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Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation.
Tranguch S, Cheung-Flynn J, Daikoku T, Prapapanich V, Cox MB, Xie H, Wang H, Das SK, Smith DF, Dey SK
(2005) Proc Natl Acad Sci U S A 102: 14326-31
MeSH Terms: Animals, Blotting, Northern, Blotting, Southern, Down-Regulation, Embryo Implantation, Female, Histological Techniques, In Situ Hybridization, Mice, Mice, Inbred C57BL, Mice, Knockout, Molecular Chaperones, Progesterone, Receptors, Progesterone, Reverse Transcriptase Polymerase Chain Reaction, Tacrolimus Binding Proteins, Uterus
Show Abstract · Added March 9, 2015
Embryo implantation in the uterus is a critical step in mammalian reproduction, requiring preparation of the uterus receptive to blastocyst implantation. Uterine receptivity, also known as the window of implantation, lasts for a limited period, and it is during this period blastocysts normally implant. Ovarian steroid hormones estrogen and progesterone (P(4)) are the primary regulators of this process. The immunophilin FKBP52 serves as a cochaperone for steroid hormone nuclear receptors to govern appropriate hormone action in target tissues. Here we show a critical role for FKBP52 in mouse implantation. This immunophilin has unique spatiotemporal expression in the uterus during implantation, and females missing the Fkbp52 gene have complete implantation failure due to lack of attainment of uterine receptivity. The overlapping uterine expression of FKBP52 with nuclear progesterone receptor (PR) in wild-type mice together with reduced P(4) binding to PR, attenuated PR transcriptional activity and down-regulation of several P(4)-regulated genes in uteri of Fkbp52(-/-) mice, establishes this cochaperone as a critical regulator of uterine P(4) function. Interestingly, ovulation, another P(4)-mediated event, remains normal. Collectively, the present investigation provides evidence for an in vivo role for this cochaperone in regulating tissue-specific hormone action and its critical role in uterine receptivity for implantation.
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17 MeSH Terms
Loss of one allele of ARF rescues Mdm2 haploinsufficiency effects on apoptosis and lymphoma development.
Eischen CM, Alt JR, Wang P
(2004) Oncogene 23: 8931-40
MeSH Terms: ADP-Ribosylation Factor 1, Alleles, Animals, Apoptosis, B-Lymphocytes, Blotting, Southern, Blotting, Western, Cell Survival, Cyclin-Dependent Kinase Inhibitor p16, Flow Cytometry, Gamma Rays, Genes, p53, Lymphocytes, Lymphoma, Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Models, Biological, Nuclear Proteins, Phenotype, Proteome, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-mdm2, Sensitivity and Specificity, Sequence Analysis, DNA, Spleen, Time Factors, Transcription, Genetic, Transgenes, Tumor Suppressor Protein p14ARF, Tumor Suppressor Protein p53
Show Abstract · Added March 5, 2014
The tumor suppressor p19ARF inhibits Mdm2, which restricts the activity of p53. Complicated feedback and control mechanisms regulate ARF, Mdm2, and p53 interactions. Here we report that ARF haploinsufficiency completely rescued the p53-dependent effects of Mdm2 haploinsufficiency on B-cell development, survival, and transformation. In contrast to Mdm2+/- B cells, Mdm2+/- B cells deficient in ARF were similar to wild-type B cells in their rates of growth and apoptosis and activation of p53. Consequently, the profoundly reduced numbers of B cells in Mdm2+/-Emu-myc transgenic mice were restored to normal levels in ARF+/-Mdm2+/-Emu-myc transgenics. Additionally, ARF+/-Mdm2+/-Emu-myc transgenics developed lymphomas at rates analogous to those observed for wild-type Emu-myc transgenics, demonstrating that loss of one allele of ARF rescued the protracted lymphoma latency in Mdm2+/-Emu-myc transgenics. Importantly, in ARF+/-Mdm2+/-Emu-myc transgenic lymphomas, p53 was inactivated at the frequency observed in lymphomas of wild-type Emu-myc transgenics. Collectively, these results support a model whereby the stoichiometry of Mdm2 and ARF controls apoptosis and tumor development, which should have significant implications in the treatment of malignancies that have inactivated ARF.
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32 MeSH Terms
Aberrant cannabinoid signaling impairs oviductal transport of embryos.
