Assessment by Matrix‐Assisted Laser Desorption/Ionization Time‐of‐Flight Mass Spectrometry of the Effects of Preanalytical Variables on Serum Peptidome Profiles Following Long‐Term Sample Storage

Tsuchida, Sachio; Satoh, Mamoru; Umemura, Hiroshi; Sogawa, Kazuyuki; Takiwaki, Masaki; Ishige, Takayuki; Miyabayashi, Yui; Iwasawa, Yuuya; Kobayashi, Sohei; Beppu, Minako; Nishimura, Motoi; Kodera, Yasuhiro; Matsushita, Hiroshi; Nomura, Fumio

doi:10.1002/prca.201700047

Cited by 10 publications

(5 citation statements)

References 43 publications

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“…Collection, processing, storage and handling expose clinical biospecimens to pre-analytical variables that, when unaccounted for, have the potential to produce misleading results in downstream clinical research (1–5). For blood plasma and serum (P/S) 1 samples, numerous pre-analytical variables such as the type of collection tube, degree of tube filling, number of tube inversions, degree of hemolysis, and pre-centrifugation delay can quantitatively impact clinical measurements (6–9).…”

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confidence: 99%

Delta-S-Cys-Albumin: A Lab Test that Quantifies Cumulative Exposure of Archived Human Blood Plasma and Serum Samples to Thawed Conditions*[S]

Jeffs¹,

Jehanathan²,

Thibert³

et al. 2019

Molecular & Cellular Proteomics

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Exposure of blood plasma/serum (P/S) to thawed conditions (> −30 °C) can produce biomolecular changes that skew measurements of biomarkers within archived patient samples, potentially rendering them unfit for molecular analysis. Because freeze-thaw histories are often poorly documented, objective methods for assessing molecular fitness before analysis are needed. We report a 10-μl, dilute-and-shoot, intact-protein mass spectrometric assay of albumin proteoforms called “ΔS-Cys-Albumin” that quantifies cumulative exposure of archived P/S samples to thawed conditions. The relative abundance of S-cysteinylated (oxidized) albumin in P/S increases inexorably but to a maximum value under 100% when samples are exposed to temperatures > −30 °C. The difference in the relative abundance of S-cysteinylated albumin (S-Cys-Alb) before and after an intentional incubation period that drives this proteoform to its maximum level is denoted as ΔS-Cys-Albumin. ΔS-Cys-Albumin in fully expired samples is zero. The range (mean ± 95% CI) observed for ΔS-Cys-Albumin in fresh cardiac patient P/S (n = 97) was, for plasma 12–29% (20.9 ± 0.75%) and for serum 10–24% (15.5 ± 0.64%). The multireaction rate law that governs S-Cys-Alb formation in P/S was determined and shown to predict the rate of formation of S-Cys-Alb in plasma and serum samples—a step that enables back-calculation of the time at which unknown P/S specimens have been exposed to room temperature. A blind challenge demonstrated that ΔS-Cys-Albumin can detect exposure of groups (n = 6 each) of P/S samples to 23 °C for 2 h, 4 °C for 16 h, or −20 °C for 24 h—and exposure of individual specimens for modestly increased times. An unplanned case study of nominally pristine serum samples collected under NIH-sponsorship demonstrated that empirical evidence is required to ensure accurate knowledge of archived P/S biospecimen storage history.

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confidence: 99%

Delta-S-Cys-Albumin: A Lab Test that Quantifies Cumulative Exposure of Archived Human Blood Plasma and Serum Samples to Thawed Conditions*[S]

Jeffs¹,

Jehanathan²,

Thibert³

et al. 2019

Molecular & Cellular Proteomics

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show abstract

“…Provided standardized sample pretreatment, MS measurement, data processing and analysis, peptide and protein profiles are highly reproducible. Standardization of preanalytical factors such as anticoagulants, temperature, freeze-thaw cycles and storage conditions is critical in MS studies because they have significant impact on dynamic alterations of the acquired proteome (Baumann et al, 2005;Periano et al, 2016;Tsuchida et al, 2018).…”

