Smirnov, Alexander V.

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Clinica Chimica Acta"],["dc.bibliographiccitation.lastpage","12"],["dc.bibliographiccitation.volume","292"],["dc.contributor.author","Smirnov, Alexander V."],["dc.contributor.author","Tumani, Hayrettin"],["dc.contributor.author","Henne, Sergej"],["dc.contributor.author","Barchfeld, Sandra"],["dc.contributor.author","Olgemöller, Ulrike"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Mäder, Michael"],["dc.contributor.author","Nau, Roland"],["dc.date.accessioned","2017-09-07T11:45:22Z"],["dc.date.available","2017-09-07T11:45:22Z"],["dc.date.issued","2000"],["dc.description.abstract","Glutamine synthetase (GS) activity is higher in the neocortex but not in the hippocampal formation of rabbit brain during Streptococcus pneumoniae meningitis compared to the respective brain region of uninfected control animals. One-dimensional polyacrylamide gel electrophoresis (1D-SDS-PAGE) revealed an apparent molecular mass (Mr) of 44 000 Dalton (Da) for GS from rabbit brain. After two-dimensional gel electrophoresis (2D-PAGE), followed by Coomassie-blue staining, GS separated into three distinct spots (S1, S2, S3). One additional spot (S4) occurred on the immunoblot. All four GS spots exhibited the same Mr (44 000 Da), but differed in their isoelectric points. Densitometric evaluation of the two-dimensional maps revealed a strong increase of optical density (OD) of S3 in the frontal cortex of infected animals. The calculated OD ratio S3/S2 in the frontal cortex from rabbits with meningitis was 1.75±0.68 (mean±standard deviation). Compared to controls (0.85±0.39), this value was significantly increased (p=0.0006). In the hippocampal formation, the ratio S3/S2 was nearly unchanged during meningitis. It is suggested that the ratio S3/S2 may indicate a neuroprotective feature of rabbit brain during meningitis since neuronal apoptosis occurs only in the dentate gyrus and not in the frontal cortex."],["dc.identifier.doi","10.1016/s0009-8981(99)00180-1"],["dc.identifier.gro","3151752"],["dc.identifier.pmid","10686272"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8576"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0009-8981"],["dc.title","Glutamine synthetase in experimental meningitis: increased ratio of the subunits 3 and 2 may indicate enhanced activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","481"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","496"],["dc.bibliographiccitation.volume","81"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Esselmann, Hermann"],["dc.contributor.author","Bibl, M."],["dc.contributor.author","Smirnov, A."],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Paul, S."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Klafki, Hans-Wolfgang"],["dc.contributor.author","Maler, Manuel"],["dc.contributor.author","Dyrks, T."],["dc.contributor.author","Bienert, M."],["dc.contributor.author","Beyermann, Michael"],["dc.contributor.author","Rüther, Eckart"],["dc.contributor.author","Kornhuber, Johannes"],["dc.date.accessioned","2017-09-07T11:44:26Z"],["dc.date.available","2017-09-07T11:44:26Z"],["dc.date.issued","2003"],["dc.description.abstract","Human lumbar CSF patterns of Aβ peptides were analysed by urea-based β-amyloid sodium dodecyl sulphate polyacrylamide gel electrophoresis with western immunoblot (Aβ-SDS–PAGE/immunoblot). A highly conserved pattern of carboxyterminally truncated Aβ1–37/38/39 was found in addition to Aβ1–40 and Aβ1–42. Remarkably, Aβ1–38 was present at a higher concentration than Aβ1–42, being the second prominent Aβ peptide species in CSF. Patients with Alzheimer's disease (AD, n = 12) and patients with chronic inflammatory CNS disease (CID, n = 10) were differentiated by unique CSF Aβ peptide patterns from patients with other neuropsychiatric diseases (OND, n = 37). This became evident only when we investigated the amount of Aβ peptides relative to their total Aβ peptide concentration (Aβ1–x%, fractional Aβ peptide pattern), which may reflect disease-specific γ-secretase activities. Remarkably, patients with AD and CID shared elevated Aβ1–38% values, whereas otherwise the patterns were distinct, allowing separation of AD from CID or OND patients without overlap. The presence of one or two ApoE ε4 alleles resulted in an overall reduction of CSF Aβ peptides, which was pronounced for Aβ1–42. The severity of dementia was significantly correlated to the fractional Aβ peptide pattern but not to the absolute Aβ peptide concentrations."],["dc.identifier.doi","10.1046/j.1471-4159.2002.00818.x"],["dc.identifier.gro","3151651"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8468"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","chake"],["dc.relation.issn","0022-3042"],["dc.title","Highly conserved and disease-specific patterns of carboxyterminally truncated Aβ peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2095"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Infectious