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Author (up) Aertsen, A.; Michiels, C.W. file  url
  Title SulA-dependent hypersensitivity to high pressure and hyperfilamentation after high-pressure treatment of Escherichia coli lon mutants Type Journal Article
  Year 2005 Publication Research in Microbiology Abbreviated Journal Res Microbiol  
  Volume 156 Issue 2 Pages 233-237  
  Keywords Colony Count, Microbial; Culture Media; Escherichia coli--genetics, growth & development; Escherichia coli Proteins--genetics, metabolism; Gene Expression Regulation, Bacterial; Hydrostatic Pressure; Mutation; Protease La--genetics; SOS Response (Genetics); Ultraviolet Rays  
  Abstract High-pressure treatment (>100 MPa) is known to induce several heat shock proteins as well as an SOS response in Escherichia coli. In the current work, we have investigated properties with respect to high-pressure treatment of mutants-deficient in Lon, a pressure-induced ATP-dependent protease that belongs to the heat shock regulon but that also has a link to the SOS regulon. We report that lon mutants show increased pressure sensitivity and exhibit hyperfilamentation during growth after high-pressure treatment. Both phenotypes could be entirely attributed to the action of the SOS protein SulA, a potent inhibitor of the cell division ring protein FtsZ and a specific target of the Lon protease, since they were suppressed by knock-out of SulA. Introduction of the lexA1 allele, which effectively blocks the entire SOS response, also suppressed the high pressure hypersensitivity of lon mutants, but not their UV hypersensitivity. These results indicate the existence of a SulA-dependent pathway of high-pressure-induced cell filamentation, and suggest involvement of the SOS response, and particularly of SulA, in high-pressure-mediated cell death in E. coli strains which are compromised in Lon function.  
  Call Number Serial 301  
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Author (up) Albuquerque, E.X.; Pereira, E.F.R.; Alkondon, M.; Rogers, S.W. file  url
  Title Mammalian nicotinic acetylcholine receptors: from structure to function Type Journal Article
  Year 2009 Publication Physiological Reviews Abbreviated Journal Physiol Rev  
  Volume 89 Issue 1 Pages 73-120  
  Keywords Alzheimer Disease/physiopathology; Animals; Brain/physiology; Disease Models, Animal; Gene Expression Regulation/physiology; Humans; Parkinson Disease/physiopathology; Receptors, Nicotinic/*chemistry/*physiology  
  Abstract The classical studies of nicotine by Langley at the turn of the 20th century introduced the concept of a “receptive substance,” from which the idea of a “receptor” came to light. Subsequent studies aided by the Torpedo electric organ, a rich source of muscle-type nicotinic receptors (nAChRs), and the discovery of alpha-bungarotoxin, a snake toxin that binds pseudo-irreversibly to the muscle nAChR, resulted in the muscle nAChR being the best characterized ligand-gated ion channel hitherto. With the advancement of functional and genetic studies in the late 1980s, the existence of nAChRs in the mammalian brain was confirmed and the realization that the numerous nAChR subtypes contribute to the psychoactive properties of nicotine and other drugs of abuse and to the neuropathology of various diseases, including Alzheimer's, Parkinson's, and schizophrenia, has since emerged. This review provides a comprehensive overview of these findings and the more recent revelations of the impact that the rich diversity in function and expression of this receptor family has on neuronal and nonneuronal cells throughout the body. Despite these numerous developments, our understanding of the contributions of specific neuronal nAChR subtypes to the many facets of physiology throughout the body remains in its infancy.  
