecules. We have generated mice with a disrupted TAP1 gene using embryonic stem cell technology. TAP1-deficient mice are defective in the stable assembly and intracellular transport of class I molecules and consequently show severely reduced levels of surface class I molecules. These properties are strikingly similar to those described for the TAP2 mutant cell line RMA-S. Cells from the TAP1-deficient mice are unable to present cytosolic antigens to class I-restricted cytotoxic T cells. As predicted from the near absence of class I surface expression, TAP1-deficient mice lack CD4-8+ T cells.
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12 MeSH Terms
Complete human NF1 cDNA sequence: two alternatively spliced mRNAs and absence of expression in a neuroblastoma line.
Bernards A, Haase VH, Murthy AE, Menon A, Hannigan GE, Gusella JF
(1992) DNA Cell Biol 11: 727-34
MeSH Terms: Alternative Splicing, Amino Acid Sequence, Base Sequence, DNA, Gene Expression, Genes, Neurofibromatosis 1, Humans, Molecular Sequence Data, Mutation, Neuroblastoma, RNA, Messenger, Tumor Cells, Cultured
Show Abstract · Added August 19, 2013
Neurofibromatosis type 1 (NF1) is caused by mutations in a large gene on chromosome 17q11.2. Previously described partial cDNAs for this gene predicted a protein related to yeast IRA1/IRA2 and the mammalian RAS GTPase activator protein GAP. To initiate a detailed study of the role of this gene in NF1, we have characterized a set of overlapping cDNAs that represent its complete coding sequence. Our results show that two differentially expressed human NF1 mRNAs differ by a 63-bp insertion in the GAP-related domain. These mRNAs predict two 2,818- and 2,839-amino acid proteins with calculated molecular masses of approximately 317 and 319 kD. Extensive similarity to IRA proteins is evident in a 1,450-amino-acid central segment, roughly between amino acids 900 and 2,350. However, the remainder of the NF1 protein is not significantly similar to other proteins. Interestingly, the SK-N-SH human neuroblastoma line expresses no detectable NF1 mRNA, indicating that expression of NF1 is not essential for viability of this neural crest-derived tumor cell line.
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12 MeSH Terms
Reading-frame restoration with an apolipoprotein B gene frameshift mutation.
Linton MF, Pierotti V, Young SG
(1992) Proc Natl Acad Sci U S A 89: 11431-5
MeSH Terms: Alleles, Amino Acid Sequence, Animals, Apolipoproteins B, Base Sequence, DNA, Frameshift Mutation, Gene Expression, Genes, Humans, Hypobetalipoproteinemias, In Vitro Techniques, Molecular Sequence Data, Pedigree, RNA, Messenger, Rats, Transcription, Genetic, Tumor Cells, Cultured
Show Abstract · Added May 27, 2014
We examined a mutant human apolipoprotein B (apoB) allele that causes hypobetalipoproteinemia and has a single cytosine deletion in exon 26. This frameshift mutation was associated with the synthesis of a truncated apoB protein of the predicted size; however, studies in human subjects and minigene expression studies in cultured cells indicated that the mutant allele also yielded a full-length apoB protein. The 1-base-pair deletion in the mutant apoB allele created a stretch of eight consecutive adenines. To understand the mechanism whereby the mutant apoB allele yielded a full-length apoB protein, the cDNA from cells transfected with the mutant apoB minigene expression vector was examined. Splicing of the mRNA was normal; however, 11% of the cDNA clones had an additional adenine within the stretch of eight adenines, yielding nine consecutive adenines. The insertion of the extra adenine, presumably during apoB gene transcription, is predicted to restore the correct apoB reading frame, thereby permitting the synthesis of a full-length apoB protein.
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18 MeSH Terms
Induction of aP2 gene expression by nonmetabolized long-chain fatty acids.
