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Article ; Online: Borna disease virus docks on neuronal DNA double-strand breaks to replicate and dampens neuronal activity.

Marty, Florent Henri / Bettamin, Luca / Thouard, Anne / Bourgade, Karine / Allart, Sophie / Larrieu, Guilhem / Malnou, Cécile Evelyne / Gonzalez-Dunia, Daniel / Suberbielle, Elsa

iScience

2021 Volume 25, Issue 1, Page(s) 103621

Abstract: Borna disease viruses (BoDV) have recently emerged as zoonotic neurotropic pathogens. These persistent RNA viruses assemble nuclear replication centers (vSPOT) in close interaction with the host chromatin. However, the topology of this interaction and ... ...

Abstract	Borna disease viruses (BoDV) have recently emerged as zoonotic neurotropic pathogens. These persistent RNA viruses assemble nuclear replication centers (vSPOT) in close interaction with the host chromatin. However, the topology of this interaction and its consequences on neuronal function remain unexplored. In neurons, DNA double-strand breaks (DSB) have been identified as novel epigenetic mechanisms regulating neurotransmission and cognition. Activity-dependent DSB contribute critically to neuronal plasticity processes, which could be impaired upon infection. Here, we show that BoDV-1 infection, or the singled-out expression of viral Nucleoprotein and Phosphoprotein, increases neuronal DSB levels. Of interest, inducing DSB promoted the recruitment anew of vSPOT colocalized with DSB and increased viral RNA replication. BoDV-1 persistence decreased neuronal activity and response to stimulation by dampening the surface expression of glutamate receptors. Taken together, our results propose an original mechanistic cross talk between persistence of an RNA virus and neuronal function, through the control of DSB levels.
Language	English
Publishing date	2021-12-16
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2021.103621
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Article ; Online: Fatal encephalitis and Borna Disease Virus-1 seropositivity in two kidney-transplant patients living in the same nonendemic area.

Bourgade, Karine / Thouard, Anne / Abravanel, Florence / Hebral, Anne-Laure / Del Bello, Arnaud / Viguier, Alain / Gonzalez-Dunia, Daniel / Kamar, Nassim

Transplant infectious disease : an official journal of the Transplantation Society

2021 Volume 23, Issue 6, Page(s) e13734

MeSH term(s)	Animals ; Borna disease virus ; Encephalitis ; Humans ; Kidney ; Zoonoses
Language	English
Publishing date	2021-12-14
Publishing country	Denmark
Document type	Letter ; Comment
ZDB-ID	1476094-0
ISSN	1399-3062 ; 1398-2273
ISSN (online)	1399-3062
ISSN	1398-2273
DOI	10.1111/tid.13734
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Article ; Online: HSPA9/Mortalin mediates axo-protection and modulates mitochondrial dynamics in neurons.

Ferré, Cécile A / Thouard, Anne / Bétourné, Alexandre / Le Dorze, Anne-Louise / Belenguer, Pascale / Miquel, Marie-Christine / Peyrin, Jean-Michel / Gonzalez-Dunia, Daniel / Szelechowski, Marion

Scientific reports

2021 Volume 11, Issue 1, Page(s) 17705

Abstract: Mortalin is a mitochondrial chaperone protein involved in quality control of proteins imported into the mitochondrial matrix, which was recently described as a sensor of neuronal stress. Mortalin is down-regulated in neurons of patients with ... ...

