Dataset Information

Oxidized fibrinogen HPLC-MS/MS

ABSTRACT: Fibrinogen is highly susceptible to oxidation compared to other plasma proteins. Fibrinogen oxidation damages its structure and affects the protein function. Fibrinogen was isolated from citrated human plasma by the modified cold ethanol precipitation technique. Oxidation of fibrinogen by ozone: a solution of 2.0 mg of fibrinogen in 1 ml of 0.05 M Tris/0.15 M NaCl buffer (pH 7.4) was introduced into a quartz reactor filled with ozone–oxygen mixture. The full exhaustion of ozone in each experiment was confirmed by spectrophotometry by the absorption band at 254 nm. The amount of ozone was varied in the range of 50–100 μM per 1 μM of fibrinogen. Ozone-induced oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains upon addition of various amounts of the oxidizer have been studied by mass-spectrometry.

INSTRUMENT(S): LTQ FT Ultra

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Lyubov Yurina

LAB HEAD: Mark Rosenfeld

PROVIDER: PXD012046 | Pride | 2019-04-04

REPOSITORIES: Pride

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Publications

Ozone-induced damage of fibrinogen molecules: identification of oxidation sites by high-resolution mass spectrometry.

Yurina Lyubov L Vasilyeva Alexandra A Indeykina Maria M Bugrova Anna A Biryukova Marina M Kononikhin Alexey A Nikolaev Evgene E Rosenfeld Mark M

Free radical research 20190401 4

Fibrinogen is highly susceptible to oxidation compared to other plasma proteins. Fibrinogen oxidation damages its structure and affects the protein function. Ozone-induced oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains upon addition of various amounts of the oxidiser were studied by mass spectrometry. Amino acid residues located on all three chains and main structural parts of the protein were revealed to be involved in oxidation. The αC-connector was shown to be most ...[more]

PMID: 30935261

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Project description:Our experiments examined T-lymphocyte numbers and effector-functions in peritoneal contamination and infection (PCI) a mouse model of sepsis. One of our main questions was how T-lymphocytes reconstitute after sepsis-induced lymphopenia. We investigated the quantitative and qualitative recovery of T lymphocytes for 3.5 months after sepsis with or without IL-7 treatment. Sepsis is an immunological dysfunction against pathogens leading to inflammation with massive cytokine production. Simultaneously immunosuppression occurs e.g. lymphopenia, which is a hallmark of sepsis. The resulting immunosuppression is associated with secondary infections, which are often lethal. Moreover sepsis-survivors are burdened with increased morbidity and mortality for several years after the sepsis episode. The duration and clinical consequences of sepsis induced-immunosuppression are currently unknown. More than 50% of T-cells undergo apoptosis shortly after sepsis-induction. However, 8 days after sepsis onset, surviving mice present normal lymphocyte counts. Theoretically, T-cells could reconstitute in two different ways. Firstly, the diminished pool of T-cells is replenished by newly in thymus produced T-cells with new diverse T-cell-receptors (TCRs). Alternatively, remaining T-cells start to proliferate until reaching normal cell count. If this was the case all divided cells shared the same TCRs as primary cells. This could lead to a narrowed TCR diversity within a quantitative normalized T-cell pool and would be an explanation for the long-lasting immune incompetence. To address the question how T-cells recover from lymphopenia we applied next generation sequencing (NGS) to analyse TCR diversity in septic and healthy mice. One group of septic mice received Interleukin-7 (IL-7), an interleukin which regulates T-cell homeostasis and is a promising therapeutically approach for septic patients. 50000 sequences per mouse were analyzed and the three different groups (controls, sepsis, sepsis + IL-7 treatment) compared regarding their diversity. The sequenced raw data (fastq) are uploaded in this library.

Dataset Information

Oxidized fibrinogen HPLC-MS/MS

Publications

Ozone-induced damage of fibrinogen molecules: identification of oxidation sites by high-resolution mass spectrometry.

Similar Datasets

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