Section: Discussionmentioning

confidence: 99%

Plasma Peptidome Pattern of Breast Cancer Using Magnetic Beads-Based Plasma Fractionation and MALDI-TOF MS: A Case Control Study in Egypt

Zaki

Ramadan

Moez

et al. 2019

Asian Pac J Cancer Prev

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Objective: The present study aimed to determine peptidome patterns in breast cancer (BC). Methods: We analyzed the plasma proteomic profiling of 80 BC patients and 50 healthy controls, using hydrophobic interaction chromatography magnetic beads (MB-HIC8) separation followed by Matrix assisted laser desorption ionization/ time of flight mass spectrometry (MALDI-TOF MS). Results: ClinProTools software identified 92 peaks that differed among the analyzed groups, 33 peaks were significantly different (P < 0.05). Of those, 22 peaks were up-regulated while 11 peaks were down-regulated in BC patients compared with the healthy controls. Three peptide ion signatures ( m/z 1,570.31, 1,897.4 and 2,568.17) were provided by the Quick Classifier model to discriminate BC patients from healthy control subjects with 96.4% accuracy. External validation was performed by an independent group and this achieved a sensitivity of 100% and a specificity of 76.9%. Conclusion: MALDI-TOF MS has good analytical performance in distinguishing BC patients from healthy controls.

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“…It is important to note that the level of detection (LOD) of MALDI-TOF-MS for a specific compound is primarily influenced by the chemical background noise. Therefore, increasing the number of laser shots does not significantly enhance the spectral quality ( 20 ).…”

Section: Methodsmentioning

confidence: 99%

Polyherbal formulation PL02 alleviates pain, inflammation, and subchondral bone deterioration in an osteoarthritis rodent model

Upadhyay,

Kalra,

Nilakhe

et al. 2023

Front. Nutr.

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IntroductionOsteoarthritis (OA) is a debilitating disease with significant personal and socioeconomic burdens worldwide.MethodsTo address this, we developed a multitargeted formulation called PL02, which includes standardized extracts of Rosa canina L, Hippophae rhamnoides, and collagen peptide. We tested the pharmacological efficacy of PL02 in a rodent model of OA induced by Monosodium iodoacetate (MIA).ResultsOur results demonstrate that oral administration of PL02 has antioxidant effects by down-regulating NOS, reduces pain-related behavior, and mitigates inflammation by inhibiting IL-1b and TNF-α production, as well as downregulating CGRP1 and COX-II. PL02 also exhibits anti-catabolic and chondroprotective activity by significantly downregulating MMP13 and upregulating BCL2. Additionally, PL02 demonstrates chondrogenic activity by significantly upregulating SOX-9 (a master regulator of chondrogenesis), Coll-I, and aggrecan, which are major components of articular cartilage. Furthermore, PL02 prevents microarchitectural deterioration of subchondral bone.ConclusionOverall, PL02 is an orally active, multi-targeted therapy that not only alleviates pain and inflammation but also effectively halts cartilage and subchondral bone deterioration. It represents a safe and promising candidate for the treatment and management of OA.

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Assessment by Matrix‐Assisted Laser Desorption/Ionization Time‐of‐Flight Mass Spectrometry of the Effects of Preanalytical Variables on Serum Peptidome Profiles Following Long‐Term Sample Storage

Cited by 10 publications

References 43 publications

Delta-S-Cys-Albumin: A Lab Test that Quantifies Cumulative Exposure of Archived Human Blood Plasma and Serum Samples to Thawed Conditions*[S]

Delta-S-Cys-Albumin: A Lab Test that Quantifies Cumulative Exposure of Archived Human Blood Plasma and Serum Samples to Thawed Conditions*[S]

Plasma Peptidome Pattern of Breast Cancer Using Magnetic Beads-Based Plasma Fractionation and MALDI-TOF MS: A Case Control Study in Egypt

Polyherbal formulation PL02 alleviates pain, inflammation, and subchondral bone deterioration in an osteoarthritis rodent model

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