Abstract	Mortalin is a mitochondrial chaperone protein involved in quality control of proteins imported into the mitochondrial matrix, which was recently described as a sensor of neuronal stress. Mortalin is down-regulated in neurons of patients with neurodegenerative diseases and levels of Mortalin expression are correlated with neuronal fate in animal models of Alzheimer's disease or cerebral ischemia. To date, however, the links between Mortalin levels, its impact on mitochondrial function and morphology and, ultimately, the initiation of neurodegeneration, are still unclear. In the present study, we used lentiviral vectors to over- or under-express Mortalin in primary neuronal cultures. We first analyzed the early events of neurodegeneration in the axonal compartment, using oriented neuronal cultures grown in microfluidic-based devices. We observed that Mortalin down-regulation induced mitochondrial fragmentation and axonal damage, whereas its over-expression conferred protection against axonal degeneration mediated by rotenone exposure. We next demonstrated that Mortalin levels modulated mitochondrial morphology by acting on DRP1 phosphorylation, thereby further illustrating the crucial implication of mitochondrial dynamics on neuronal fate in degenerative diseases.
MeSH term(s)	Animals ; Cerebral Cortex/drug effects ; Cerebral Cortex/metabolism ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Mitochondrial Dynamics/drug effects ; Mitochondrial Dynamics/physiology ; Neurons/drug effects ; Neurons/metabolism ; Rats ; Rats, Sprague-Dawley ; Rotenone/pharmacology
Chemical Substances	HSP70 Heat-Shock Proteins ; mortalin ; Rotenone (03L9OT429T)
Language	English
Publishing date	2021-09-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-97162-1
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Article ; Online: Conserved aromatic residues of the hepatitis B virus Precore propeptide are involved in a switch between distinct dimeric conformations and essential in the formation of heterocapsids.

Duriez, Marion / Thouard, Anne / Bressanelli, Stéphane / Rossignol, Jean-Michel / Sitterlin, Delphine

Virology

2014 Volume 462-463, Page(s) 273–282

Abstract: The Hepatitis B virus Precore protein, present in the secretory pathway as the HBeAg precursor, can associate in the cytoplasm with the Core protein to form heterocapsids, likely to favor viral persistence. Core and Precore proteins share their primary ... ...

Abstract	The Hepatitis B virus Precore protein, present in the secretory pathway as the HBeAg precursor, can associate in the cytoplasm with the Core protein to form heterocapsids, likely to favor viral persistence. Core and Precore proteins share their primary sequence except for ten additional aminoacids at the N-terminus of Precore. To address the role of this propeptide sequence in the formation of Precore heterocapsids, we designed a Precore mutant in which the two propeptide tryptophans are replaced by glycines. This mutant retains the properties of the wild-type Precore, notably cell trafficking and ability to interact with Core. However, it is not incorporated into heterocapsids and forms stable dimers distinct from the labile HBe dimers and the presumably Core-like dimers assembled into heterocapsids. Our data highlights the essential role of Precore׳s propeptide in switching between different conformations for different functions and pinpoint the propeptide Tryptophan residues as central in these properties.
MeSH term(s)	Amino Acid Substitution ; Cell Line ; Conserved Sequence ; Hepatitis B Core Antigens/genetics ; Hepatitis B Core Antigens/metabolism ; Hepatitis B virus/genetics ; Hepatitis B virus/physiology ; Humans ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Protein Conformation ; Protein Multimerization ; Protein Precursors/genetics ; Protein Precursors/metabolism
Chemical Substances	Hepatitis B Core Antigens ; Mutant Proteins ; Protein Precursors
Language	English
Publishing date	2014-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2014.06.013
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Article ; Online: Neuronal retrograde transport of Borna disease virus occurs in signalling endosomes.

Charlier, Caroline M / Debaisieux, Solène / Foret, Charlotte / Thouard, Anne / Schiavo, Giampietro / Gonzalez-Dunia, Daniel / Malnou, Cécile E

The Journal of general virology

2016 Volume 97, Issue 12, Page(s) 3215–3224

Abstract: Long-range axonal retrograde transport is a key mechanism for the cellular dissemination of neuroinvasive viruses, such as Borna disease virus (BDV), for which entry and egress sites are usually distant from the nucleus, where viral replication takes ... ...

