LIVIVO - Search results -

Search results

Result 1 - 8 of total 8

Search options

Article ; Online: A RaPID Macrocyclic Peptide That Inhibits the Formation of α-Synuclein Amyloid Fibrils.

Ikenoue, Tatsuya / Oono, Miki / So, Masatomo / Yamakado, Hodaka / Arata, Toshiaki / Takahashi, Ryosuke / Kawata, Yasushi / Suga, Hiroaki

Chembiochem : a European journal of chemical biology

2023 Volume 24, Issue 12, Page(s) e202300320

Abstract: There is considerable interest in drug discovery targeting the aggregation of α-synuclein (αSyn) since this molecular process is closely associated with Parkinson's disease. However, inhibiting αSyn aggregation remains a major challenge because of its ... ...

Abstract	There is considerable interest in drug discovery targeting the aggregation of α-synuclein (αSyn) since this molecular process is closely associated with Parkinson's disease. However, inhibiting αSyn aggregation remains a major challenge because of its highly dynamic nature which makes it difficult to form a stable binding complex with a drug molecule. Here, by exploiting Random non-standard Peptides Integrated Discovery (RaPID) system, we identified a macrocyclic peptide, BD1, that could interact with immobilized αSyn and inhibit the formation of fibrils. Furthermore, improving the solubility of BD1 suppresses the co-aggregation with αSyn fibrils while it kinetically inhibits more effectively without change in their morphology. We also revealed the molecular mechanism of kinetic inhibition, where peptides bind to fibril ends of αSyn, thereby preventing further growth of fibrils. These results suggest that our approach for generating non-standard macrocyclic peptides is a promising approach for developing potential therapeutics against neurodegeneration.
MeSH term(s)	Humans ; alpha-Synuclein/metabolism ; Amyloid/chemistry ; Parkinson Disease/drug therapy ; Parkinson Disease/metabolism ; Peptides/pharmacology ; Kinetics
Chemical Substances	alpha-Synuclein ; Amyloid ; Peptides
Language	English
Publishing date	2023-05-16
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202300320
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- Full text online
- Order with fees

Article ; Online: Rheumatoid meningitis developed in patient with stable rheumatoid arthritis and myasthenia gravis-detailed analysis of intracranial inflammation using flow cytometry.

Oono, Miki / Fujita, Yoshimasa / Uchida, Nobuaki / Kawai, Ukichiro / Fujita-Nakata, Michiyo / Nakanishi, Megumi / Sanada, Mitsuru / Nagayama, Shigemi / Matsui, Makoto

Journal of neuroinflammation

2018 Volume 15, Issue 1, Page(s) 151

Abstract: Background: Rheumatoid meningitis (RM) is a rare disorder that often develops during a remission phase of rheumatoid arthritis (RA). This is the first study to demonstrate differences in regard to immunological disturbance between blood and ... ...

