Smirnov, Alexander V.

[["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","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"]]