Spreer, Annette

[["dc.bibliographiccitation.firstpage","739"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Neural Transmission"],["dc.bibliographiccitation.lastpage","746"],["dc.bibliographiccitation.volume","119"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Trautmann, Ellen"],["dc.contributor.author","Otte, Birgit"],["dc.contributor.author","Ng, Juliana"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Sixel-Doering, Friederike"],["dc.contributor.author","Hakimi, Mansoureh"],["dc.contributor.author","VonSattel, Jean-Paul"],["dc.contributor.author","Nussbaum, Robert"],["dc.contributor.author","Trenkwalder, Claudia"],["dc.contributor.author","Schlossmacher, Michael G."],["dc.date.accessioned","2018-11-07T09:08:50Z"],["dc.date.available","2018-11-07T09:08:50Z"],["dc.date.issued","2012"],["dc.description.abstract","The source of Parkinson disease-linked alpha-synuclein (aSyn) in human cerebrospinal fluid (CSF) remains unknown. We decided to measure the concentration of aSyn and its gradient in human CSF specimens and compared it with serum to explore its origin. We correlated aSyn concentrations in CSF versus serum (Q(aSyn)) to the albumin quotient (Q(albumin)) to evaluate its relation to blood-CSF barrier function. We also compared aSyn with several other CSF constituents of either central or peripheral sources (or both) including albumin, neuron-specific enolase, beta-trace protein and total protein content. Finally, we examined whether aSyn is present within the structures of the choroid plexus (CP). We observed that Q(aSyn) did not rise or fall with Q(albumin) values, a relative measure of blood-CSF barrier integrity. In our CSF gradient analyses, aSyn levels decreased slightly from rostral to caudal fractions, in parallel to the recorded changes for neuron-specific enolase; the opposite trend was recorded for total protein, albumin and beta-trace protein. The latter showed higher concentrations in caudal CSF fractions due to the diffusion-mediated transfer of proteins from blood and leptomeninges into CSF in the lower regions of the spine. In postmortem sections of human brain, we detected highly variable aSyn reactivity within the epithelial cell layer of CP in patients diagnosed with a range of neurological diseases; however, in sections of mice that express only human SNCA alleles (and in those without any Snca gene expression), we detected no aSyn signal in the epithelial cells of the CP. We conclude from these complementary results that despite its higher levels in peripheral blood products, neurons of the brain and spinal cord represent the principal source of aSyn in human CSF."],["dc.identifier.doi","10.1007/s00702-012-0784-0"],["dc.identifier.isi","000305525800002"],["dc.identifier.pmid","22426833"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26122"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","0300-9564"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","alpha-Synuclein in human cerebrospinal fluid is principally derived from neurons of the central nervous system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","126"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Dementia and Geriatric Cognitive Disorders"],["dc.bibliographiccitation.lastpage","134"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Fronek, Kathrin"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Eiffert, Helmut"],["dc.contributor.author","Nau, Roland"],["dc.contributor.author","Lange, Peter"],["dc.date.accessioned","2018-11-07T08:51:09Z"],["dc.date.available","2018-11-07T08:51:09Z"],["dc.date.issued","2011"],["dc.description.abstract","Background/Aims: Determination of marker proteins of neuronal degeneration in cerebrospinal fluid (CSF) is of increasing importance. However, preanalytical problems may compromise the results. Methods: We studied the influence of the transport tube material and shaking at room temperature on the CSF concentrations of beta-amyloid and tau protein determined by enzyme immunoassays. Results: The materials of the transport tube moderately influenced the CSF concentrations of beta-amyloid and tau protein. Polyethylene and polypropylene tubes were well suited, but glass, polycarbonate and polystyrene tubes caused a decrease in the CSF beta-amyloid and tau protein concentrations. The strongest impact, however, was caused by bacterial contamination of samples. Contamination with high concentrations of Pseudomonas aeruginosa and related species rendered beta-amyloid undetectable and strongly diminished tau protein concentrations. The effects of several Gram-positive bacteria were less pronounced. Addition of 0.1% sodium azide prior to bacterial contamination increased the interval at which CSF could be kept at room temperature without a substantial reduction of the beta-amyloid or tau protein concentration. Conclusion: Polyethylene or polypropylene tubes are suitable transport vessels for CSF samples. Bacterial contamination during sampling and portioning must be avoided. Addition of sodium azide may be an option when transport of the sample is delayed. Copyright (C) 2011 S. Karger