Diseases"],["dc.bibliographiccitation.lastpage","2098"],["dc.bibliographiccitation.volume","181"],["dc.contributor.author","Bottcher, T."],["dc.contributor.author","Gerber, Joachim"],["dc.contributor.author","Wellmer, A."],["dc.contributor.author","Smirnov, A. V."],["dc.contributor.author","Fakhrjanali, F."],["dc.contributor.author","Mix, E."],["dc.contributor.author","Pilz, J."],["dc.contributor.author","Zettl, Uwe K."],["dc.contributor.author","Nau, R."],["dc.date.accessioned","2018-11-07T10:48:14Z"],["dc.date.available","2018-11-07T10:48:14Z"],["dc.date.issued","2000"],["dc.description.abstract","Bacterial compounds induce the production of reactive oxygen species (ROS) in meningitis. Rifampin releases smaller quantities of proinflammatory compounds from Streptococcus pneumoniae than do beta-lactam antibiotics. Therefore, rabbits infected intracisternally with S. pneumoniae were treated intravenously either with rifampin 5 mg/kg/h or ceftriaxone 10 mg/kg/h (n = 9 each). Before initiation of antibiotic treatment, a strong positive correlation between ROS production of cerebrospinal fluid (CSF) phagocyte populations and bacterial CSF titers was observed (granulocytes: r(s) = .90, P < .0001; monocytes: r(s) = .81, P < .0001). CSF leukocytes from rifampin-treated rabbits produced less ROS (monocytes at 2 h after initiation of treatment: P = .045; at 5 h: P = .014; granulocytes at 5 h: P = .036) than did leukocytes from animals receiving ceftriaxone. The CSF malondialdehyde concentrations and the density of apoptotic neurons in the dentate gyrus were lower in rifampin- than in ceftriaxone-treated animals (P = .002 and .005). The use of rifampin to reduce the release of ROS and to decrease secondary brain injury appears promising."],["dc.identifier.doi","10.1086/315518"],["dc.identifier.isi","000087923900038"],["dc.identifier.pmid","10837202"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48141"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Univ Chicago Press"],["dc.relation.issn","0022-1899"],["dc.title","Rifampin reduces production of reactive oxygen species of cerebrospinal fluid phagocytes and hippocampal neuronal apoptosis in experimental Streptococcus pneumoniae meningitis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3336"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","ELECTROPHORESIS"],["dc.bibliographiccitation.lastpage","3343"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Lewczuk, Piotr"],["dc.contributor.author","Esselmann, Hermann"],["dc.contributor.author","Bibl, Mirko"],["dc.contributor.author","Paul, Sabine"],["dc.contributor.author","Svitek, Jana"],["dc.contributor.author","Miertschischk, Johannes"],["dc.contributor.author","Meyrer, Robert"],["dc.contributor.author","Smirnov, Alexandr"],["dc.contributor.author","Maler, Juan Manuel"],["dc.contributor.author","Klein, Christian"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Bleich, Stefan"],["dc.contributor.author","Sperling, Wolfgang"],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Rüther, Eckhard"],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2017-09-07T11:44:31Z"],["dc.date.available","2017-09-07T11:44:31Z"],["dc.date.issued","2004"],["dc.description.abstract","In this prospective study, for the first time we have separated and quantified amyloid β (Aβ) peptides in the plasma of patients with Alzheimer's disease (AD, n = 8) and age- and environment-matched healthy controls (n = 9) with urea-based Aβ-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)/immunoblot. In addition to the Aβ peptides 1–37/38/39/40/42, which we recently identified as regular constituents of human cerebrospinal fluid (CSF), we have observed a novel electrophoretic band migrating slightly cathodically to Aβ1–42. Since a standard peptide with the amino acid sequence Aβ2–40 migrates in the same position, we hypothesize that this plasma-specific band may correspond to Aβ2–40. The concentration of Aβ peptides in the plasma has been approximately 100-fold lower compared to the CSF. Interestingly, the concentration of the two shortest peptides and the longest one of these considered here (i.e., Aβ1–37/38/42) have increased significantly when the samples have been frozen at –80°C before immunoprecipitation, while the ‘middle-length' peptides (i.e., Aβ1–39/40) have not been affected by this procedure. We have not observed significant differences of the Aβ peptides concentrations between AD and control subjects. Our method can be used to investigate the significance of plasma Aβ peptides in neurodegenerative disorders, and to monitor the efficiency of drugs with β/γ-secretase inhibitory potency."],["dc.identifier.doi","10.1002/elps.200406068"],["dc.identifier.gro","3151677"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8495"],["dc.language.iso","en"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","0173-0835"],["dc.title","Electrophoretic separation of amyloid β peptides in plasma"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]