Wang H, Guo Y, Wang D, Kingsley PJ, Marnett LJ, Das SK, DuBois RN, Dey SK
(2004) Nat Med 10: 1074-80
MeSH Terms: Adrenergic beta-Agonists, Animals, Arachidonic Acids, Blotting, Southern, Embryo Transfer, Fallopian Tubes, Female, Isoproterenol, Mice, Models, Genetic, Muscle Contraction, Norepinephrine, Ovum Transport, Pregnancy, Receptor, Cannabinoid, CB1, Reverse Transcriptase Polymerase Chain Reaction, Signal Transduction
Show Abstract · Added March 5, 2014
Ectopic pregnancy is a major reproductive health issue. Although other underlying causes remain largely unknown, one cause of ectopic pregnancy is embryo retention in the fallopian tube. Here we show that genetic or pharmacologic silencing of cannabinoid receptor CB1 causes retention of a large number of embryos in the mouse oviduct, eventually leading to pregnancy failure. This is reversed by isoproterenol, a beta-adrenergic receptor agonist. Impaired oviductal embryo transport is also observed in wild-type mice treated with methanandamide. Collectively, the results suggest that aberrant cannabinoid signaling impedes coordinated oviductal smooth muscle contraction and relaxation crucial to normal oviductal embryo transport. Colocalization of CB1 and beta2-adrenergic receptors in the oviduct muscularis implies that a basal endocannabinoid tone in collaboration with adrenergic receptors coordinates oviductal motility for normal journey of embryos into the uterus. Besides uncovering a new regulatory mechanism, this study could be clinically relevant to ectopic pregnancy.
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17 MeSH Terms
Dopamine D2-like antagonists induce chromatin remodeling in striatal neurons through cyclic AMP-protein kinase A and NMDA receptor signaling.
Li J, Guo Y, Schroeder FA, Youngs RM, Schmidt TW, Ferris C, Konradi C, Akbarian S
(2004) J Neurochem 90: 1117-31
MeSH Terms: Acetylation, Animals, Animals, Newborn, Blotting, Southern, Blotting, Western, Chromatin Assembly and Disassembly, Corpus Striatum, Cyclic AMP, Cyclic AMP-Dependent Protein Kinases, Dizocilpine Maleate, Dopamine Agents, Dopamine Antagonists, Dopamine D2 Receptor Antagonists, Drug Administration Routes, Drug Interactions, Enzyme Inhibitors, Excitatory Amino Acid Antagonists, Female, Genes, fos, Glial Fibrillary Acidic Protein, Glutamic Acid, Haloperidol, Histones, Immunohistochemistry, In Vitro Techniques, Indoles, Isoquinolines, Male, Methylation, Mice, Neurons, Phosphopyruvate Hydratase, Phosphorylation, RNA, Messenger, Rats, Rats, Sprague-Dawley, Receptors, AMPA, Receptors, Dopamine D2, Receptors, N-Methyl-D-Aspartate, Reverse Transcriptase Polymerase Chain Reaction, Sulfonamides, Thionucleotides, Time Factors
Show Abstract · Added May 27, 2014
Antipsychotic drugs regulate gene transcription in striatal neurons by blocking dopamine D2-like receptors. Little is known about the underlying changes in chromatin structure, including covalent modifications at histone N-terminal tails that are epigenetic regulators of gene expression. We show that treatment with D2-like antagonists rapidly induces the phosphorylation of histone H3 at serine 10 and the acetylation of H3-lysine 14 in bulk chromatin from striatum and in nuclei of striatal neurons. We find that, in vivo, D2-like antagonist-induced H3 phospho-acetylation is inhibited by the NMDA receptor antagonist MK-801 and by the protein kinase A (PKA) inhibitor Rp-adenosine 3c',5c'-cyclic monophosphorothioate triethylammonium salt but increased by the PKA activator Sp-adenosine 3c',5c'-cyclic monophosphorothioate triethylammonium salt. Furthermore, in dissociated striatal cultures which lack midbrain and cortical pre-synaptic inputs, H3 phospho-acetylation was induced by glutamate, L-type Ca2+ channel agonists and activators of cAMP-dependent PKA but inhibited by NMDA receptor antagonists or PKA antagonists. The dual modification, H3pS10-acK14, was enriched at genomic sites with active transcription and showed the kinetics of the early response. Together, these results suggest that histone modifications and chromatin structure in striatal neurons are dynamically regulated by dopaminergic and glutamatergic inputs converging on the cellular level. Blockade of D2-like receptors induces H3 phospho-acetylation, H3pS10-acK14, through cAMP-dependent PKA, and post-synaptic NMDA receptor signaling.
Copyright 2004 International Society for Neurochemistry
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43 MeSH Terms
Perp is a mediator of p53-dependent apoptosis in diverse cell types.