AG, Basel"],["dc.identifier.doi","10.1159/000330912"],["dc.identifier.fs","580959"],["dc.identifier.isi","000295875400006"],["dc.identifier.pmid","21952521"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21862"],["dc.language.iso","en"],["dc.notes","This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively."],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","In goescholar merged with http://resolver.sub.uni-goettingen.de/purl?gs-1/8159"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","S. Karger AG"],["dc.relation.eissn","1421-9824"],["dc.relation.issn","1420-8008"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.mesh","Amyloid beta-Peptides"],["dc.subject.mesh","Cerebrospinal Fluid"],["dc.subject.mesh","Cerebrospinal Fluid Proteins"],["dc.subject.mesh","Dementia"],["dc.subject.mesh","Enzyme-Linked Immunosorbent Assay"],["dc.subject.mesh","Equipment Design"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Pseudomonas aeruginosa"],["dc.subject.mesh","Quality Control"],["dc.subject.mesh","Specimen Handling"],["dc.subject.mesh","Stenotrophomonas maltophilia"],["dc.subject.mesh","tau Proteins"],["dc.title","Bacterial Contamination and the Transport Vial Material Affect Cerebrospinal Fluid Concentrations of beta-Amyloid and Tau Protein as Determined by Enzyme Immunoassay"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","865"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Infection and Immunity"],["dc.bibliographiccitation.lastpage","871"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Ribes, Sandra"],["dc.contributor.author","Ebert, Sandra"],["dc.contributor.author","Regen, Tommy"],["dc.contributor.author","Agarwal, Amit"],["dc.contributor.author","Tauber, Simone C."],["dc.contributor.author","Czesnik, Dirk"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Bunkowski, Stephanie"],["dc.contributor.author","Eiffert, Helmut"],["dc.contributor.author","Hanisch, Uwe-Karsten"],["dc.contributor.author","Hammerschmidt, Sven"],["dc.contributor.author","Nau, Roland"],["dc.date.accessioned","2018-11-07T08:46:16Z"],["dc.date.available","2018-11-07T08:46:16Z"],["dc.date.issued","2010"],["dc.description.abstract","Toll-like receptors (TLRs) are crucial pattern recognition receptors in innate immunity that are expressed in microglia, the resident macrophages of the brain. TLR2, -4, and -9 are important in the responses against Streptococcus pneumoniae, the most common agent causing bacterial meningitis beyond the neonatal period. Murine microglial cultures were stimulated with agonists for TLR1/2 (Pam3CSK4), TLR4 (lipopolysaccharide), and TLR9 (CpG oligodeoxynucleotide) for 24 h and then exposed to either the encapsulated D39 (serotype 2) or the nonencapsulated R6 strain of S. pneumoniae. After stimulation, the levels of interleukin-6 and CCL5 (RANTES [regulated upon activation normal T-cell expressed and secreted]) were increased, confirming microglial activation. The TLR1/2, -4, and -9 agonist-stimulated microglia ingested significantly more bacteria than unstimulated cells (P < 0.05). The presence of cytochalasin D, an inhibitor of actin polymerizaton, blocked >90% of phagocytosis. Along with an increased phagocytic activity, the intracellular bacterial killing was also increased in TLR-stimulated cells compared to unstimulated cells. Together, our data suggest that microglial stimulation by these TLRs may increase the resistance of the brain against pneumococcal infections."],["dc.identifier.doi","10.1128/IAI.01110-09"],["dc.identifier.isi","000273855600033"],["dc.identifier.pmid","19933834"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20648"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0019-9567"],["dc.title","Toll-Like Receptor Stimulation Enhances Phagocytosis and Intracellular Killing of Nonencapsulated and Encapsulated Streptococcus pneumoniae by Murine Microglia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","630"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Neurology"],["dc.bibliographiccitation.lastpage","636"],["dc.bibliographiccitation.volume","259"],["dc.contributor.author","Djukic, Marija"],["dc.contributor.author","Schmidt-Samoa, Carsten"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Neubieser, Katja"],["dc.contributor.author","Eiffert, Helmut"],["dc.contributor.author","Nau, Roland"],["dc.contributor.author","Schmidt, Holger"],["dc.date.accessioned","2018-11-07T09:11:41Z"],["dc.date.available","2018-11-07T09:11:41Z"],["dc.date.issued","2012"],["dc.description.abstract","Presence of BB-specific antibodies in the cerebrospinal fluid (CSF) with evidence of their intrathecal production in conjunction with the white cell count in the CSF and typical clinical symptoms is the traditional diagnostic gold standard of Lyme neuroborreliosis (LNB). Few data are available on the CSF lactate concentration in European adults with the diagnosis of acute LNB. The objective of the study was to investigate the CSF changes during acute LNB. Routine CSF parameters [leukocyte count, protein, lactate and albumin concentrations, CSF/serum quotients of albumin (Q(Alb)), IgG, IgA and IgM, and oligoclonal IgG bands] and the Borrelia burgdorferi (BB)-specific antibody index were retrospectively studied in relation to the clinical presentation in patients