Abstract	Background: Rheumatoid meningitis (RM) is a rare disorder that often develops during a remission phase of rheumatoid arthritis (RA). This is the first study to demonstrate differences in regard to immunological disturbance between blood and cerebrospinal fluid (CSF) samples obtained from a patient with RM using flow cytometry. Case presentation: A 36-year-old woman with RA and generalized myasthenia gravis (MG) developed RM during a remission phase. Although both RA and MG were stable and well controlled, she noticed fever, headache, and transient sensory disturbance. Blood and CSF examination findings suggested aseptic meningitis, while brain magnetic resonance imaging revealed restricted portions of meningitis and associated cortical lesions, compatible with a diagnosis of RM. The dose of oral prednisolone was increased, which ameliorated the symptoms within 1 week along with improvement in CSF findings. This patient exhibited features of RM that were manifested in a manner independent of the activity of RA. An investigation of cellular immunity using CSF specimens with flow cytometry showed differences in regard to the pathogenesis of inflammation in the CSF as compared to outside of the central nervous system. In contrast to results obtained with paired blood samples, CSF cells at the peak stage of RM showed a marked increase in CCR3 Conclusions: RM is not a simple reflection of the immune status of RA, as the pathogenesis seems related to, at least in part, CSF-specific immunological dysregulation.
MeSH term(s)	Adult ; Anti-Inflammatory Agents/therapeutic use ; Antigens, CD/metabolism ; Arthritis, Rheumatoid/complications ; Arthritis, Rheumatoid/diagnostic imaging ; Female ; Flow Cytometry/methods ; Humans ; Inflammation/diagnostic imaging ; Inflammation/etiology ; Magnetic Resonance Imaging ; Meningitis/diagnostic imaging ; Meningitis/drug therapy ; Meningitis/etiology ; Meningitis/immunology ; Myasthenia Gravis/complications ; Myasthenia Gravis/diagnostic imaging ; Prednisolone/therapeutic use ; Treatment Outcome
Chemical Substances	Anti-Inflammatory Agents ; Antigens, CD ; Prednisolone (9PHQ9Y1OLM)
Language	English
Publishing date	2018-05-18
Publishing country	England
Document type	Case Reports ; Journal Article
ISSN	1742-2094
ISSN (online)	1742-2094
DOI	10.1186/s12974-018-1196-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Severe and prolonged ictal paresis in an elderly patient.

Oono, Miki / Uno, Hisakazu / Umesaki, Arisa / Nagatsuka, Kazuyuki / Kinoshita, Masako / Naritomi, Hiroaki

Epilepsy & behavior case reports

2014 Volume 2, Page(s) 105–107

Abstract: We report an 84-year-old female who showed a rare manifestation of epilepsy, ictal paresis, a type of simple partial seizure presenting with focal motor dysfunction. While the patient exhibited severe left hemiplegia which lasted for a week, cranial ... ...

Abstract	We report an 84-year-old female who showed a rare manifestation of epilepsy, ictal paresis, a type of simple partial seizure presenting with focal motor dysfunction. While the patient exhibited severe left hemiplegia which lasted for a week, cranial diffusion-weighted MRI demonstrated slightly high intensity in the right posterior quadrant, and electroencephalography (EEG) showed continuous epileptiform discharges located mainly in the right parieto-occipital area, strongly suggesting that the patient was in an ictal state. (99m)Tc-hexamethylpropylene amine oxime-single photon emission computed tomography (HMPAO-SPECT) showed markedly high blood perfusion in the right parieto-temporo-occipital areas. Considering the distribution of EEG epileptiform activities and HMPAO-SPECT hyperperfusion, it is most likely that the ictal paresis of our patient was associated with epileptic activities at the sensorimotor area which caused either direct or indirect activation of an inhibitory system. Careful clinical consideration of the possibility of ictal paresis is needed in elderly patients, especially in those with preexisting dementia, because paresis can be as severe as complete flaccid hemiplegia and can last as long as for a week.
Language	English
Publishing date	2014-05-04
Publishing country	United States
Document type	Case Reports
ZDB-ID	2708718-9
ISSN	2213-3232
ISSN	2213-3232
DOI	10.1016/j.ebcr.2014.03.009
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: [Trial of rituximab in three patients with neuromyelitis optica].

Imamura, Hisaji / Tanaka, Masami / Kitagawa, Naoyuki / Tahara, Masayuki / Oono, Miki / Tanaka, Keiko / Konishi, Tetsuro

Rinsho shinkeigaku = Clinical neurology

2009 Volume 49, Issue 8, Page(s) 457–462

Abstract: Patients with relapsing neuromyelitis optica (NMO) showing contiguous long spinal cord lesions extending over three vertebral segments on the MRI and with positive anti-aquaporin 4 antibodies in sera are usually treated with glucocorticoids or ... ...