Abstract	Long-range axonal retrograde transport is a key mechanism for the cellular dissemination of neuroinvasive viruses, such as Borna disease virus (BDV), for which entry and egress sites are usually distant from the nucleus, where viral replication takes place. Although BDV is known to disseminate very efficiently in neurons, both in vivo and in primary cultures, the modalities of its axonal transport are still poorly characterized. In this work, we combined different methodological approaches, such as confocal microscopy and biochemical purification of endosomes, to study BDV retrograde transport. We demonstrate that BDV ribonucleoparticles (composed of the viral genomic RNA, nucleoprotein and phosphoprotein), as well as the matrix protein, are transported towards the nucleus into endocytic carriers. These specialized organelles, called signalling endosomes, are notably used for the retrograde transport of neurotrophins and activated growth factor receptors. Signalling endosomes have a neutral luminal pH and thereby offer protection against degradation during long-range transport. This particularity could allow the viral particles to be delivered intact to the cell body of neurons, avoiding their premature release in the cytoplasm.
MeSH term(s)	Animals ; Borna Disease/metabolism ; Borna Disease/virology ; Borna disease virus/genetics ; Borna disease virus/metabolism ; Cell Nucleus/metabolism ; Cell Nucleus/virology ; Endosomes/metabolism ; Endosomes/virology ; Neurons/metabolism ; Neurons/virology ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Rats ; Rats, Sprague-Dawley ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virion/genetics ; Virion/metabolism
Chemical Substances	Phosphoproteins ; RNA, Viral ; Viral Proteins
Language	English
Publishing date	2016-11-08
Publishing country	England
Document type	Journal Article
ZDB-ID	219316-4
ISSN	1465-2099 ; 0022-1317
ISSN (online)	1465-2099
ISSN	0022-1317
DOI	10.1099/jgv.0.000652
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Article ; Online ; Research data: (with research data) Manipulation of the N-terminal sequence of the Borna disease virus X protein improves its mitochondrial targeting and neuroprotective potential.

Ferré, Cécile A / Davezac, Noélie / Thouard, Anne / Peyrin, Jean-Michel / Belenguer, Pascale / Miquel, Marie-Christine / Gonzalez-Dunia, Daniel / Szelechowski, Marion

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2016 Volume 30, Issue 4, Page(s) 1523–1533

Abstract: To favor their replication, viruses express proteins that target diverse mammalian cellular pathways. Due to the limited size of many viral genomes, such proteins are endowed with multiple functions, which require targeting to different subcellular ... ...

Abstract	To favor their replication, viruses express proteins that target diverse mammalian cellular pathways. Due to the limited size of many viral genomes, such proteins are endowed with multiple functions, which require targeting to different subcellular compartments. One salient example is the X protein of Borna disease virus, which is expressed both at the mitochondria and in the nucleus. Moreover, we recently demonstrated that mitochondrial X protein is neuroprotective. In this study, we sought to examine the mechanisms whereby the X protein transits between subcellular compartments and to define its localization signals, to enhance its mitochondrial accumulation and thus, potentially, its neuroprotective activity. We transfected plasmids expressing fusion proteins bearing different domains of X fused to enhanced green fluorescent protein (eGFP) and compared their subcellular localization to that of eGFP. We observed that the 5-16 domain of X was responsible for both nuclear export and mitochondrial targeting and identified critical residues for mitochondrial localization. We next took advantage of these findings and constructed mutant X proteins that were targeted only to the mitochondria. Such mutants exhibited enhanced neuroprotective properties in compartmented cultures of neurons grown in microfluidic chambers, thereby confirming the parallel between mitochondrial accumulation of the X protein and its neuroprotective potential.-Ferré C. A., Davezac, N., Thouard, A., Peyrin, J. M., Belenguer, P., Miquel, M.-C., Gonzalez-Dunia, D., Szelechowski, M. Manipulation of the N-terminal sequence of the Borna disease virus X protein improves its mitochondrial targeting and neuroprotective potential.
MeSH term(s)	Amino Acid Sequence ; Animals ; Aspartic Acid/genetics ; Aspartic Acid/metabolism ; Axons/drug effects ; Axons/metabolism ; Blotting, Western ; Borna disease virus/genetics ; Borna disease virus/metabolism ; COS Cells ; Cells, Cultured ; Cercopithecus aethiops ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Microscopy, Fluorescence ; Mitochondria/metabolism ; Molecular Sequence Data ; Mutation ; Neurons/cytology ; Neurons/drug effects ; Neurons/metabolism ; Nuclear Localization Signals/genetics ; Sequence Homology, Amino Acid ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Nuclear Localization Signals ; Viral Proteins ; Green Fluorescent Proteins (147336-22-9) ; Aspartic Acid (30KYC7MIAI)
Language	English
Publishing date	2016-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.15-279620
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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Hippocampal expression of a virus-derived protein impairs memory in mice.