Grimaldi PA, Knobel SM, Whitesell RR, Abumrad NA
(1992) Proc Natl Acad Sci U S A 89: 10930-4
MeSH Terms: Adipose Tissue, Animals, Arachidonic Acid, Biological Transport, Carrier Proteins, Cell Line, Coenzyme A Ligases, Dexamethasone, Fatty Acid-Binding Proteins, Gene Expression Regulation, Kinetics, Neoplasm Proteins, Palmitates, Palmitic Acid, Palmitic Acids, RNA, Messenger, Repressor Proteins, Saccharomyces cerevisiae Proteins
Show Abstract · Added December 10, 2013
Long-chain fatty acids (FA) have been shown to regulate expression of the gene for the adipocyte FA-binding protein aP2. We examined whether this effect was exerted by FA themselves or by a FA metabolite. The alpha-bromo derivative of palmitate, an inhibitor of FA oxidation, was synthesized in the radioactive form, and its metabolism was investigated and correlated with its ability to induce aP2 in Ob1771 preadipocytes. alpha-Bromopalmitate was not utilized by preadipocytes. It was not cleared from the medium over a 24-hr period and was not incorporated into cellular lipids. Short incubations indicated that alpha-bromopalmitate exchanged across the preadipocyte membrane but remained in the free form inside the cell. In line with this, preadipocyte homogenates did not activate alpha-bromopalmitate to the acyl form. However, although it was not metabolized, bromopalmitate was much more potent than native FA in inducing aP2 gene expression. Induction exhibited the characteristics previously described for native FA, indicating that a similar if not identical mechanism was involved. The data indicated that induction of aP2 was exerted by unprocessed FA. Finally, in contrast to preadipocytes, adipocytes metabolized bromopalmitate. This reflected increased activity with cell differentiation of a palmitoyl-CoA synthase that could activate palmitate and bromopalmitate at about one-fifth the rate for palmitate. In preadipocytes, the predominant fatty-acyl-CoA synthase, arachidonyl-CoA synthase, had very low affinity for both FA. Increased activity of the palmitoyl-CoA synthase, which has a wider substrate range, is likely to be important for initiation of lipid deposition.
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18 MeSH Terms
DVR-4 (bone morphogenetic protein-4) as a posterior-ventralizing factor in Xenopus mesoderm induction.
Jones CM, Lyons KM, Lapan PM, Wright CV, Hogan BL
(1992) Development 115: 639-47
MeSH Terms: Activins, Animals, Base Sequence, Bone Morphogenetic Proteins, Embryo, Nonmammalian, Embryonic Induction, Gene Expression, Growth Substances, Inhibins, Mesoderm, Microinjections, Molecular Sequence Data, Morphogenesis, Proteins, Xenopus laevis
Show Abstract · Added June 11, 2010
Establishment of mesodermal tissues in the amphibian body involves a series of inductive interactions probably elicited by a variety of peptide growth factors. Results reported here suggest that mesodermal patterning involves an array of signalling molecules including DVR-4, a TGF-beta-like molecule. We show that ectopic expression of DVR-4 causes embryos to develop with an overall posterior and/or ventral character, and that DVR-4 induces ventral types of mesoderm in animal cap explants. Moreover, DVR-4 overrides the dorsalizing effects of activin. DVR-4 is therefore the first molecule reported both to induce posteroventral mesoderm and to counteract dorsalizing signals such as activin. Possible interactions between these molecules resulting in establishment of the embryonic body plan are discussed.
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15 MeSH Terms
Differential regulation of transforming growth factor alpha autoinduction in a nontransformed and transformed epithelial cell.
Coffey RJ, Graves-Deal R, Dempsey PJ, Whitehead RH, Pittelkow MR
(1992) Cell Growth Differ 3: 347-54
MeSH Terms: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, Cell Line, Transformed, Colon, Gene Expression Regulation, Neoplastic, Humans, Isoquinolines, Keratinocytes, Piperazines, Protein Kinase C, RNA, Messenger, Signal Transduction, Transcription, Genetic, Transforming Growth Factor alpha
Show Abstract · Added March 27, 2014
Addition of transforming growth factor alpha (TGF-alpha) to cultured human keratinocytes results in enhanced expression of TGF-alpha mRNA. This phenomenon of TGF-alpha autoinduction is also observed in a TGF-alpha responsive colon cancer cell line, LIM 1215. In the present study, regulation of TGF-alpha autoinduction is examined in these two cell types. In human keratinocytes, but not in LIM 1215 cells, the increase in steady-state TGF-alpha mRNA following administration of TGF-alpha is due to stabilization of the 4.8-kilobase TGF-alpha transcript, as determined by actinomycin D decay curves. Nuclear run-on experiments confirmed transcriptional control in LIM 1215 cells. Basal and TGF-alpha-stimulated TGF-alpha expression is mediated, at least in part, through a protein kinase C-dependent pathway in both cell types, as determined by the protein kinase C inhibitor 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H7), which attenuates TGF-alpha mRNA accumulation. In the keratinocytes, but not in the LIM 1215 cells, basal TGF-alpha expression is mediated through an epidermal growth factor receptor-dependent pathway, as determined by antibody blockade of the epidermal growth factor receptor. Thus, differential regulation of TGF-alpha autoinduction exists in these nontransformed and transformed epithelial cell types.
