A PSA-guided approach for a better diagnosis of prostatic adenocarcinoma based on MALDI profiling and peptide identification

Differentiating tumor heterogeneity in formalin-fixed paraffin-embedded (FFPE) prostate adenocarcinoma tissues using principal component analysis of matrix-assisted laser desorption/ionization imaging mass spectral data

“…Our findings are in accordance with some of the MALDI‐IMS data presented in other studies. In MALDI‐MS profiling of human serum samples, Fania and coworkers recently found an overexpression of the ion peaks at m/z 3448.63 and 6809.47 when compared with matched normal samples, which correlates with the ion peaks at m/z 3441 and 6799 detected in our study . The mass ion peak at m/z 3441 was also detected with increased expression in cancerous regions of fresh‐frozen prostate tissues in a MALDI‐IMS study presented by Schwamborn and coworkers .…”

“…[20][21][22] Recently, MALDI -MS profiling of serum proteins demonstrated the ability to discriminate PCa patients' profiles from control samples. [23] MALDI-time-of-flight (TOF)-MS protein profiles of urine samples of healthy donors have been compared with prostate cancer patients for a differential proteomic study. [24] Matrix coating assisted by an electric field (MCAEF) has been used for overall enhancement of MALDI-IMS analysis of human prostate cancer biomarkers.…”

Protein signature in cerebrospinal fluid and serum of Alzheimer’s disease patients: The case of apolipoprotein A-1 proteoforms

“…In addition, this analysis allows to process a considerable number of samples in a short time with low costs, providing simple spectra, thus reducing the burden of MS data generated by bottom-up approaches, making clinical studies affordable. The drawback of this approach is that it requires two steps: the first implies the presence of best separating peaks, and the second requires peak isolation by chromatography or gel-based fractionation and identification as described by our and other studies [23, 31, 32]. However, this approach enables a protein fingerprint of intact proteins of minute quantities of CSF.…”

“…One ug of each CSF sample of AD, iNPH and healthy subjects were diluted 1:1 (w/V) in DHAP (2,5-dihydroxyacetophenone) matrix (15 mg/mL in 3:1 ethanol:diammonium hydrogen citrate, 5% trifluoroacetic acid), analyzed in four replicates by MALDI profiling using an AnchorChip plate (800–384 target, Bruker Daltonics), and dried at room temperature. For serum analysis, samples were immunodepleted from the 6 most abundant proteins and subjected to mass spectrometric analysis as previously described [23, 24]. …”

“…Spectrometer and spectra acquisition settings were as described in [23]. Spectra were analyzed by ClinProTools software v. 2.2 (Bruker Daltonics) using 800 resolution, Top Hat Baseline, 10% minimal baseline width, Savitsky-Golay smoothing as spectra parameters.…”