Bétourné, Alexandre / Szelechowski, Marion / Thouard, Anne / Abrial, Erika / Jean, Arnaud / Zaidi, Falek / Foret, Charlotte / Bonnaud, Emilie M / Charlier, Caroline M / Suberbielle, Elsa / Malnou, Cécile E / Granon, Sylvie / Rampon, Claire / Gonzalez-Dunia, Daniel

Proceedings of the National Academy of Sciences of the United States of America

2018 Volume 115, Issue 7, Page(s) 1611–1616

Abstract: The analysis of the biology of neurotropic viruses, notably of their interference with cellular signaling, provides a useful tool to get further insight into the role of specific pathways in the control of behavioral functions. Here, we exploited the ... ...

Abstract	The analysis of the biology of neurotropic viruses, notably of their interference with cellular signaling, provides a useful tool to get further insight into the role of specific pathways in the control of behavioral functions. Here, we exploited the natural property of a viral protein identified as a major effector of behavioral disorders during infection. We used the phosphoprotein (P) of Borna disease virus, which acts as a decoy substrate for protein kinase C (PKC) when expressed in neurons and disrupts synaptic plasticity. By a lentiviral-based strategy, we directed the singled-out expression of P in the dentate gyrus of the hippocampus and we examined its impact on mouse behavior. Mice expressing the P protein displayed increased anxiety and impaired long-term memory in contextual and spatial memory tasks. Interestingly, these effects were dependent on P protein phosphorylation by PKC, as expression of a mutant form of P devoid of its PKC phosphorylation sites had no effect on these behaviors. We also revealed features of behavioral impairment induced by P protein expression but that were independent of its phosphorylation by PKC. Altogether, our findings provide insight into the behavioral correlates of viral infection, as well as into the impact of virus-mediated alterations of the PKC pathway on behavioral functions.
MeSH term(s)	Animals ; Borna Disease/metabolism ; Borna Disease/pathology ; Borna Disease/virology ; Borna disease virus/physiology ; Cells, Cultured ; Cognition Disorders/etiology ; Cognition Disorders/metabolism ; Cognition Disorders/pathology ; Dentate Gyrus/metabolism ; Dentate Gyrus/pathology ; Dentate Gyrus/virology ; Hippocampus/metabolism ; Hippocampus/pathology ; Hippocampus/virology ; Memory, Long-Term/physiology ; Mice ; Mutation ; Neuronal Plasticity ; Neurons/metabolism ; Neurons/pathology ; Neurons/virology ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Viral Structural Proteins/genetics ; Viral Structural Proteins/metabolism
Chemical Substances	P protein, Borna disease virus ; Phosphoproteins ; Viral Structural Proteins ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2018--13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1711977115
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Article ; Online: Borna disease virus phosphoprotein modulates epigenetic signaling in neurons to control viral replication.

Bonnaud, Emilie M / Szelechowski, Marion / Bétourné, Alexandre / Foret, Charlotte / Thouard, Anne / Gonzalez-Dunia, Daniel / Malnou, Cécile E

Journal of virology

2015 Volume 89, Issue 11, Page(s) 5996–6008

Abstract: Unlabelled: Understanding the modalities of interaction of neurotropic viruses with their target cells represents a major challenge that may improve our knowledge of many human neurological disorders for which viral origin is suspected. Borna disease ... ...

