{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T22:15:31Z","timestamp":1759961731472,"version":"3.37.3"},"reference-count":80,"publisher":"Walter de Gruyter GmbH","issue":"10","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,1,28]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background:<\/jats:title><jats:p>A decreased level of A\u03b21-42 in cerebrospinal fluid (CSF) is characteristic of Alzheimer disease and often used to support clinical diagnosis. The measured concentration of CSF A\u03b21-42, however, depends strongly on several pre-analytical and analytical \u201cconfounding\u201d factors such as sample collection, material of testing tube, CSF handling and storage procedures (e.g. transfer to new tubes after centrifugation, freeze-thaw effects). As a consequence, substantial variations in the measured levels of this biomarker are observed even for the same sample. This study investigates whether the accuracy of quantitative analysis of CSF A\u03b21-42 can be improved by pre-analytical treatment of CSF with agents that could potentially reduce a freeze-thaw and adhesion-related depletion of A\u03b21-42 from CSF, including modulators of A\u03b2 aggregation and cryoprotecting or anti-adhesion agents.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods:<\/jats:title><jats:p>The concentration of CSF A\u03b21-42 was assessed with a novel Elecsys immunoassay developed for quantification of A\u03b21-42 in human CSF.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results:<\/jats:title><jats:p>Low-molecular weight A\u03b2 oligomerization inhibitors, \u03b2-sheet breaker peptides, or the mid domain 4G8 antibody do not improve the stability of CSF A\u03b21-42 during a repeated freeze-thaw treatment. Cryoprotecting agents reduce a freeze-thaw dependent loss of A\u03b21-42 only when spiked to CSF to final concentration of 300 mM or higher. Adhesion of A\u03b21-42 can be prevented by pre-treating CSF with Tween or by using tubes with a siliconized surface.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions:<\/jats:title><jats:p>Between-center variability in measured level of CSF A\u03b21-42 can be reduced only by standardized CSF collection into one specific tube that, without centrifugation, transfer or other types of pre-analytical processing, is directly analyzed after sample collection.<\/jats:p><\/jats:sec>","DOI":"10.1515\/cclm-2016-1061","type":"journal-article","created":{"date-parts":[[2017,2,4]],"date-time":"2017-02-04T13:26:25Z","timestamp":1486214785000},"source":"Crossref","is-referenced-by-count":18,"title":["Accuracy of cerebrospinal fluid A\u03b21-42 measurements: evaluation of pre-analytical factors using a novel Elecsys immunosassay"],"prefix":"10.1515","volume":"55","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9857-6320","authenticated-orcid":false,"given":"Malgorzata","family":"Rozga","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tobias","family":"Bittner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kina","family":"H\u00f6glund","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kaj","family":"Blennow","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","reference":[{"key":"ref31","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1038\/nsmb.1799","article-title":"Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils","volume":"17","year":"2010","journal-title":"Nat Struct Mol Biol"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"8368","DOI":"10.1073\/pnas.91.18.8368","article-title":"Transthyretin sequesters amyloid beta protein and prevents amyloid formation","volume":"91","year":"1994","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref311","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1365-2621.1988.tb10163.x","article-title":"Cryoprotective effects of sugar, polyols, and or phosphates on Alaska pollack surimi","volume":"53","year":"1988","journal-title":"J Food Sci"},{"key":"ref621","doi-asserted-by":"crossref","first-page":"1848","DOI":"10.1002\/cmdc.200800273","article-title":"Reduction of Alzheimer\u2019s disease amyloid plaque load in transgenic mice by D3, A D-enantiomeric peptide identified by mirror image phage display","volume":"3","year":"2008","journal-title":"ChemMedChem"},{"key":"ref241","doi-asserted-by":"crossref","first-page":"9906","DOI":"10.1021\/bi060837s","article-title":"N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. 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