Multiparametric Analysis of Mass Spectrometry‐Based Proteome Profiling in Gestation‐Related Diseases

Glocker, Michael O.; Röwer, Claudia; Wölter, Manja; Koy, Cornelia; Reimer, Toralf; Pecks, Ulrich

doi:10.1002/9783527654703.ch12

Cited by 5 publications

(13 citation statements)

References 61 publications

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“…Ion signal areas were determined with the ClinProTools 2.2 software (Bruker Daltronik, Bremen, Germany) as described previously. 23,29…”

Section: Patients Materials and Methodsmentioning

confidence: 99%

“…Conventional blood serum sample treatment was applied, i.e. serum was shock frozen and stored at À80 C. 9,10,23 Altogether, time between blood sample collection and storage of frozen serum aliquots averaged around less than 1 hour. Frozen serum aliquots were shipped on dry ice to the Proteome Center Rostock to maintain the cold-chain.…”

Section: Serum Storage and Transportmentioning

confidence: 99%

“…Ion signal areas were determined with the ClinProTools 2.2 software (Bruker Daltronik, Bremen, Germany) as described previously. 23,29 Raw data processing and bio-statistical analysis Our recently established multiparametric analysis 9,10,23 in which the signal areas of five ion signals within each spectrum were brought into context to each other by forming quotients of ion signal areas was applied. First, the signal area of the ion at m/z 8916 was divided by the signal area of the ion at m/z 8205 from one and the same spectrum to produce a value for spectra assessment (quotient A).…”

Section: Maldi-ms Analysis Of Serum Proteinsmentioning

confidence: 99%

“…In this study, we are comparing the linear mode MALDI-ToF mass spectra obtained from intact blood serum proteins either stored on a membrane disc which functions as serum storage device and onto which serum can be deposited and kept at room temperature with mass spectra obtained from fresh frozen serum after conventional work-up. 9,10,23 Key step for successful relative abundance analysis of intact serum proteins derived from dried serum spots by mass spectrometry is the resolubilization procedure by which deposited proteins can be prepared and analyzed in a reliable and robust fashion.…”

Section: Introductionmentioning

confidence: 99%

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Comparison of blood serum protein analysis by MALDI-MS from either conventional frozen samples or storage disc-deposited samples: A study with human serum from pregnant donors and from patients with intrauterine growth restriction

Wölter

Russ

Okai

et al. 2018

Eur J Mass Spectrom (Chichester)

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Mass spectrometric profiling of intact serum proteins, i.e. determination of relative protein abundance differences, was performed using two different serum sample preparation methods: one with frozen and thawed serum, the other with at room temperature deposited and dried serum. Since in a typical clinical setting freezing of serum is difficult to achieve, sampling at room temperature is preferred and can be met when using the Noviplex™ card system. Once deposited and dried, serum proteins can be stored and shipped at room temperature. After resolubilization of serum proteins from “dried serum spots”, mass spectra of high quality have been recorded comparable to those that were obtained using fresh-frozen and subsequently thawed serum samples. Differentiation between patients with intrauterine growth restriction and control individuals was achievable, independent from the sample work-up procedure. Having at hand a reliable and robust method for serum storage and shipment which works at room temperature bridges the gap between the clinics and the protein analysis laboratory. Our novel serum handling protocol reduces costs for both, storage and shipping, and ultimately enables clinical risk assessment based on mass spectrometric determination of intact protein abundance profiles.

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“…Ion signal areas were determined with the ClinProTools 2.2 software (Bruker Daltronik, Bremen, Germany) as described previously. 23,29…”

Section: Patients Materials and Methodsmentioning

confidence: 99%

Section: Serum Storage and Transportmentioning

confidence: 99%

Section: Maldi-ms Analysis Of Serum Proteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Comparison of blood serum protein analysis by MALDI-MS from either conventional frozen samples or storage disc-deposited samples: A study with human serum from pregnant donors and from patients with intrauterine growth restriction

Wölter

Russ

Okai

et al. 2018

Eur J Mass Spectrom (Chichester)

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“…SELDI-MS has been applied to acquire proteomic profiles of cerebrospinal fluid [ 65 ], amniotic fluid [ 66 , 67 , 68 , 69 , 70 , 71 ], and urine [ 72 , 73 , 74 ] to determine protein biomarkers for pre-eclampsia and intra-amniotic infection (IAI)—a major cause of preterm birth. Serum proteomic profiles obtained by MALDI-MS have also been used to differentiate pre-eclampsia patient samples from those of healthy controls [ 75 , 76 ]. Various potential protein biomarkers for pre-eclampsia and IAI were identified ( Table 1 ).…”