diagnosed with acute LNB. A total of 118 patients with LNB were categorized into the following groups according to their symptoms at presentation; group 1: polyradiculoneuritis (Bannwarth's syndrome), group 2: isolated facial palsy and group 3: predominantly meningitic course of the disease. In addition to the CSF of patients with acute LNB, CSF of 19 patients with viral meningitis (VM) and 3 with neurolues (NL) were analyzed. There were 97 patients classified with definite LNB, and 21 as probable LNB. Neck stiffness and fever were reported by 15.3% of patients. Most of these patients were younger than 50 years. Polyradiculoneuritis was frequently found in patients older than 50 years. Lymphopleocytosis was found in all patients. Only 5 patients had a CSF lactate >= 3.5 mmol/l, and the mean CSF lactate level was not elevated (2.1 +/- A 0.6 mmol/l). The patients with definite LNB had significantly higher lactate levels than patients with probable LNB. Elevated lactate levels were accompanied by fever and headache. In the Reiber nomograms, intrathecal immunoglobulin synthesis was found for IgM in 70.2% followed by IgG in 19.5%. Isoelectric focussing detected an intrathecal IgG synthesis in 83 patients (70.3%). Elevated BB AIs in the CSF were found in 97 patients (82.2%). Patients with VM showed lower CSF protein concentration and CSF/serum quotients of albumin than LNB patients. In acute LNB, all patients had elevated cerebrospinal fluid (CSF) leukocyte counts. In contrast to infections by other bacteria, CSF lactate was lower than 3.5 mmol/l in all but 5 patients. The CSF findings did not differ between polyradiculoneuritis, facial palsy, and meningitis. The CSF in LNB patients strongly differed from CSF in VM patients with respect to protein concentration and the CSF/serum albumin quotient."],["dc.identifier.doi","10.1007/s00415-011-6221-8"],["dc.identifier.isi","000302489400004"],["dc.identifier.pmid","21898139"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8098"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26777"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Heidelberg"],["dc.relation.issn","0340-5354"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Cerebrospinal fluid findings in adults with acute Lyme neuroborreliosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","15"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Fluids and Barriers of the CNS"],["dc.bibliographiccitation.lastpage","5"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Djukic, Marija"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Bunkowski, Stephanie"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Nau, Roland"],["dc.date.accessioned","2017-09-07T11:44:33Z"],["dc.date.available","2017-09-07T11:44:33Z"],["dc.date.issued","2016"],["dc.description.abstract","Background The composition of the cerebrospinal fluid (CSF) is not homogeneous, and concentrations of proteins from different origins diverge among ventricular, cisternal and lumbar CSF fractions. Concentrations of blood-derived proteins increase and of brain-derived proteins decrease from ventricular to lumbar fractions. We studied whether the origin of the CSF portion analysed may affect results in CSF analysis for dementia. Methods In 16 geriatric patients with suspected normal pressure hydrocephalus [age 82.5 (76/87) years; median (25th/75th percentile)] a lumbar spinal tap of 40 ml was performed. The CSF was sequentially collected in 8 fractions of 5 ml with the 1st fraction corresponding to lumbar CSF, the 8th to cisterna magna-near CSF. Fractions were analysed for total protein, albumin, Tau protein (Tau), phosphorylated Tau (pTau), Amyloid beta 1–42 (Aβ1–42), Amyloid beta 1–40 (Aβ1–40), and the Aβ1–42/Aβ1–40 ratio. Results The concentrations of total protein and albumin increased from cisternal to lumbar fractions due to diffusion-related accumulation from blood to CSF with significantly higher concentrations in fraction 1 compared to fraction 8. The concentrations of Tau showed a non-significant trend towards decreased values in lumbar samples, and pTau was slightly, but significantly decreased in the lumbar fraction 1 [26.5 (22.5/35.0) pg/ml] compared to the cistern-near fraction 8 [27.0 (24.2/36.3) pg/ml] (p = 0.02, Wilcoxon signed rank test). Aβ1-42, Aβ1-40, and the Aβ1-42/Aβ1-40 ratio remained almost constant. Conclusions According to the flow-related diverging dynamics of blood-derived and brain-derived proteins in CSF, the concentrations of Tau and pTau tended to be lower in lumbar compared to cisternal CSF fractions after a spinal tap of 40 ml. The differences reached statistical significance for pTau only. The small differences will not affect clinical interpretation of markers of dementia in the vast majority of cases."],["dc.identifier.doi","10.1186/s12987-016-0039-9"],["dc.identifier.gro","3151687"],["dc.identifier.pmid","27581842"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13876"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8505"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","2045-8118"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Small cisterno-lumbar gradient of phosphorylated Tau protein in geriatric