Identification of Serum Peptidome Signatures of Non-Small Cell Lung Cancer

Klupczynska, Agnieszka; Światły, Agata; Hajduk, Joanna; Matysiak, Jan; Dyszkiewicz, Wojciech; Pawlak, Krystian; Kokot, Zenon J.

doi:10.3390/ijms17040410

Cited by 21 publications

(12 citation statements)

References 62 publications

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“…Mass spectroscopy is the most commonly reported technique for the recent investigations screening the LMWF for disease‐related information, probing and profiling proteomic information of hundreds of candidate disease biomarkers without the need for a priori knowledge of their existence or relevance to disease states . Facing the complexity of human serum, most approaches aiming for the identification and validation of LMWF diagnostic biomarkers have introduced HMWF depletion in their protocols .…”

Section: Results and Discussionmentioning

confidence: 99%

Screening the low molecular weight fraction of human serum using ATR-IR spectroscopy

et al. 2016

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Vibrational spectroscopic techniques can detect small variations in molecular content, linked with disease, showing promise for screening and early diagnosis. Biological fluids, particularly blood serum, are potentially valuable for diagnosis purposes. The so-called Low Molecular Weight Fraction (LMWF) contains the associated peptidome and metabolome and has been identified as potentially the most relevant molecular population for disease-associated biomarker research. Although vibrational spectroscopy can deliver a specific chemical fingerprint of the samples, the High Molecular Weight Fraction (HMWF), composed of the most abundant serum proteins, strongly dominates the response and ultimately makes the detection of minor spectral variations a challenging task. Spectroscopic detection of potential serum biomarkers present at relatively low concentrations can be improved using pre-analytical depletion of the HMWF. In the present study, human serum fractionation by centrifugal filtration was used prior to analysis by Attenuated Total Reflection infrared spectroscopy. Using a model sample based on glycine spiked serum, it is demonstrated that the screening of the LMWF can be applied to quantify blinded concentrations up to 50 times lower. Moreover, the approach is easily transferable to different bodily fluids which would support the development of more efficient and suitable clinical protocols exploring vibrational spectroscopy based ex-vivo diagnostic tools

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Section: Results and Discussionmentioning

confidence: 99%

Screening the low molecular weight fraction of human serum using ATR-IR spectroscopy

et al. 2016

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“…FlexControl 3.4 (Bruker Daltonics, Bremen, Germany) software was applied for the acquisition and processing of MS spectra. Evaluation of intra-day and inter-day reproducibility and of the applied protocol was reported previously [ 22 ].…”

Section: Methodsmentioning

confidence: 99%

Association between Venom Immunotherapy and Changes in Serum Protein—Peptide Patterns

et al. 2021

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Venom immunotherapy (VIT) is administered to allergic patients to reduce the risk of dangerous systemic reactions following an insect sting. To better understand the mechanism of this treatment and its impact on the human organism, we analysed serum proteomic patterns obtained at five time-points from Hymenoptera-venom-allergic patients undergoing VIT. For statistical analyses, patients were additionally divided into two groups (high responders and low responders) according to serum sIgG4 levels. VIT was found to be associated with changes in seven proteins: the fibrinogen alpha chain, complement C4-A, complement C3, filamin-B, kininogen-1, myosin-9 and inter-alpha-trypsin inhibitor heavy chain H1. The number of discriminative m/z (mass-to-charge ratio) features increased up to the 90th day of VIT, which may be associated with the development of immunity after the administration of increased venom doses. It may also suggest that during VIT, there may occur processes involved not only in protein synthesis but also in protein degradation (caused by proteolytic venom components). The results are consistent with measured serum sIgG4 levels, which increased from 2.04 mgA/I at baseline to 7.25 mgA/I at 90 days. Moreover, the major proteomic changes were detected separately in the high responder group. This may suggest that changes in protein–peptide profiles reflect the actual response to VIT.

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“…To obtain average serum proteomic/peptidomic profiles of each study groups and for collection and processing of the spectra, FlexControl 3.4 (Bruker Daltonics, Bremen, Germany) software was applied. Inter-day and intra-day reproducibility of the spectra obtained after ZipTip depletion was evaluated in our previous study [11].…”

Section: Methodsmentioning

confidence: 99%

Proteomic features characterization of Hymenoptera venom allergy

Matuszewska

Matysiak

Bręborowicz

et al. 2019

Allergy Asthma Clin Immunol

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BackgroundHymenoptera venom allergy is one of the most frequent causes of anaphylaxis. In its most severe form, the reaction to wasp and honey bee stings may be life-threatening. Therefore, immediate and proper diagnosis of venom allergy and implementation of suitable therapy are extremely important. Broadening the knowledge on the mechanism of the allergic reaction may contribute to the improvement of both diagnostic and treatment methods. Thus, this study aimed to discover changes in protein expression in serum of patients allergic to Hymenoptera (wasp and honeybee) venom and to point out proteins and peptides involved in the allergic inflammation.MethodsSerum proteomic patterns typical to allergic patients and healthy volunteers were obtained with MALDI-TOF (matrix-assisted laser desorption/ionization-time of flight) mass spectrometer. The spectra were processed, analyzed and compared using advanced bioinformatics tools. The discriminative peaks were subjected to identification with liquid chromatography coupled with tandem mass spectrometry.ResultsThis methodology allowed for the identification of four features differentiating between allergy and control groups. They were: fibrinogen alpha chain, coagulation factor XIII chain A, complement C4-A, and inter-alpha-trypsin inhibitor heavy chain H4. All of these proteins are involved in allergic inflammatory response.ConclusionsExtending the knowledge of the Hymenoptera venom sensitization will contribute to the development of novel, sensitive and specific methods for quick and unambiguous allergy diagnosis. Understanding the basis of the allergy at the proteomic level will support the improvement of preventive and therapeutic measures.

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Identification of Serum Peptidome Signatures of Non-Small Cell Lung Cancer

Cited by 21 publications

References 62 publications

Screening the low molecular weight fraction of human serum using ATR-IR spectroscopy

Screening the low molecular weight fraction of human serum using ATR-IR spectroscopy

Association between Venom Immunotherapy and Changes in Serum Protein—Peptide Patterns

Proteomic features characterization of Hymenoptera venom allergy

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