Mass Spectrometry–Based Candidate Reference Measurement Procedure for Quantification of Amyloid-β in Cerebrospinal Fluid

Leinenbach, Andreas; Pannee, Josef; Dülffer, Thomas; Huber, Andreas; Bittner, Tobias; Andréasson, Ulf; Gobom, Johan; Zetterberg, Henrik; Kobold, Uwe; Portelius, Erik; Blennow, Kaj

doi:10.1373/clinchem.2013.220392

Cited by 138 publications

(106 citation statements)

References 22 publications

(15 reference statements)

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“…If the methods give correlating results, the use of a commutable CRM for calibration should make it possible to produce values that are comparable irrespective of analytical method, time or place of measurement [32]. In the present study, it was shown that the majority of the results of the different immunoassays correlate well; and in addition, they also correlate with results from the SRM-based method, which has now been published as candidate SRM-based RMP [27,33]. The first substudy confirmed that the majority of methods tested were highly correlated (R 2 > 0.9) as shown previously [19].…”

Section: Discussionmentioning

confidence: 49%

“…Duplicate samples 300 ng/L, 800 ng/L, and 1300 ng/L. The SRM method was performed on a triple quadrupole MS as previously described [26], except that calibration was performed using the surrogate analyte approach [27]. All CSF samples were left-over samples from the clinical routine at the Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden.…”

Section: Materials and Measurement Procedures Commutability I And Iimentioning

confidence: 99%

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

Bjerke

Andréasson

Kuhlmann

et al. 2015

Clinical Chemistry and Laboratory Medicine (CCLM)

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Background: The cerebrospinal fluid (CSF) amyloid-β (Aβ42) peptide is an important biomarker for Alzheimer's disease (AD). Variability in measured Aβ42 concentrations at different laboratories may be overcome by standardization and establishing traceability to a reference system. Candidate certified reference materials (CRMs) are validated herein for this purpose. Methods: Commutability of 16 candidate CRM formats was assessed across five CSF Aβ42 immunoassays and one mass spectrometry (MS) method in a set of 48 individual clinical CSF samples. Promising candidate CRM formats (neat CSF and CSF spiked with Aβ42) were identified and subjected to validation across eight (Elecsys, EUROIMMUN, IBL, INNO-BIA AlzBio3, INNOTEST, MSD,

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Section: Discussionmentioning

confidence: 49%

Section: Materials and Measurement Procedures Commutability I And Iimentioning

confidence: 99%

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

Bjerke

Andréasson

Kuhlmann

et al. 2015

Clinical Chemistry and Laboratory Medicine (CCLM)

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“…2A) and CHO-7PA2-APP751 (Fig. 2B) using LC-MS/MS [34,35]. Like Aftins [13,14], triazines induced a reduction in Aβ 38 levels, a slight increase or modest decrease in Aβ 40 levels and a strong increase in Aβ 42 levels (Fig.…”

Section: Mass Spectrometric Quantification and Profile Analysis Of Inmentioning

confidence: 99%

“…Solid phase extraction, liquid chromatography (LC) and MS/MS analysis of Aβ species was performed as described previously [34,35] peptides (rPeptide) were added to a final concentration of 1.6 ng/mL in calibrators and unknown samples as internal standards. Standard curves were constructed using the unlabeled to 15 N-Aβ peak area ratios and fitted using linear regression.…”

Section: Supplementary Informationmentioning

confidence: 99%

Specific Triazine Herbicides Induce Amyloid-β42 Production

Portelius

Durieu

Bodin

et al. 2016

JAD

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Proteolytic cleavage of the amyloid precursor protein (AβPP) by secretases leads to extracellular release of amyloid β (Aβ) peptides. Increased production of Aβ 42 over Aβ 40 and aggregation into oligomers and plaques constitute an Alzheimer's disease (AD) hallmark.Identifying products of the 'human chemical exposome' (HCE) able to induce Aβ 42 production may be a key to understand some of the initiating causes of AD and to generate non-genetic, chemically-induced AD animal models. A cell model was used to screen HCE libraries for Aβ 42 inducers. Out of 3500+ compounds, six triazine herbicides were found that induced a β-and γ-secretases -dependent, 2-10 fold increase in the production of extracellular Aβ 40 than neurons derived from healthy controls iPSCs (AβPP WT). Triazines enhanced Aβ 42 production in both control and AD neurons. Triazines also shifted the cleavage pattern of alcadeinα, another γ-secretase substrate, suggesting a direct effect of triazines on γ-secretase activity. In conclusion, several widely used triazines enhance the production of toxic, aggregation prone Aβ 42 /Aβ 43 amyloids, suggesting the possible existence of environmental "Alzheimerogens" which may contribute to the initiation and propagation of the amyloidogenic process in late-onset AD.

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“…Production of candidate CRMs for Aβ 42 is an ongoing work with the efforts from the IFCC working group on CSF proteins [49] and from the BIOMARKAPAD consortium. Thereby, two candidate RMPs for quantification of Aβ 42 [50,51] and one for quantification of t-Tau [52] were recently reported.…”

Section: Variability Linked To Kit Providersmentioning

confidence: 99%

Pre-analytical and analytical factors influencing Alzheimer's disease cerebrospinal fluid biomarker variability

Fourier

Portelius

Zetterberg

et al. 2015

Clinica Chimica Acta

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Mass Spectrometry–Based Candidate Reference Measurement Procedure for Quantification of Amyloid-β in Cerebrospinal Fluid

Cited by 138 publications

References 22 publications

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

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

Specific Triazine Herbicides Induce Amyloid-β42 Production

Pre-analytical and analytical factors influencing Alzheimer's disease cerebrospinal fluid biomarker variability

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