patients with suspected normal pressure hydrocephalus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","327"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Chemotherapy"],["dc.bibliographiccitation.lastpage","331"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","von Rueden, Christian"],["dc.contributor.author","Mitchell, Timothy J."],["dc.contributor.author","Eiffert, Helmut"],["dc.contributor.author","Nau, Roland"],["dc.date.accessioned","2018-11-07T11:06:16Z"],["dc.date.available","2018-11-07T11:06:16Z"],["dc.date.issued","2007"],["dc.description.abstract","Objective: Pneumolysin is an important virulence factor of Streptococcus pneumoniae with cytotoxic and proinflammatory activities released during growth and autolysis. At concentrations above the minimal inhibitory concentration, the protein-synthesis-inhibiting antibiotics erythromycin, clindamycin and rifampicin inhibit the production and/or release of virulence factors in various bacterial species. We investigated the influence of subinhibitory concentrations of these antibiotics on production and release of pneumolysin by S. pneumoniae strain D39. Methods: The pneumococcal strain D39 was grown in broth and treated with antibiotics at a concentration of 1/32 of the respective minimal inhibitory concentration. Cytoplasmic and extracellular pneumolysin was measured by quantitative immunoblotting with recombinant pneumolysin as standard. Results: The subinhibitory antibiotic concentrations evaluated did not affect bacterial growth. During logarithmic growth, production of pneumolysin was decreased by clindamycin, erythromycin and rifampicin by approximately 50% compared with untreated controls. The release of pneumolysin was decreased to a similar extent. Conclusion: A decrease in pneumolysin production by 50% probably has a moderate biological effect. We do not advocate the use of subinhibitory concentrations of antibiotics to modulate the expression of virulence factors during pneumococcal disease, particularly with regard to the risk of development of antibiotic resistance. Copyright (C) 2007 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000107691"],["dc.identifier.isi","000249306100005"],["dc.identifier.pmid","17728540"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52264"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","0009-3157"],["dc.title","Influence of subinhibitory concentrations of protein-synthesis-inhibiting antibiotics on production and release of the pneumococcal virulence factor pneumolysin in vitro"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","723"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Medical Mycology"],["dc.bibliographiccitation.lastpage","731"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Ruechel, Reinhard"],["dc.contributor.author","Reichard, Utz"],["dc.date.accessioned","2018-11-07T08:54:56Z"],["dc.date.available","2018-11-07T08:54:56Z"],["dc.date.issued","2006"],["dc.description.abstract","An endoprotease Arp (alkaline Rhizopus protease) was identified and purified to virtual homogeneity from the culture supernatant of an isolate of Rhizopus microsporus var. rhizopodiformis recovered from a non-fatal case of rhinoorbital mucormycosis. N-terminal sequencing of the mature native enzyme was obtained for the first 20 amino acids and revealed high homology to serine proteases of the subtilisin subfamily. Arp migrated in SDS-PAGE with an estimated molecular mass of 33 kDa and had a pI determined to be at pH 8.8. Arp is proteolytically active against various substrates, including elastin, over a broad pH range between 6 and 12 with an optimum at pH 10.5. After invasive mucormycosis, specific antibodies against Arp were detected in stored serum samples taken from the patient from whom the R. microsporus strain of this study had been isolated. Furthermore, in search of factors involved in thrombosis as a typical complication of mucormycosis, a procoagulatory effect of the enzyme has recently been shown. Altogether, these data substantiate the expression of Arp during human rhinoorbital mucormycosis and suggest a role of the enzyme in pathogenesis."],["dc.identifier.doi","10.1080/13693780600936399"],["dc.identifier.isi","000244151400005"],["dc.identifier.pmid","17127629"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22790"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Ltd"],["dc.relation.issn","1369-3786"],["dc.title","Characterization of an extracellular subtilisin protease of Rhizopus microsporus and evidence for its expression during invasive rhinoorbital mycosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","210"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Pediatric Research"],["dc.bibliographiccitation.lastpage","215"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Gerber, Joachim"],["dc.contributor.author","Hanssen, Mareike"],["dc.contributor.author","Schindler, Stefanie"],["dc.contributor.author","Hermann, Corinna"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Eiffert, Helmut"],["dc.contributor.author","Nau, Roland"],["dc.date.accessioned","2018-11-07T09:30:34Z"],["dc.date.available","2018-11-07T09:30:34Z"],["dc.date.issued","2006"],["dc.description.abstract","Mortality