Beta-amyloid peptide variants in brains and cerebrospinal fluid from amyloid precursor protein (APP) transgenic mice: comparison with human Alzheimer amyloid.

In this study, we report a detailed analysis of the different variants of amyloid-β (Aβ) peptides in the brains and the cerebrospinal fluid from APP23 transgenic mice, expressing amyloid precursor protein with the Swedish familial Alzheimer disease mutation, at different ages. Using one- and two-dimensional gel electrophoresis, immunoblotting, and mass spectrometry, we identified the Aβ peptides Aβ(1-40), -(1-42), -(1-39), -(1-38), -(1-37), -(2-40), and -(3-40) as well as minor amounts of pyroglutamate-modified Aβ (Aβ(N3pE)) and endogenous murine Aβ in brains from 24-month-old mice. Chemical modifications of the N-terminal amino group of Aβ were identified that had clearly been introduced during standard experimental procedures.

Apolipoprotein A-I as a candidate serum marker for the response to lithium treatment in bipolar disorder.

The molecular basis of bipolar disorder (BD) is still unknown as is the mechanism through which lithium, the therapy of choice, exerts its effects in treatment of BD. So far, no biomarkers exist to facilitate diagnosis of BD or treatment evaluation. To investigate whether BD and its treatment with lithium leaves a characteristic signature in the serum proteome, we used SELDI-TOF MS to analyze individual serum samples from BD patients treated with lithium (BD-plus-Li, n=15) or other drugs (BD-minus-Li, n=10) and from healthy controls (n=15).

Metallomics studies of human blood serum from treated bipolar disorder patients.

In the present work, metallomics studies using biomolecular (matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry, MALDI-TOF MS/MS) and elemental mass spectrometry (laser ablation inductively coupled plasma mass spectrometry, LA-ICPMS) of human blood serum samples from bipolar disorder (BD) patients compared to controls were performed. The serum samples from three different groups: control (n = 25), BD patients treated with Li (n = 15), and BD patients not treated with Li (n = 10), were pooled according to their groups and separated by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). Then, in order to determine the metals bound to the protein spots and search for differences among the studied groups, the 2-D gels were analyzed by LA-ICPMS in three distinct modes: bioimaging of metals in gel sections, line scan through the protein spots, and microlocal analysis of selected protein spots.

Lysozyme in wine: A risk evaluation for consumers allergic to hen's egg.

Lysozyme used in wine production could present a risk for consumers allergic to hen's egg. Thus, precautionary labeling of lysozyme on wines has been adopted within the European Community by updating Annex IIIa by Directive 2007/68/EC on November 27, 2007. Since no scientific data is known about the actual amounts and risks of lysozyme in wines, various in vitro efforts and skin prick tests were applied in this study to evaluate the presence of lysozyme in wines and the reactivity of those residues in allergic individuals and to fulfill the claim of updating Annex IIIa announced in Directive 2003/89/EC.

Cerebrospinal fluid-optimized two-dimensional difference gel electrophoresis (2-D DIGE) facilitates the differential diagnosis of Creutzfeldt-Jakob disease.

So far only the detection of 14-3-3 proteins in cerebrospinal fluid (CSF) is included in the diagnostic criteria for sporadic Creutzfeldt-Jakob disease (sCJD). However, this assay cannot be used for screening because of the high rate of false positive results in sCJD, and often negative results in variant CJD. To facilitate the differential diagnosis of CJD, we applied 2-D differential gel-electrophoresis (2-D DIGE) as a quantitative proteomic screening system for CSF proteins.