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13 MeSH Terms
Transforming growth factor (TGF)-beta stimulates hepatic jun-B and fos-B proto-oncogenes and decreases albumin mRNA.
Beauchamp RD, Sheng HM, Ishizuka J, Townsend CM, Thompson JC
(1992) Ann Surg 216: 300-7; discussion 307-8
MeSH Terms: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, Albumins, Animals, Cells, Cultured, Down-Regulation, Gene Expression Regulation, Genes, fos, Genes, jun, Isoquinolines, Liver, Mice, Piperazines, Protein Kinase Inhibitors, RNA, Messenger, Sulfonamides, Tetradecanoylphorbol Acetate, Transforming Growth Factor beta
Show Abstract · Added May 3, 2013
Transforming growth factor-beta (TGF-beta) modulates some components of the acute phase response in hepatic cells. The mechanisms for these actions of TGF-beta are largely unknown. The authors recently found that the decrease in albumin mRNA after TGF-beta 1 treatment required de novo RNA and protein synthesis, suggesting that TGF-beta acts through induction of another gene. The purpose of the current study was to determine whether TGF-beta 1 could regulate the expression of both the jun and fos genes that encode transcriptional regulatory proteins that constitute the AP-1 complex, and to determine whether expression of these genes may be coordinated with the decrease in albumin mRNA. Northern blot hybridization was used to determine levels of specific mRNAs. Transforming growth factor-beta 1 increased the levels of both jun-B and fos-B mRNA by 60 minutes after treatment of mouse hepatoma (BWTG3) cells. When TGF-beta 1 was removed from the media after 4 hours, there was a sustained effect of increased jun-B and decreased albumin mRNA (greater than 48 hours), and the subsequent decrease in jun-B levels coincided with the increase in albumin mRNA. The tumor-promoting phorbol ester (phorbol 12-myristate 13-acetate [PMA]), known to induce jun and fos gene expression, caused increases in jun-B and fos-B that preceded the decrease in albumin mRNA levels at 24 hours. These observations are consistent with our hypothesis that jun-B and fos-B induction may participate in downregulation of albumin synthesis as well as other hepatic responses to TGF-beta.
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17 MeSH Terms
Downregulation of JE and KC genes by glucocorticoids does not prevent the G0----G1 transition in BALB/3T3 cells.
Rameh LE, Armelin MC
(1992) Mol Cell Biol 12: 4612-21
MeSH Terms: 3T3 Cells, Animals, Antigens, Polyomavirus Transforming, Base Sequence, Blotting, Northern, Chemokine CCL2, Chemokine CXCL1, Chemokines, Chemokines, CXC, Chemotactic Factors, Cycloheximide, Cytokines, DNA, Dexamethasone, Down-Regulation, G1 Phase, Gene Expression Regulation, Glucocorticoids, Hydrocortisone, Kinetics, Mice, Molecular Sequence Data, Proto-Oncogene Proteins c-jun, Resting Phase, Cell Cycle
Show Abstract · Added November 26, 2018
The effects of glucocorticoid hormones on the expression of the growth factor-inducible genes JE, KC, and c-myc were analyzed in parental BALB/3T3 and polyomavirus middle-T antigen-transfected cell lines. Northern (RNA) blot hybridization and run-on transcription analysis showed that (i) glucocorticoid hormones selectively inhibit JE and KC expression at the transcriptional level and (ii) the downregulatory effect of glucocorticoids on JE and KC expression is partial for serum-stimulated and middle T antigen-transformed cells and total for quiescent and exponentially growing cells. Gel mobility assays using AP-1 oligonucleotides showed a positive correlation between glucocorticoid downregulating effect and presence of the AP-1 complex. JE and KC downregulation by means of the AP-1 complex may play a role in the actions of glucocorticoids as anti-inflammatory and antitumor agents. The ability of glucocorticoids to downregulate JE and KC was used to investigate the relevance of these genes to the mitogenic response to serum growth factors. Hydrocortisone did not alter the basal DNA synthesis level displayed by quiescent 3T3 cells, but it potentiated both the mitogenic effect of platelet-derived growth factor and c-myc induction by serum growth factors. Upon serum restimulation, untreated and dexamethasone-treated quiescent 3T3 cultures entered the S phase after an identical time lag (G1). These results suggest that (i) JE and KC are not necessary for the G0----G1----S transition and (ii) c-myc overexpression is likely to be the basis for the potentiating effect of glucocorticoids on serum growth factors.