  Call Number Serial 1876  
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Author (up) Ambrosone, A.; Costa, A.; Leone, A.; Grillo, S. file  url
doi  openurl
  Title Beyond transcription: RNA-binding proteins as emerging regulators of plant response to environmental constraints Type Journal Article
  Year 2012 Publication Plant Science : an International Journal of Experimental Plant Biology Abbreviated Journal Plant Sci  
  Volume 182 Issue Pages 12-18  
  Keywords Abscisic Acid/metabolism; Acclimatization/*physiology; Gene Expression Regulation, Plant; Osmotic Pressure/physiology; *Plant Physiological Processes; Plants/genetics; RNA-Binding Proteins/genetics/metabolism/*physiology; Transcription, Genetic  
  Abstract RNA-binding proteins (RBPs) govern many aspects of RNA metabolism, including pre-mRNA processing, transport, stability/decay and translation. Although relatively few plant RNA-binding proteins have been characterized genetically and biochemically, more than 200 RBP genes have been predicted in Arabidopsis and rice genomes, suggesting that they might serve specific plant functions. Besides their role in normal cellular functions, RBPs are emerging also as an interesting class of proteins involved in a wide range of post-transcriptional regulatory events that are important in providing plants with the ability to respond rapidly to changes in environmental conditions. Here, we review the most recent results and evidence on the functional role of RBPs in plant adaptation to various unfavourable environmental conditions and their contribution to enhance plant tolerance to abiotic stresses, with special emphasis on osmotic and temperature stress.  
  Call Number Serial 1226  
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Author (up) Baselga, J.; Pfister, D.; Cooper, M.R.; Cohen, R.; Burtness, B.; Bos, M.; D'Andrea, G.; Seidman, A.; Norton, L.; Gunnett, K.; Falcey, J.; Anderson, V.; Waksal, H.; Mendelsohn, J. file  url
  Title Phase I studies of anti-epidermal growth factor receptor chimeric antibody C225 alone and in combination with cisplatin Type Journal Article
  Year 2000 Publication Journal of Clinical Oncology : Official Journal of the American Society of Clinical Oncology Abbreviated Journal J Clin Oncol  
  Volume 18 Issue 4 Pages 904-914  
  Keywords Adult; Antibodies, Monoclonal/adverse effects/pharmacokinetics/*therapeutic use; Antibodies, Monoclonal, Humanized; Antineoplastic Agents/adverse effects/pharmacokinetics/*therapeutic use; Area Under Curve; Carcinoma, Non-Small-Cell Lung/drug therapy/therapy; Carcinoma, Squamous Cell/drug therapy/therapy; Cetuximab; Cisplatin/*therapeutic use; Dose-Response Relationship, Drug; Drug Administration Schedule; Female; Gene Expression Regulation, Neoplastic; Head and Neck Neoplasms/drug therapy/therapy; Humans; Infusions, Intravenous; Lung Neoplasms/drug therapy/therapy; Male; Neoplasms, Glandular and Epithelial/drug therapy/*therapy; Receptor, Epidermal Growth Factor/*antagonists & inhibitors/genetics; Recombinant Fusion Proteins/adverse effects/pharmacokinetics/*therapeutic use; Remission Induction; Safety  
  Abstract PURPOSE: The epidermal growth factor (EGF) receptor is frequently overexpressed in epithelial tumors. C225 is a human-to-murine chimeric monoclonal antibody that binds to the receptor and inhibits growth of cancer cells expressing the receptor. We evaluated the pharmacokinetics and toxicity of C225 in patients with advanced tumors overexpressing EGF receptors. PATIENTS AND METHODS: We treated 52 patients in three successive phase I clinical trials of C225 as a single dose (n = 13), weekly multiple dose (n = 17), and weekly multiple dose with cisplatin (n = 22). C225 dose levels were 5, 20, 50, and 100 mg/m(2). In the study combining C225 with cisplatin, limited to patients with either head and neck or non-small-cell lung cancer, C225 was further escalated to 200 and 400 mg/m(2). Cisplatin was given at a dose of 60 mg/m(2) once every 4 weeks, and treatment was continued for up to 12 weeks if no disease progression occurred. RESULTS: C225 displayed nonlinear pharmacokinetics, with antibody doses in the range of 200 to 400 mg/m(2) being associated with complete saturation of systemic clearance. C225 clearance did not change with repeated administration or with coadministration of cisplatin. Antibodies against C225 were detected in only one patient, and C225-associated toxicity was minimal. Patients experiencing disease stabilization were seen in all studies. In the study combining C225 and cisplatin, nine (69%) of 13 patients treated with antibody doses >/= 50 mg/m(2) completed 12 weeks of therapy, and two partial responses were observed. CONCLUSION: C225 has dose-dependent pharmacokinetics, and doses that achieve saturation of systemic clearance are well tolerated. C225 given in combination with cisplatin has biologic activity at pharmacologically relevant doses.  