Abstract	Patients with relapsing neuromyelitis optica (NMO) showing contiguous long spinal cord lesions extending over three vertebral segments on the MRI and with positive anti-aquaporin 4 antibodies in sera are usually treated with glucocorticoids or azathioprine. However, some NMO patients even after adequate treatments show relapses. Rituximab (anti-CD 20) therapy has recently been reported to inhibit relapses. We used rituximab to treat three NMO patients defined by the revised NMO criteria of Wingerchuk et al, with rituximab for 2 years and 3 months (mean) at an intervals of about nine months. The annualized relapse rate for the 3 patients during the year before rituximab therapy was 4, 5, and 6, respectively, and this decreased to 3, 1, and 0 in the year after therapy. Case 1 showed three relapses after therapy: however, the symptoms and signs of each of the relapses were milder and the patient showed good responses to steroid pulse therapy. One year after therapy, relapses had disappeared in all cases (observation periods; 18, 18, and 9 months, respectively). After rituximab therapy, these NMO patients showed a decreased mean annualized relapse rate (from 5.0 to 0.6) and EDSS score (from 8.7 to 8.0) after rituximab therapy. No adverse effects were seen. We recommend rituximab therapy for NMO patients resistant to other immunosuppressive therapies such as oral glucocorticoid administration introduced after a severe relapse. However, during long term rituximab treatment, attention needs to be given to infections such as progressive multifocal leucoencephalopathy.
MeSH term(s)	Adult ; Antibodies, Monoclonal/administration & dosage ; Antibodies, Monoclonal, Murine-Derived ; Drug Administration Schedule ; Female ; Humans ; Immunologic Factors/administration & dosage ; Infusions, Intravenous ; Middle Aged ; Neuromyelitis Optica/drug therapy ; Rituximab ; Secondary Prevention ; Time Factors ; Treatment Outcome
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Monoclonal, Murine-Derived ; Immunologic Factors ; Rituximab (4F4X42SYQ6)
Language	Japanese
Publishing date	2009-10-12
Publishing country	Japan
Document type	Case Reports ; English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604200-4
ISSN	1882-0654 ; 0009-918X
ISSN (online)	1882-0654
ISSN	0009-918X
DOI	10.5692/clinicalneurol.49.457
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 1455: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 223: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Conserved acidic amino acid residues in a second RNA recognition motif regulate assembly and function of TDP-43.

Shodai, Akemi / Ido, Akemi / Fujiwara, Noriko / Ayaki, Takashi / Morimura, Toshifumi / Oono, Miki / Uchida, Tsukasa / Takahashi, Ryosuke / Ito, Hidefumi / Urushitani, Makoto

PloS one

2012 Volume 7, Issue 12, Page(s) e52776

Abstract: Accumulating evidence suggests that pathogenic TAR DNA-binding protein (TDP)-43 fragments contain a partial RNA-recognition motif domain 2 (RRM2) in amyotrophic lateral sclerosis (ALS)/frontotemporal lobar degeneration. However, the molecular basis for ... ...

Abstract	Accumulating evidence suggests that pathogenic TAR DNA-binding protein (TDP)-43 fragments contain a partial RNA-recognition motif domain 2 (RRM2) in amyotrophic lateral sclerosis (ALS)/frontotemporal lobar degeneration. However, the molecular basis for how this domain links to the conformation and function of TDP-43 is unclear. Previous crystal analyses have documented that the RRM2-DNA complex dimerizes under acidic and high salt conditions, mediated by the intermolecular hydrogen bonds of Glu246-Ile249 and Asp247-Asp247. The aims of this study were to investigate the roles of Glu246 and Asp247 in the molecular assembly of RRM2 under physiological conditions, and to evaluate their potential use as markers for TDP-43 misfolding due to the aberrantly exposed dimer interface. Unexpectedly, gel filtration analyses showed that, regardless of DNA interaction, the RRM2 domain remained as a stable monomer in phosphate-buffered saline. Studies using substitution mutants revealed that Glu246 and, especially, Asp247 played a crucial role in preserving the functional RRM2 monomers. Substitution to glycine at Glu246 or Asp247 induced the formation of fibrillar oligomers of RRM2 accompanied by the loss of DNA-binding affinity, which also affected the conformation and the RNA splicing function of full-length TDP-43. A novel monoclonal antibody against peptides containing Asp247 was found to react with TDP-43 inclusions of ALS patients and mislocalized cytosolic TDP-43 in cultured cells, but not with nuclear wild-type TDP-43. Our findings indicate that Glu246 and Asp247 play pivotal roles in the proper conformation and function of TDP-43. In particular, Asp247 should be studied as a molecular target with an aberrant conformation related to TDP-43 proteinopathy.
MeSH term(s)	Aged ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Antibodies, Monoclonal, Murine-Derived/chemistry ; Conserved Sequence ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/immunology ; DNA-Binding Proteins/metabolism ; HEK293 Cells ; Humans ; Hydrogen Bonding ; Inclusion Bodies/metabolism ; Mice ; Mice, Inbred C57BL ; Middle Aged ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nuclear Localization Signals ; Protein Binding ; Protein Folding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Transport ; RNA Splicing ; Solubility ; Spinal Cord/metabolism
Chemical Substances	Antibodies, Monoclonal, Murine-Derived ; DNA-Binding Proteins ; Nuclear Localization Signals
Language	English
Publishing date	2012-12-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0052776
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Transglutaminase 2 accelerates neuroinflammation in amyotrophic lateral sclerosis through interaction with misfolded superoxide dismutase 1.