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Multiple elements in the upstream glucokinase promoter contribute to transcription in insulinoma cells.
Shelton KD, Franklin AJ, Khoor A, Beechem J, Magnuson MA
(1992) Mol Cell Biol 12: 4578-89
MeSH Terms: 3T3 Cells, Animals, Base Sequence, Cloning, Molecular, Cricetinae, DNA, Gene Expression Regulation, Enzymologic, Glucokinase, Insulin, Insulinoma, Islets of Langerhans, Mice, Molecular Sequence Data, Mutagenesis, Organ Specificity, Promoter Regions, Genetic, Transcription Factors, Transcription, Genetic, Transfection, Tumor Cells, Cultured
Show Abstract · Added February 23, 2011
beta-cell type-specific expression of the upstream glucokinase promoter was studied by transfection of fusion genes and analysis of DNA-protein interactions. A construct containing 1,000 bp of 5'-flanking DNA was efficiently expressed in HIT M2.2.2 cells, a beta-cell-derived line that makes both insulin and glucokinase, but not in NIH 3T3 cells, a heterologous cell line. In a series of 5' deletion mutations between bases -1000 and -100 (relative to a base previously designated +1), efficient expression in HIT cells was maintained until -280 bp, after which transcription decreased in a stepwise manner. The sequences between -180 and -1 bp contributing to transcriptional activity in HIT cells were identified by studying 28 block transversion mutants that spanned this region in 10-bp steps. Two mutations reduced transcription 10-fold or more, while six reduced transcription between 3- and 10-fold. Three mutationally sensitive regions of this promoter were found to bind to a factor that was expressed preferentially in pancreatic islet beta cells. The binding sites, designated upstream promoter elements (UPEs), shared a consensus sequence of CAT(T/C)A(C/G). Methylation of adenine and guanine residues within this sequence prevented binding of the beta-cell factor, as did mutations at positions 2, 3, and 5. Analysis of nuclear extracts from different cell lines identified UPE-binding activity in HIT M2.2.2 and beta-TC-3 cells but not in AtT-20, NIH 3T3, or HeLa cells; the possibility of a greatly reduced amount in alpha-TC-6 cells could not be excluded. UV laser cross-linking experiments supported the beta-cell type expression of this factor and showed it to be approximately 50 kDa in size. Gel mobility shift competition experiments showed that this beta-cell factor is the same that binds to similar elements, termed CT boxes, in the insulin promoter. Thus, a role for these elements (UPEs or CT boxes), and the beta-cell factor that binds to them, in determining the expression of genes in the beta cells of pancreatic islets is suggested.
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20 MeSH Terms
Amygdala kindling potentiates seizure-stimulated immediate-early gene expression in rat cerebral cortex.
Duman RS, Craig JS, Winston SM, Deutch AY, Hernandez TD
(1992) J Neurochem 59: 1753-60
MeSH Terms: Amygdala, Animals, Cerebral Cortex, Gene Expression Regulation, Genes, fos, Kindling, Neurologic, Male, Nerve Growth Factors, RNA, Messenger, Rats, Rats, Sprague-Dawley, Seizures
Show Abstract · Added May 27, 2014
Kindling induces long-term adaptations in neuronal function that lead to a decreased threshold for induction of seizures. In the present study, the influence of amygdala kindling on levels of mRNA for the immediate-early genes (IEGs) c-fos, c-jun, and NGF1-A were examined both before and after an acute electroconvulsive seizure (ECS). Although amygdala kindling did not significantly influence resting levels of c-fos mRNA in cerebral cortex, ECS-stimulated levels of c-fos mRNA (examined 45 min after ECS) were approximately twofold greater in the cerebral cortex of kindled rats relative to sham-treated controls. The influence of kindling on IEG expression was dependent on the time course of kindling, as ECS-stimulated levels of c-fos mRNA were not significantly increased in stage 2 kindled animals. ECS-stimulated levels of c-jun and NGF1-A mRNA were also significantly increased in cerebral cortex of kindled rats relative to sham-treated controls. The influence of kindling on IEG expression was long-lasting because an acute ECS stimulus significantly elevated levels of c-fos and c-jun mRNA in the cerebral cortex of animals that were kindled 5 months previously. In contrast to these effects in cerebral cortex, kindling did not influence ECS-stimulated levels of c-fos mRNA in hippocampus. Finally, immunohistochemical studies revealed lamina-specific changes in the cerebral cortex.(ABSTRACT TRUNCATED AT 250 WORDS)
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12 MeSH Terms