  Call Number Serial 2015  
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Author (up) Bourne, G.L.; Grainger, D.J. file  url
  Title Development and characterisation of an assay for furin activity Type Journal Article
  Year 2011 Publication Journal of Immunological Methods Abbreviated Journal J Immunol Methods  
  Volume 364 Issue 1-2 Pages 101-108  
  Keywords Anoxia/diagnosis/genetics/*metabolism; Antibodies/immunology/*metabolism; Biochemistry/methods; Cell Extracts/chemistry; Furin/*genetics/immunology/*metabolism; Gene Expression Regulation, Enzymologic; Hep G2 Cells; Humans; Immunomodulation; *Immunosorbent Techniques; RNA, Messenger/*analysis; Reference Standards; Sensitivity and Specificity; Transforming Growth Factor beta/immunology/metabolism  
  Abstract Furin is a serine endoprotease that is responsible for the proteolytic processing of proteins within the secretory pathway, including cytokines, hormones, integrins, other proteases, and also pathogen-derived proteins. It is likely that the level of furin activity determines the extent of processing of these substrates. Furin is ubiquitously expressed across all tissues, at low levels, but can be induced in response to environmental cues such as hypoxia and cytokine stimulation. However, all studies to date that have investigated furin expression have been limited to analysis of furin mRNA; there has been no assay sensitive enough to quantify endogenous furin. Though activity-based assays have been described for furin-like enzyme activity, we demonstrate that these assays are dominated by the activity of other enzymes and cannot be used to approximate furin activity. A sensitive and specific assay for furin activity was therefore developed and characterised, using an antibody capture step to immobilise furin from whole cell lysates. Furin activity is quantified relative to that of recombinant active furin protein, to allow estimation of active furin protein concentration. The assay has a minimum detection limit of 0.006 nM; sensitive enough to determine the furin activity of many of the cell lines tested. The specificity of the assay was demonstrated by genetic modulation of furin expression. Furthermore, the assay was used to demonstrate that the cytokine transforming growth factor beta (TGF-beta) stimulates increased furin activity in HepG2 cells, confirming and extending previous reports that TGF-beta increases furin expression, and adding to the mounting body of evidence that cellular furin activity can be modulated.  
  Call Number Serial 525  
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Author (up) Cabiscol, E.; Tamarit, J.; Ros, J. file  url
  Title Oxidative stress in bacteria and protein damage by reactive oxygen species Type Journal Article
  Year 2000 Publication International Microbiology : the Official Journal of the Spanish Society for Microbiology Abbreviated Journal Int Microbiol  
  Volume 3 Issue 1 Pages 3-8  
  Keywords Adaptation, Physiological; Aerobiosis; Amino Acids/chemistry; Bacteria/genetics/*metabolism; Bacterial Proteins/genetics/*metabolism/*physiology; DNA Damage; DNA, Bacterial/genetics/metabolism; *DNA-Binding Proteins; *Escherichia coli Proteins; Free Radicals; Gene Expression Regulation, Bacterial; Heat-Shock Proteins/metabolism; Iron-Sulfur Proteins/metabolism; Lipid Peroxidation; Oxidation-Reduction; Oxidative Stress/*genetics/physiology; Peroxides/metabolism; Reactive Oxygen Species/*metabolism; Repressor Proteins/genetics/*physiology; *Trans-Activators; Transcription Factors/genetics/*physiology; Transcription, Genetic  
  Abstract The advent of O2 in the atmosphere was among the first major pollution events occurred on earth. The reaction between ferrous iron, very abundant in the reductive early atmosphere, and oxygen results in the formation of harmful superoxide and hydroxyl radicals, which affect all macromolecules (DNA, lipids and proteins). Living organisms have to build up mechanisms to protect themselves against oxidative stress, with enzymes such as catalase and superoxide dismutase, small proteins like thioredoxin and glutaredoxin, and molecules such as glutathione. Bacterial genetic responses to oxidative stress are controlled by two major transcriptional regulators (OxyR and SoxRS). This paper reviews major key points in the generation of reactive oxygen species in bacteria, defense mechanisms and genetic responses to oxidative stress. Special attention is paid to the oxidative damage to proteins.  