Abstract	Unlabelled: Understanding the modalities of interaction of neurotropic viruses with their target cells represents a major challenge that may improve our knowledge of many human neurological disorders for which viral origin is suspected. Borna disease virus (BDV) represents an ideal model to analyze the molecular mechanisms of viral persistence in neurons and its consequences for neuronal homeostasis. It is now established that BDV ensures its long-term maintenance in infected cells through a stable interaction of viral components with the host cell chromatin, in particular, with core histones. This has led to our hypothesis that such an interaction may trigger epigenetic changes in the host cell. Here, we focused on histone acetylation, which plays key roles in epigenetic regulation of gene expression, notably for neurons. We performed a comparative analysis of histone acetylation patterns of neurons infected or not infected by BDV, which revealed that infection decreases histone acetylation on selected lysine residues. We showed that the BDV phosphoprotein (P) is responsible for these perturbations, even when it is expressed alone independently of the viral context, and that this action depends on its phosphorylation by protein kinase C. We also demonstrated that BDV P inhibits cellular histone acetyltransferase activities. Finally, by pharmacologically manipulating cellular acetylation levels, we observed that inhibiting cellular acetyl transferases reduces viral replication in cell culture. Our findings reveal that manipulation of cellular epigenetics by BDV could be a means to modulate viral replication and thus illustrate a fascinating example of virus-host cell interaction. Importance: Persistent DNA viruses often subvert the mechanisms that regulate cellular chromatin dynamics, thereby benefitting from the resulting epigenetic changes to create a favorable milieu for their latent and persistent states. Here, we reasoned that Borna disease virus (BDV), the only RNA virus known to durably persist in the nucleus of infected cells, notably neurons, might employ a similar mechanism. In this study, we uncovered a novel modality of virus-cell interaction in which BDV phosphoprotein inhibits cellular histone acetylation by interfering with histone acetyltransferase activities. Manipulation of cellular histone acetylation is accompanied by a modulation of viral replication, revealing a perfect adaptation of this "ancient" virus to its host that may favor neuronal persistence and limit cellular damage.
MeSH term(s)	Acetylation ; Animals ; Borna disease virus/physiology ; Cells, Cultured ; Epigenesis, Genetic ; Histones/metabolism ; Host-Pathogen Interactions ; Neurons/virology ; Phosphoproteins/metabolism ; Protein Processing, Post-Translational ; Rats, Sprague-Dawley ; Viral Structural Proteins/metabolism ; Virus Replication
Chemical Substances	Histones ; P protein, Borna disease virus ; Phosphoproteins ; Viral Structural Proteins
Language	English
Publishing date	2015-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00454-15
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Article ; Online: A viral peptide that targets mitochondria protects against neuronal degeneration in models of Parkinson's disease.

Szelechowski, Marion / Bétourné, Alexandre / Monnet, Yann / Ferré, Cécile A / Thouard, Anne / Foret, Charlotte / Peyrin, Jean-Michel / Hunot, Stéphane / Gonzalez-Dunia, Daniel

Nature communications

2014 Volume 5, Page(s) 5181

Abstract: Mitochondrial dysfunction is a common feature of many neurodegenerative disorders, notably Parkinson's disease. Consequently, agents that protect mitochondria have strong therapeutic potential. Here, we sought to divert the natural strategy used by Borna ...