Section: Top-down Proteomic Profiling By Laser Mass Spectrometrymentioning

confidence: 99%

Mass Spectrometry-Based Proteomics for Pre-Eclampsia and Preterm Birth

Law

Han

Tong

et al. 2015

IJMS

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Pregnancy-related complications such as pre-eclampsia and preterm birth now represent a notable burden of adverse health. Pre-eclampsia is a hypertensive disorder unique to pregnancy. It is an important cause of maternal death worldwide and a leading cause of fetal growth restriction and iatrogenic prematurity. Fifteen million infants are born preterm each year globally, but more than one million of those do not survive their first month of life. Currently there are no predictive tests available for diagnosis of these pregnancy-related complications and the biological mechanisms of the diseases have not been fully elucidated. Mass spectrometry-based proteomics have all the necessary attributes to provide the needed breakthrough in understanding the pathophysiology of complex human diseases thorough the discovery of biomarkers. The mass spectrometry methodologies employed in the studies for pregnancy-related complications are evaluated in this article. Top-down proteomic and peptidomic profiling by laser mass spectrometry, liquid chromatography or capillary electrophoresis coupled to mass spectrometry, and bottom-up quantitative proteomics and targeted proteomics by liquid chromatography mass spectrometry have been applied to elucidate protein biomarkers and biological mechanism of pregnancy-related complications. The proteomes of serum, urine, amniotic fluid, cervical-vaginal fluid, placental tissue, and cytotrophoblastic cells have all been investigated. Numerous biomarkers or biomarker candidates that could distinguish complicated pregnancies from healthy controls have been proposed. Nevertheless, questions as to the clinically utility and the capacity to elucidate the pathogenesis of the pre-eclampsia and preterm birth remain to be answered.

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Profiling of intact blood proteins by matrix‐assisted laser desorption/ionization mass spectrometry without the need for freezing – Dried serum spots as future clinical tools for patient screening

Okai

Wölter

Russ

et al. 2021

Rapid Comm Mass Spectrometry

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Rationale To open up new ways for matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS)‐based patient screening, blood serum is the most preferred specimen because of its richness in patho‐physiological information and due to ease of collection. To overcome deleterious freeze/thaw cycles and to reduce high costs for shipping and storage, we sought to develop a procedure which enables MALDI‐MS protein profiling of blood serum proteins without the need for serum freezing. Methods Blood sera from patients/donors were divided into portions which after pre‐incubation were fast frozen. Thawed aliquots were deposited on filter paper discs and air‐dried at room temperature. Intact serum proteins were eluted with acid‐labile detergent‐containing solutions and were desalted by employing a reversed‐phase bead system. Purified protein solutions were screened by MALDI‐MS using standardized instrument settings. Results MALDI mass spectra from protein solutions which were eluted from filter paper discs and desalted showed on average 25 strong ion signals (mass range m/z 6000 to 10,000) from intact serum proteins (apolipoproteins, complement proteins, transthyretin and hemoglobin) and from proteolytic processing products. Semi‐quantitative analysis of three ion pairs: m/z 6433 and 6631, m/z 8205 and 8916, as well as m/z 9275 and 9422, indicated that the mass spectra from either pre‐incubated fast‐frozen serum or pre‐incubated dried serum spot eluted serum contained the same information on protein composition. Conclusions A workflow that avoids the conventional cold‐chain and yet enables the investigation of intact serum proteins and/or serum proteolysis products by MALDI‐MS profiling was developed. The presented protocol tremendously broadens the clinical application of MALDI‐MS and simultaneously allows a reduction in the costs for storage and shipping of serum samples. This will pave the way for clinical screening of patients also in areas with limited access to health care systems, and/or specialized laboratories.

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Multiparametric Analysis of Mass Spectrometry‐Based Proteome Profiling in Gestation‐Related Diseases

Cited by 5 publications

References 61 publications

Comparison of blood serum protein analysis by MALDI-MS from either conventional frozen samples or storage disc-deposited samples: A study with human serum from pregnant donors and from patients with intrauterine growth restriction

Comparison of blood serum protein analysis by MALDI-MS from either conventional frozen samples or storage disc-deposited samples: A study with human serum from pregnant donors and from patients with intrauterine growth restriction

Mass Spectrometry-Based Proteomics for Pre-Eclampsia and Preterm Birth

Profiling of intact blood proteins by matrix‐assisted laser desorption/ionization mass spectrometry without the need for freezing – Dried serum spots as future clinical tools for patient screening

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