Assessing the commutability of reference material formats for the harmonization of amyloid-β measurements

Bjerke, Maria; Andréasson, Ulf; Kuhlmann, Julia; Portelius, Erik; Pannee, Josef; Lewczuk, Piotr; Umek, Robert M.; Vanmechelen, Eugeen; Vanderstichele, Hugo; Stoops, Erik; Lewis, Jennifer; Vandijck, Manu; Kostanjevečki, Vesna; Jeromin, Andreas; Salamone, Salvatore J.; Schmidt, Oliver; Matzen, Anja; Madin, Kairat; Eichenlaub, Udo; Bittner, Tobias; Shaw, Leslie M.; Zegers, Ingrid; Zetterberg, Henrik; Blennow, Kaj

doi:10.1515/cclm-2015-0733

Cited by 54 publications

(55 citation statements)

References 32 publications

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“…Although both platforms are consistent in showing increases in plasma tau levels in patients with AD, the Aβ42 findings were opposite. It has been cautioned that comparing findings between different platforms could be problematic [73, 74]. However, future studies are needed to replicate the differences in findings between platforms before the issue of whether plasma Aβ42 levels are increased or decreased in AD can be resolved.…”

Section: Resultsmentioning

confidence: 99%

Amyloid Beta and Tau as Alzheimer’s Disease Blood Biomarkers: Promise From New Technologies

2017

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The utility of the levels of amyloid beta (Aβ) peptide and tau in blood for diagnosis, drug development, and assessment of clinical trials for Alzheimer’s disease (AD) has not been established. The lack of availability of ultra-sensitive assays is one critical issue that has impeded progress. The levels of Aβ species and tau in plasma and serum are much lower than levels in cerebrospinal fluid. Furthermore, plasma or serum contain high levels of assay-interfering factors, resulting in difficulties in the commonly used singulex or multiplex ELISA platforms. In this review, we focus on two modern immune-complex-based technologies that show promise to advance this field. These innovative technologies are immunomagnetic reduction technology and single molecule array technology. We describe the technologies and discuss the published studies using these technologies. Currently, the potential of utilizing these technologies to advance Aβ and tau as blood-based biomarkers for AD requires further validation using already collected large sets of samples, as well as new cohorts and population-based longitudinal studies.

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Section: Resultsmentioning

confidence: 99%

Amyloid Beta and Tau as Alzheimer’s Disease Blood Biomarkers: Promise From New Technologies

2017

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“…This pattern may suggest that the reanalysed results are a more faithful approximation of amyloid-β 42 levels across groups, the centralized analysis component having removed the variance imposed by differences in INNOTEST measurements between laboratories. While it is thus tempting to speculate that MSD and MS-RMP providing more accurate estimates of amyloid-β 42 concentration levels, this explanation seems unlikely since these analytical techniques have been shown to correlate tightly—both with one another, and with INNOTEST—when samples are analysed in a single run under standardized conditions (Bjerke et al , 2016). …”

Section: Discussionmentioning

confidence: 99%

“…Future studies on amyloid biomarkers, however, should examine the effect of this type of correction. As a further caveat, the INNOTEST amyloid-β 42 ELISA would ideally have been used instead of MSD, though the effect of this is likely to have been minimal (Bjerke et al , 2016). Other possible limitations include the relatively low number of cognitively normal subjects and patients with FTD and VaD, as well as the fact that APOE genotype data was not available for all subjects.…”

Section: Discussionmentioning

confidence: 99%

Pittsburgh compound B imaging and cerebrospinal fluid amyloid-β in a multicentre European memory clinic study

Leuzy

Chiotis

Hasselbalch

et al. 2016

Brain

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110

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“…When using algorithms including concentrations of a number of different biomarkers (e.g., synapse proteins, tau, Aβ isoforms) for decision-making, one needs to understand how each individual protein will be affected by changes in (pre-)analytical conditions. For example, Bjerke et al [17] reported that only native CSF without additives is commutable for multiple method comparisons, including mass spectrometry. In addition, the selection of the matrix type for use as a quality control sample in the assay is important [18], while the effect of changes in biomarker concentrations on clinical decision-making must be documented for each analyte [19].…”

Section: Discussionmentioning

confidence: 99%

Recommendations for cerebrospinal fluid collection for the analysis by ELISA of neurogranin trunc P75, α-synuclein, and total tau in combination with Aβ(1–42)/Aβ(1–40)

Vanderstichele¹,

Demeyer²,

Janelidze

et al. 2017

Alz Res Therapy

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BackgroundThe pathophysiology of neurodegeneration is complex. Its diagnosis requires an early identification of sequential changes in several hallmarks in the brains of affected subjects. The presence of brain pathology can be visualized in the cerebrospinal fluid (CSF) by protein profiling. It is clear that the field of Alzheimer’s disease (AD) will benefit from an integration of algorithms including CSF concentrations of individual proteins, especially as an aid in clinical decision-making or to improve patient enrolment in clinical trials. The protein profiling approach requires standard operating procedures for collection and storage of CSF which must be easy to integrate into a routine clinical lab environment. Our study provides recommendations for analysis of neurogranin trunc P75, α-synuclein, and tau, in combination with the ratio of β-amyloid Aβ(1–42)/Aβ(1–40).MethodsProtocols for CSF collection were compared with CSF derived from subjects with normal pressure hydrocephalus (n = 19). Variables included recipient type (collection, storage), tube volume, and addition of detergents at the time of collection. CSF biomarker analysis was performed with enzyme-linked immunosorbent assays (ELISAs). Data were analyzed with linear repeated measures and mixed effects models.ResultsAdsorption to recipients is lower for neurogranin trunc P75, α-synuclein, and tau (<10%), as compared to Aβ(1–42). For neurogranin trunc P75 and total tau, there is still an effect on analyte concentrations as a function of the tube volume. Protocol-related differences for Aβ(1–42) can be normalized at the (pre-)analytical level using the ratio Aβ(1–42)/Aβ(1–40), but not by using the ratio Aβ(1–42)/tau. The addition of detergent at the time of collection eliminates differences due to adsorption.ConclusionsOur study recommends the use of low protein binding tubes for quantification in CSF (without additives) of all relevant CSF biomarkers. Pre-analytical factors have less effect on α-synuclein, neurogranin trunc P75, and total tau, as compared to Aβ(1–42). The ratio of Aβ(1–42)/Aβ(1–40), but not Aβ(1–42)/tau, can be used to adjust for pre-analytical differences in analyte concentrations. Our study does not recommend the inclusion of detergents at the time of collection of CSF. The present results provide an experimental basis for new recommendations for parallel analysis of several proteins using one protocol for collection and storage of CSF.Electronic supplementary materialThe online version of this article (doi:10.1186/s13195-017-0265-7) contains supplementary material, which is available to authorized users.

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Assessing the commutability of reference material formats for the harmonization of amyloid-β measurements

Cited by 54 publications

References 32 publications

Amyloid Beta and Tau as Alzheimer’s Disease Blood Biomarkers: Promise From New Technologies

Amyloid Beta and Tau as Alzheimer’s Disease Blood Biomarkers: Promise From New Technologies

Pittsburgh compound B imaging and cerebrospinal fluid amyloid-β in a multicentre European memory clinic study

Recommendations for cerebrospinal fluid collection for the analysis by ELISA of neurogranin trunc P75, α-synuclein, and total tau in combination with Aβ(1–42)/Aβ(1–40)

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