  Call Number Serial 181  
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Author (up) Cho, J.H.; Bandyopadhyay, J.; Lee, J.; Park, C.S.; Ahnn, J. file  url
  Title Two isoforms of sarco/endoplasmic reticulum calcium ATPase (SERCA) are essential in Caenorhabditis elegans Type Journal Article
  Year 2000 Publication Gene Abbreviated Journal Gene  
  Volume 261 Issue 2 Pages 211-219  
  Keywords Alternative Splicing; Amino Acid Sequence; Animals; Caenorhabditis elegans/embryology/enzymology/*genetics; Calcium-Transporting ATPases/*genetics/metabolism; Embryo, Nonmammalian/drug effects/enzymology; Embryonic Development; Gene Expression Regulation, Enzymologic; Green Fluorescent Proteins; Isoenzymes/genetics/metabolism; Luminescent Proteins/genetics/metabolism; Microscopy, Fluorescence; Molecular Sequence Data; Phenotype; Promoter Regions, Genetic/genetics; RNA, Double-Stranded/administration & dosage/genetics; Recombinant Fusion Proteins/genetics/metabolism; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Sequence Homology, Amino Acid; Tissue Distribution  
  Abstract SERCA (Sarco/Endoplasmic Reticulum Calcium ATPase), a membrane bound Ca(2+)- /Mg(2+)- dependent ATPase that sequesters Ca(2+) into the SR/ER lumen, is one of the essential components for the maintenance of intracellular Ca(2+) homeostasis. Here we describe the identification and functional characterization of a C. elegans SERCA gene (ser-1). ser-1 is a single gene alternatively spliced at its carboxyl terminus to form two isoforms (SER-1A and SER-1B) and displays a high homology (70% identity, 80% similarity) with mammalian SERCAs. Green fluorescent protein (GFP) and whole-mount immunostaining analyses reveal that SER-1 expresses in neuronal cells, body-wall muscles, pharyngeal and vulval muscles, excretory cells, and vulva epithelial cells. Furthermore, SER-1::GFP expresses during embryonic stages and the expression is maintained through the adult stages. Double-stranded RNA injection (also known as RNAi) targeted to each SER-1 isoform results in severe phenotypic defects: ser-1A(RNAi) animals show embryonic lethality, whereas ser-1B(RNAi) results in L1 larval arrest phenotype. These findings suggest that both isoforms of C. elegans SERCA, like in mammals, are essential for embryonic development and post-embryonic growth and survival.  
  Call Number Serial 451  
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Author (up) Cleary, M.D.; Meiering, C.D.; Jan, E.; Guymon, R.; Boothroyd, J.C. file  url
  Title Biosynthetic labeling of RNA with uracil phosphoribosyltransferase allows cell-specific microarray analysis of mRNA synthesis and decay Type Journal Article
  Year 2005 Publication Nature Biotechnology Abbreviated Journal Nat Biotechnol  
  Volume 23 Issue 2 Pages 232-237  
  Keywords Animals; Gene Expression Profiling/*methods; Gene Expression Regulation/*physiology; Humans; Metabolic Clearance Rate; Oligonucleotide Array Sequence Analysis/*methods; Pentosyltransferases/chemistry/*metabolism; RNA, Messenger/chemistry/*genetics/*metabolism; Signal Transduction/physiology; Staining and Labeling/methods; Toxoplasma/genetics/metabolism; Transcription Factors/*metabolism; Transcriptional Activation/*physiology  
  Abstract Standard microarrays measure mRNA abundance, not mRNA synthesis, and therefore cannot identify the mechanisms that regulate gene expression. We have developed a method to overcome this limitation by using the salvage enzyme uracil phosphoribosyltransferase (UPRT) from the protozoan Toxoplasma gondii. T. gondii UPRT has been well characterized because of its application in monitoring parasite growth: mammals lack this enzyme activity and thus only the parasite incorporates (3)H-uracil into its nucleic acids. In this study we used RNA labeling by UPRT to determine the roles of mRNA synthesis and decay in the control of gene expression during T. gondii asexual development. We also used this approach to specifically label parasite RNA during a mouse infection and to incorporate thio-substituted uridines into the RNA of human cells engineered to express T. gondii UPRT, indicating that engineered UPRT expression will allow cell-specific analysis of gene expression in organisms other than T. gondii.  