Oono, Miki / Okado-Matsumoto, Ayako / Shodai, Akemi / Ido, Akemi / Ohta, Yasuyuki / Abe, Koji / Ayaki, Takashi / Ito, Hidefumi / Takahashi, Ryosuke / Taniguchi, Naoyuki / Urushitani, Makoto

Journal of neurochemistry

2014 Volume 128, Issue 3, Page(s) 403–418

Abstract: Although the aberrant assembly of mutant superoxide dismutase 1 (mSOD1) is implicated in the pathogenesis of familial amyotrophic lateral sclerosis (ALS), the molecular basis of superoxide dismutase 1 (SOD1) oligomerization remains undetermined. We ... ...

Abstract	Although the aberrant assembly of mutant superoxide dismutase 1 (mSOD1) is implicated in the pathogenesis of familial amyotrophic lateral sclerosis (ALS), the molecular basis of superoxide dismutase 1 (SOD1) oligomerization remains undetermined. We investigated the roles of transglutaminase 2 (TG2), an endogenous cross-linker in mSOD1-linked ALS. TG2 interacted preferentially with mSOD1 and promoted its oligomerization in transfected cells. Purified TG2 directly oligomerized recombinant mutant SOD1 and the apo-form of the wild-type SOD1 proteins in a calcium-dependent manner, indicating that misfolded SOD1 is a substrate of TG2. Moreover, the non-cell-autonomous effect of extracellular TG2 on the neuroinflammation was suggested, since the TG2-mediated soluble SOD1 oligomers induced tumor necrosis factor-α, interleukin-1β, and nitric oxide in microglial BV2 cells. TG2 was up-regulated in the spinal cord of pre-symptomatic G93A SOD1 transgenic mice and in the hypoglossal nuclei of mice suffering nerve ligation. Furthermore, inhibition of spinal TG2 by cystamine significantly delayed the progression and reduced SOD1 oligomers and microglial activation. These results indicate a novel role of TG2 in SOD1 oligomer-mediated neuroinflammation, as well as in the involvement in the intracellular aggregation of misfolded SOD1 in ALS.
MeSH term(s)	Amyotrophic Lateral Sclerosis/pathology ; Animals ; Blotting, Western ; COS Cells ; Cell Death/drug effects ; Cercopithecus aethiops ; DNA, Complementary/biosynthesis ; DNA, Complementary/genetics ; Electrophoresis, Polyacrylamide Gel ; GTP-Binding Proteins/toxicity ; HEK293 Cells ; Humans ; Hypoglossal Nerve/pathology ; Immunoprecipitation ; Inflammation/pathology ; Mice ; Mice, Transgenic ; Microscopy, Confocal ; Motor Neurons/drug effects ; Plasmids/genetics ; Protein Folding/drug effects ; Real-Time Polymerase Chain Reaction ; Spinal Cord/pathology ; Superoxide Dismutase/drug effects ; Superoxide Dismutase-1 ; Transglutaminases/toxicity
Chemical Substances	DNA, Complementary ; SOD1 protein, human ; Sod1 protein, mouse (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1) ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2014-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/jnc.12441
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ui II Zs.170: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Colocalization of 14-3-3 proteins with SOD1 in Lewy body-like hyaline inclusions in familial amyotrophic lateral sclerosis cases and the animal model.