Ihrie RA, Reczek E, Horner JS, Khachatrian L, Sage J, Jacks T, Attardi LD
(2003) Curr Biol 13: 1985-90
MeSH Terms: Animals, Apoptosis, Blotting, Northern, Blotting, Southern, Gene Expression Profiling, In Situ Nick-End Labeling, Membrane Proteins, Mice, Mice, Mutant Strains, Tumor Suppressor Protein p53
Show Abstract · Added August 21, 2012
The induction of apoptosis by the p53 protein is critical for its activity as a tumor suppressor. Although it is clear that p53 induces apoptosis at least in part by direct transcriptional activation of target genes, the set of p53 target genes that mediate p53 function in apoptosis in vivo remains to be well defined. The Perp (p53 apoptosis effector related to PMP-22) gene is highly expressed in cells undergoing p53-dependent apoptosis as compared to cells undergoing p53-dependent G1 arrest. Perp is a direct p53 target, and its overexpression is sufficient to induce cell death in fibroblasts, implicating it as an important component of p53 apoptotic function. Here, through the generation of Perp-deficient mice, we analyze the role of Perp in the p53 apoptosis pathway in multiple primary cell types by comparing the cell death responses of Perp null cells to those of wild-type and p53 null cells. These experiments demonstrate the involvement of Perp in p53-mediated cell death in thymocytes and neurons but not in E1A-expressing MEFs, indicating a cell type-specific role for Perp in the p53 cell death pathway. In addition, we show that Perp is not required for proliferation-associated functions of p53. Thus, Perp selectively mediates the p53 apoptotic response, and the requirement for Perp is dictated by cellular context.
1 Communities
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10 MeSH Terms
NeuroD1/E47 regulates the E-box element of a novel zinc finger transcription factor, IA-1, in developing nervous system.
Breslin MB, Zhu M, Lan MS
(2003) J Biol Chem 278: 38991-7
MeSH Terms: Animals, Basic Helix-Loop-Helix Transcription Factors, Blotting, Northern, Blotting, Southern, Brain, DNA Mutational Analysis, DNA-Binding Proteins, Dimerization, Dose-Response Relationship, Drug, Gene Deletion, Genes, Reporter, HeLa Cells, Humans, Immunohistochemistry, Mice, Mice, Transgenic, Nervous System, Promoter Regions, Genetic, Repressor Proteins, Time Factors, Trans-Activators, Transcription, Genetic, Transgenes, Tumor Cells, Cultured, Zinc Fingers, beta-Galactosidase
Show Abstract · Added June 10, 2010
IA-1 is a novel zinc finger transcription factor with a restricted tissue distribution in the embryonic nervous system and tumors of neuroendocrine origin. The 1.7-kilobase 5'-upstream DNA sequence of the human IA-1 gene directed transgene expression predominantly in the developing nervous system including forebrain, midbrain, hindbrain, spinal cord, retina, olfactory bulb, and cerebellum, which recapitulated the expression patterns of neuroendocrine tissues and childhood brain tumors. The IA-1 promoter deletion reporter gene constructs revealed that the sequence between -426 and -65 bp containing three putative E-boxes (approximately 361 bp) upstream of the transcription start site was sufficient to confer tissue-specific transcriptional activity. Further mutation analysis revealed that the proximal E-box (E3) closest to the start site is critical to confer transcriptional activity. Electrophoretic mobility shift assay and transient transfection studies demonstrated that the NeuroD1 and E47 heterodimer are the key transcription factors that regulate the proximal E-box of the IA-1 promoter. Therefore, we concluded that the IA-1 gene is developmentally expressed in the nervous system and the NeuroD1/E47 transcription factors up-regulate IA-1 gene expression through the proximal E-box element of the IA-1 promoter.
1 Communities
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26 MeSH Terms
The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos.
Cao S, Bendall H, Hicks GG, Nashabi A, Sakano H, Shinkai Y, Gariglio M, Oltz EM, Ruley HE
(2003) Mol Cell Biol 23: 5301-7
MeSH Terms: Alleles, Animals, Apoptosis, Blotting, Southern, Blotting, Western, Cell Division, Cell Survival, DNA-Binding Proteins, Genes, p53, Genetic Vectors, Genotype, High Mobility Group Proteins, Homozygote, In Situ Nick-End Labeling, Mice, Models, Genetic, Mutation, Recombination, Genetic, Stem Cells, Time Factors
Show Abstract · Added May 29, 2014
The high-mobility-group (HMG) SSRP1 protein is a member of a conserved chromatin-remodeling complex (FACT/DUF/CP) implicated in DNA replication, basal and regulated transcription, and DNA repair. To assist in the functional analysis of SSRP1, the Ssrp1 gene was targeted in murine embryonic stem cells, and the mutation was introduced into the germ line. Embryos homozygous for the targeted allele die soon after implantation, and preimplantation blastocysts are defective for cell outgrowth and/or survival in vitro. The Ssrp1 mutation was also crossed into a p53 null background without affecting growth and/or survival defects caused by loss of Ssrp1 function. Thus, Ssrp1 appears to encode nonredundant and p53-independent functions that are essential for cell viability.
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20 MeSH Terms
Cell cycle-dependent transduction of cell-permeant Cre recombinase proteins.
Jo D, Lin Q, Nashabi A, Mays DJ, Unutmaz D, Pietenpol JA, Ruley HE
(2003) J Cell Biochem 89: 674-87
MeSH Terms: Amino Acid Sequence, Antineoplastic Agents, Biological Transport, Blotting, Southern, Cell Cycle, Cell Membrane Permeability, Cell Size, Cells, Cultured, DNA, Bacterial, Escherichia coli, Flow Cytometry, Genes, Reporter, Green Fluorescent Proteins, Integrases, Luminescent Proteins, Recombinant Fusion Proteins, Recombination, Genetic, Signal Transduction, Viral Proteins
Show Abstract · Added May 29, 2014
Protein transduction has been widely used to analyze biochemical processes in living cells quantitatively and under non-steady-state conditions. The present study analyzed the effects of cell cycle on the uptake and activity of cell-permeant Cre recombinase proteins. Previous studies had suggested that the efficiency of recombination and/or protein transduction varied among individual cells, even within a clonal population. We report here that cells in the G1 phase of the cell cycle undergo recombination at a lower rate than cells at other phases of the cell cycle, and that this variation results largely from differences in protein uptake, associated with differences in cell size. These results have implications regarding the mechanism of protein transduction and identify a source of heterogeneity that can influence the response of individual cells to cell-permeant proteins.
Copyright 2003 Wiley-Liss, Inc.
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19 MeSH Terms
Characterization of the CYP4A11 gene, a second CYP4A gene in humans.
Bellamine A, Wang Y, Waterman MR, Gainer JV, Dawson EP, Brown NJ, Capdevila JH
(2003) Arch Biochem Biophys 409: 221-7
MeSH Terms: Base Sequence, Blotting, Southern, Cloning, Molecular, Cytochrome P-450 CYP4A, Cytochrome P-450 Enzyme System, Exons, Gene Deletion, Humans, Hydroxyeicosatetraenoic Acids, Introns, Kidney, Mixed Function Oxygenases, Models, Genetic, Molecular Sequence Data, Polymerase Chain Reaction, Protein Isoforms, RNA, Reverse Transcriptase Polymerase Chain Reaction
Show Abstract · Added December 10, 2013
Comparison between the cDNA sequence of CYP4A11 and that deduced from a published genomic clone suggested the presence of an additional CYP4A gene in humans, CYP4A22. PCR amplification of genomic DNA yielded overlapping clones covering 13kb of genomic DNA and extending from 1003bp upstream from CYP4A11 translation initiation to 135bp upstream of the mRNA polyadenylation signal. Sequence and Southern blot analysis showed the presence in humans of two highly homologous CYP4A genes, CYP4A11 and CYP4A22. These two genes share 96% sequence identity and have similar intron/exon sizes and distribution. Short nucleotide insertions (< or =10bp) in introns 1, 3, 9, and 11, and deletions (< or =18bp) in introns 4, 6, and 11 differentiate the two genes. RT-PCR amplification of human kidney RNA followed by restriction fragment analysis showed that CYP4A11 is the predominant isoform expressed in kidney.
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18 MeSH Terms
The length of cytochrome c oxidase-negative segments in muscle fibres in patients with mtDNA myopathy.
Elson JL, Samuels DC, Johnson MA, Turnbull DM, Chinnery PF
(2002) Neuromuscul Disord 12: 858-64
MeSH Terms: Adult, Aged, Aged, 80 and over, Biopsy, Blotting, Southern, Cytochrome-c Oxidase Deficiency, DNA, Mitochondrial, Electron Transport Complex IV, Humans, Immunohistochemistry, Male, Mitochondrial Diseases, Mitochondrial Myopathies, Muscle Fibers, Skeletal, Muscle, Skeletal
Show Abstract · Added December 12, 2013
Heteroplasmic mitochondrial DNA mutations often cause a skeletal myopathy associated with a mosaic distribution of cytochrome c oxidase-deficient muscle fibres. The function of an individual muscle fibre is dependent upon the metabolic activity throughout its length, but little is known about the length of cytochrome c oxidase-deficient segments in human skeletal muscle in patients with mitochondrial disease. We studied cytochrome c oxidase activity by serial section analysis of quadriceps muscle from two patients. We observed a striking variation in the length of the cytochrome c oxidase-negative segments. The shortest segments were 10 microm long, and the longest segment was the entire length of the larger biopsy (> or =1.2 mm). The lengths of the cytochrome c oxidase-negative segments were generally shorter in the less severely affected biopsy, and we frequently observed non-contiguous segments of cytochrome c oxidase deficiency within the same muscle fibre. The findings have important implications for our understanding of the pathogenesis and progression of mitochondrial DNA myopathy.
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15 MeSH Terms