  Call Number Serial 1344  
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Author (up) Culmsee, C.; Mattson, M.P. file  url
  Title p53 in neuronal apoptosis Type Journal Article
  Year 2005 Publication Biochemical and Biophysical Research Communications Abbreviated Journal Biochem Biophys Res Commun  
  Volume 331 Issue 3 Pages 761-777  
  Keywords Animals; Apoptosis/*physiology; Apoptosis Regulatory Proteins; DNA Damage; Gene Expression Regulation; Humans; Neurodegenerative Diseases/*physiopathology; Neurons/*cytology/*physiology; Nuclear Proteins/physiology; Proto-Oncogene Proteins/physiology; Proto-Oncogene Proteins c-bcl-2/physiology; Proto-Oncogene Proteins c-mdm2; Synapses/physiology; Transcriptional Activation; Tumor Suppressor Protein p53/*physiology; bcl-2-Associated X Protein  
  Abstract The tumor suppressor and transcription factor p53 is a key modulator of cellular stress responses, and activation of p53 can trigger apoptosis in many cell types including neurons. Apoptosis is a form of programmed cell death that occurs in neurons during development of the nervous system and may also be responsible for neuronal deaths that occur in neurological disorders such as stroke, and Alzheimer's and Parkinson's diseases. p53 production is rapidly increased in neurons in response to a range of insults including DNA damage, oxidative stress, metabolic compromise, and cellular calcium overload. Target genes induced by p53 in neurons include those encoding the pro-apoptotic proteins Bax and the BH3-only proteins PUMA and Noxa. In addition to such transcriptional control of the cell death machinery, p53 may more directly trigger apoptosis by acting at the level of mitochondria, a process that can occur in synapses (synaptic apoptosis). Preclinical data suggest that agents that inhibit p53 may be effective therapeutics for several neurodegenerative conditions.  
  Call Number Serial 2167  
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Author (up) Ducey, T.F.; Jackson, L.; Orvis, J.; Dyer, D.W. file  url
doi  openurl
  Title Transcript analysis of nrrF, a Fur repressed sRNA of Neisseria gonorrhoeae Type Journal Article
  Year 2009 Publication Microbial Pathogenesis Abbreviated Journal Microb Pathog  
  Volume 46 Issue 3 Pages 166-170  
  Keywords Bacterial Proteins/*physiology; Base Sequence; Escherichia coli; Gene Expression Profiling; *Gene Expression Regulation, Bacterial; Models, Molecular; Molecular Sequence Data; Neisseria gonorrhoeae/*physiology; RNA, Bacterial/*genetics; RNA, Untranslated/*metabolism; Repressor Proteins/*physiology; Transcription Initiation Site  
  Abstract Like most microorganisms, Neisseria gonorrhoeae alters gene expression in response to iron availability. The ferric uptake regulator Fur has been shown to be involved in controlling this response, but the extent of this involvement remains unknown. It is known that in addition to working directly to repress gene expression, Fur may also work indirectly by controlling additional regulatory elements. Using in silico analysis, we identified a putative small RNA (sRNA) homolog of the meningococcal nrrF locus, and demonstrate that this sRNA is iron-repressible, suggesting that this is the gonococcal analog of the rhyB locus in Escherichia coli. Quantitative real-time RT-PCR analysis indicates that this transcript may also be temporally regulated. Transcript analysis identified the 5' start of the transcript, using a single reaction, fluorescent-based, primer extension assay. This protocol allows for the rapid identification of transcriptional start sites of RNA transcripts, and could be used for high-throughput transcript mapping.  
  Call Number Serial 417  
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