Okamoto, Yoko / Shirakashi, Yoshitomo / Ihara, Masafumi / Urushitani, Makoto / Oono, Miki / Kawamoto, Yasuhiro / Yamashita, Hirofumi / Shimohama, Shun / Kato, Shinsuke / Hirano, Asao / Tomimoto, Hidekazu / Ito, Hidefumi / Takahashi, Ryosuke

PloS one

2011 Volume 6, Issue 5, Page(s) e20427

Abstract: Background and purpose: Cu/Zn superoxide dismutase (SOD1) is a major component of Lewy body-like hyaline inclusion (LBHI) found in the postmortem tissue of SOD1-linked familial amyotrophic lateral sclerosis (FALS) patients. In our recent studies, 14-3-3 ...

Abstract	Background and purpose: Cu/Zn superoxide dismutase (SOD1) is a major component of Lewy body-like hyaline inclusion (LBHI) found in the postmortem tissue of SOD1-linked familial amyotrophic lateral sclerosis (FALS) patients. In our recent studies, 14-3-3 proteins have been found in the ubiquitinated inclusions inside the anterior horn cells of spinal cords with sporadic amyotrophic lateral sclerosis (ALS). To further investigate the role of 14-3-3 proteins in ALS, we performed immunohistochemical analysis of 14-3-3 proteins and compared their distributions with those of SOD1 in FALS patients and SOD1-overexpressing mice. Methods: We examined the postmortem brains and the spinal cords of three FALS cases (A4V SOD1 mutant). Transgenic mice expressing the G93A mutant human SOD1 (mutant SOD1-Tg mice), transgenic mice expressing the wild-type human SOD1 (wild-type SOD1-Tg mice), and non-Tg wild-type mice were also subjected to the immunohistochemical analysis. Results: In all the FALS patients, LBHIs were observed in the cytoplasm of the anterior horn cells, and these inclusions were immunopositive intensely for pan 14-3-3, 14-3-3β, and 14-3-3γ. In the mutant SOD1-Tg mice, a high degree of immunoreactivity for misfolded SOD1 (C4F6) was observed in the cytoplasm, with an even greater degree of immunoreactivity present in the cytoplasmic aggregates of the anterior horn cells in the lumbar spinal cord. Furthermore, we have found increased 14-3-3β and 14-3-3γ immunoreactivities in the mutant SOD1-Tg mice. Double immunofluorescent staining showed that C4F6 and 14-3-3 proteins were partially co-localized in the spinal cord with FALS and the mutant SOD1-Tg mice. In comparison, the wild-type SOD1-Tg and non-Tg wild-type mice showed no or faint immunoreactivity for C4F6 and 14-3-3 proteins (pan 14-3-3, 14-3-3β, and 14-3-3γ) in any neuronal compartments. Discussion: These results suggest that 14-3-3 proteins may be associated with the formation of SOD1-containing inclusions, in FALS patients and the mutant SOD1-Tg mice.
MeSH term(s)	14-3-3 Proteins/genetics ; 14-3-3 Proteins/metabolism ; Aged ; Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Humans ; Hyalin/metabolism ; Immunohistochemistry ; In Vitro Techniques ; Inclusion Bodies/metabolism ; Lewy Bodies/metabolism ; Male ; Mice ; Mice, Transgenic ; Middle Aged ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism ; Superoxide Dismutase-1
Chemical Substances	14-3-3 Proteins ; SOD1 protein, human ; Sod1 protein, mouse (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2011-05-31
Publishing country	United States
Document type	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0020427
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Induction of protective immunity by vaccination with wild-type apo superoxide dismutase 1 in mutant SOD1 transgenic mice.