and long-term sequelae rates are high among adults and children with acute bacterial meningitis. Adjunctive treatment with dexamethasone has been shown to reduce systemic complications in bacteria] meningitis patients, but corticosteroid treatment may have detrimental effects on hippocampal function. We evaluated the effect of dexamethasone treatment in addition to antibiotic therapy in a rabbit model of Escherichia coli meningitis. A moderate anti-inflammatory effect of dexamethasone could be demonstrated with respect to the inflammatory mediator prostaglandin E2, whereas no significant effect of dexamethasone on tumor necrosis factor-alpha, cerebrospinal fluid pleocytosis, protein, lactate, indicators of global neuronal damage, or blood gas analysis was found. Dexamethasone, however, increased the rate of apoptotic neurons in the granular layer of the hippocampal dentate gyrus. In view of the proapoptotic effect of adjunctive dexamethasone on hippocampal neuronal cells in animal models of Gram-positive and Gram-negative meningitis, the application of dexamethasone should be considered carefully in those forms of bacterial meningitis for which no evidence-based data of beneficial effect in humans are available, such as neonatal meningitis, bacillary Gram-negative meningitis or nosocomial forms of meningitis (e.g. following neurosurgery)."],["dc.identifier.doi","10.1203/01.pdr.0000227553.47378.9f"],["dc.identifier.isi","000239195300019"],["dc.identifier.pmid","16864706"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31335"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Int Pediatric Research Foundation, Inc"],["dc.relation.issn","0031-3998"],["dc.title","Dexamethasone increases hippocampal neuronal apoptosis in a rabbit model of Escherichia coli meningitis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3342"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Clinical Microbiology"],["dc.bibliographiccitation.lastpage","3345"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Lis, A."],["dc.contributor.author","Gerber, Joachim"],["dc.contributor.author","Reinert, R. R."],["dc.contributor.author","Eiffert, Helmut"],["dc.contributor.author","Nau, R."],["dc.date.accessioned","2018-11-07T10:47:43Z"],["dc.date.available","2018-11-07T10:47:43Z"],["dc.date.issued","2004"],["dc.description.abstract","Production and release of the pneumococcal virulence factors pneumolysin and lipoteichoic and teichoic acid in 75 clinical isolates were investigated. No difference was found between strains causing systemic infection or localized respiratory infection and isolates from asymptomatic carriers. This suggests that the presence of pneumolysin and lipoteichoic and teichoic acid is a necessary but not a sufficient condition for pneumococcal infection and development of invasive disease."],["dc.identifier.doi","10.1128/JCM.42.7.3342-3345.2004"],["dc.identifier.isi","000222672100081"],["dc.identifier.pmid","15243112"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48029"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0095-1137"],["dc.title","Differences in clinical manifestation of Streptococcus pneumoniae infection are not correlated with in vitro production and release of the virulence factors pneumolysin and lipoteichoic and teichoic acids"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","109"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Fortschritte der Neurologie · Psychiatrie"],["dc.bibliographiccitation.lastpage","122"],["dc.bibliographiccitation.volume","83"],["dc.contributor.author","Spreer, Annette"],["dc.contributor.author","Nau, R."],["dc.date.accessioned","2018-11-07T10:01:17Z"],["dc.date.available","2018-11-07T10:01:17Z"],["dc.date.issued","2015"],["dc.description.abstract","Cerebrospinal fluid analysis is of prime importance to establish an early diagnosis of central nervous system infections. Beside the basic diagnostics containing CSF white cell count, lactate concentration and protein analysis, the targeted search for agents of bacterial, viral or fungal CNS infectious diseases is essential. Decisive methods are bacterial and fungal staining techniques, microbiological culture methods, nucleic acid amplification and antigen detection methods or indirect identification of pathogens by serologic testings including the determination of pathogen-specific intrathecal immunoglobulin synthesis. Besides imparting basic principles of cerebrospinal fluid analysis, this article focuses on special aspects of detection of infectious agents. Well-directed questions and a close communication between clinician and laboratory allow optimal diagnostic analysis for successful confirmation of the diagnosis and for optimal treatment of the patient."],["dc.identifier.doi","10.1055/s-0034-1398932"],["dc.identifier.isi","000350566700017"],["dc.identifier.pmid","25723775"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37983"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Georg Thieme Verlag Kg"],["dc.relation.issn","1439-3522"],["dc.relation.issn","0720-4299"],["dc.title","Cerebrospinal Fluid Diagnostics for Neuroinfectious Diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]