Abstract	Mitochondrial dysfunction is a common feature of many neurodegenerative disorders, notably Parkinson's disease. Consequently, agents that protect mitochondria have strong therapeutic potential. Here, we sought to divert the natural strategy used by Borna disease virus (BDV) to replicate in neurons without causing cell death. We show that the BDV X protein has strong axoprotective properties, thereby protecting neurons from degeneration both in tissue culture and in an animal model of Parkinson's disease, even when expressed alone outside of the viral context. We also show that intranasal administration of a cell-permeable peptide derived from the X protein is neuroprotective. We establish that both the X protein and the X-derived peptide act by buffering mitochondrial damage and inducing enhanced mitochondrial filamentation. Our results open the way to novel therapies for neurodegenerative diseases by targeting mitochondrial dynamics and thus preventing the earliest steps of neurodegenerative processes in axons.
MeSH term(s)	Animals ; Axons/metabolism ; Axons/physiology ; Disease Models, Animal ; Female ; HEK293 Cells ; Humans ; Male ; Membrane Potential, Mitochondrial ; Mice ; Mice, Inbred C57BL ; Microfluidics ; Microscopy, Confocal ; Microscopy, Fluorescence ; Mitochondria/pathology ; Neurodegenerative Diseases/prevention & control ; Neurodegenerative Diseases/virology ; Neurons/metabolism ; Parkinson Disease/prevention & control ; Parkinson Disease/virology ; Peptides/chemistry ; Phosphorylation ; Rats ; Rats, Sprague-Dawley ; Reactive Oxygen Species/metabolism ; Rotenone/chemistry ; Viral Nonstructural Proteins/chemistry
Chemical Substances	Peptides ; Reactive Oxygen Species ; Viral Nonstructural Proteins ; Rotenone (03L9OT429T)
Language	English
Publishing date	2014-10-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms6181
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Article ; Online: Effect of tryptase inhibition on joint inflammation: a pharmacological and lentivirus-mediated gene transfer study.

Denadai-Souza, Alexandre / Ribeiro, Camilla Moreira / Rolland, Corinne / Thouard, Anne / Deraison, Céline / Scavone, Cristoforo / Gonzalez-Dunia, Daniel / Vergnolle, Nathalie / Avellar, Maria Christina Werneck

Arthritis research & therapy

2017 Volume 19, Issue 1, Page(s) 124

Abstract: Background: Increasing evidences indicate that an unbalance between tryptases and their endogenous inhibitors, leading to an increased proteolytic activity, is implicated in the pathophysiology of rheumatoid arthritis. The aim of the present study was ... ...

Abstract	Background: Increasing evidences indicate that an unbalance between tryptases and their endogenous inhibitors, leading to an increased proteolytic activity, is implicated in the pathophysiology of rheumatoid arthritis. The aim of the present study was to evaluate the impact of tryptase inhibition on experimental arthritis. Methods: Analysis of gene expression and regulation in the mouse knee joint was performed by RT-qPCR and in situ hybridization. Arthritis was induced in male C57BL/6 mice with mBSA/IL-1β. Tryptase was inhibited by two approaches: a lentivirus-mediated heterologous expression of the human endogenous tryptase inhibitor, sperm-associated antigen 11B isoform C (hSPAG11B/C), or a chronic treatment with the synthetic tryptase inhibitor APC366. Several inflammatory parameters were evaluated, such as oedema formation, histopathology, production of IL-1β, -6, -17A and CXCL1/KC, myeloperoxidase and tryptase-like activities. Results: Spag11c was constitutively expressed in chondrocytes and cells from the synovial membrane in mice, but its expression did not change 7 days after the induction of arthritis, while tryptase expression and activity were upregulated. The intra-articular transduction of animals with the lentivirus phSPAG11B/C or the treatment with APC366 inhibited the increase of tryptase-like activity, the late phase of oedema formation, the production of IL-6 and CXCL1/KC. In contrast, neutrophil infiltration, degeneration of hyaline cartilage and erosion of subchondral bone were not affected. Conclusions: Tryptase inhibition was effective in inhibiting some inflammatory parameters associated to mBSA/IL-1β-induced arthritis, notably late phase oedema formation and IL-6 production, but not neutrophil infiltration and joint degeneration. These results suggest that the therapeutic application of tryptase inhibitors to rheumatoid arthritis would be restrained to palliative care, but not as disease-modifying drugs. Finally, this study highlighted lentivirus-based gene delivery as an instrumental tool to study the relevance of target genes in synovial joint physiology and disease.
Language	English
Publishing date	2017-06-06
Publishing country	England
Document type	Journal Article
ZDB-ID	2107602-9
ISSN	1478-6362 ; 1478-6354
ISSN (online)	1478-6362
ISSN	1478-6354
DOI	10.1186/s13075-017-1326-9
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