Takeuchi, Shigeko / Fujiwara, Noriko / Ido, Akemi / Oono, Miki / Takeuchi, Yuki / Tateno, Minako / Suzuki, Keiichiro / Takahashi, Ryosuke / Tooyama, Ikuo / Taniguchi, Naoyuki / Julien, Jean-Pierre / Urushitani, Makoto

Journal of neuropathology and experimental neurology

2010 Volume 69, Issue 10, Page(s) 1044–1056

Abstract: Vaccinations targeting extracellular superoxide dismutase 1 (SOD1) mutants are beneficial in mouse models of amyotrophic lateral sclerosis (ALS). Because of its misfolded nature, wild-type nonmetallated SOD1 protein (WT-apo) may have therapeutic ... ...

Abstract	Vaccinations targeting extracellular superoxide dismutase 1 (SOD1) mutants are beneficial in mouse models of amyotrophic lateral sclerosis (ALS). Because of its misfolded nature, wild-type nonmetallated SOD1 protein (WT-apo) may have therapeutic application for vaccination of various SOD1 mutants. We compared the effects of WT-apo to those of a G93A SOD1 vaccine in low-copy G93A SOD1 transgenic mice. Both SOD1 vaccines induced antibody against G93A SOD1 and significantly delayed disease onset compared with saline/adjuvant controls. WT-apo SOD1 significantly extended the life span of vaccinated mice. The vaccines potentiated TH2 deviation in the spinal cord as determined by the ratio of interleukin-4 to interferon-γ (IFNγ) or tumor necrosis factor and induced C1q deposition around motor neurons. Transgenic mice had abundant microglial expression of signal transducers and activators of transcription 4, an activator of transcription of IFNγ, in the spinal cord implicating IFNγ in the pathogenesis. On the other hand, the sera from G93A SOD1-vaccinated mice showed higher IFNγ or tumor necrosis factor and yielded a lower IgG1/IgG2c ratio than the sera from WT-apo-vaccinated mice. These results indicate that the TH1/TH2 milieu is affected by specific vaccinations and that antigenicity might counteract beneficial effects by enhancing TH1 immunity. Thus, because of its lower TH1 induction, WT-apo may be a therapeutic option and have broader application in ALS associated with diverse SOD1 mutations.
MeSH term(s)	Amyotrophic Lateral Sclerosis/immunology ; Amyotrophic Lateral Sclerosis/pathology ; Amyotrophic Lateral Sclerosis/therapy ; Analysis of Variance ; Animals ; Chromatography, Gel/methods ; Complement C1q/metabolism ; Disease Models, Animal ; Enzyme-Linked Immunosorbent Assay/methods ; Gene Expression Regulation/immunology ; Humans ; Immunity/genetics ; Immunity/physiology ; Immunoglobulin G ; Interferon-gamma/metabolism ; Interleukin-4/metabolism ; Mice ; Mice, Transgenic ; Motor Neurons/metabolism ; Mutation ; Signal Transduction/genetics ; Spinal Cord/immunology ; Spinal Cord/metabolism ; Spinal Cord/pathology ; Spleen/metabolism ; Superoxide Dismutase/genetics ; Superoxide Dismutase/immunology ; Superoxide Dismutase-1 ; Th1 Cells/immunology ; Th1 Cells/metabolism ; Th2 Cells/immunology ; Th2 Cells/metabolism ; Vaccination/methods
Chemical Substances	Immunoglobulin G ; SOD1 protein, human ; Interleukin-4 (207137-56-2) ; Complement C1q (80295-33-6) ; Interferon-gamma (82115-62-6) ; SOD1 G93A protein (EC 1.15.1.1) ; Sod1 protein, mouse (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2010-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3088-0
ISSN	1554-6578 ; 0022-3069
ISSN (online)	1554-6578
ISSN	0022-3069
DOI	10.1097/NEN.0b013e3181f4a90a
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ui II Zs.134: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Ui II Zs.194: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito