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Catalase Activity of IgG and κκ-IgG, λλ-IgG, and κλ-IgG Subfractions in HIV-Infected Patients and Healthy Donors. / Tolmacheva, Anna S.; Sedykh, Sergey E.; Onvumere, Margarita K. et al.

In: Frontiers in Bioscience - Landmark, Vol. 29, No. 5, 05.2024.

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Tolmacheva AS, Sedykh SE, Onvumere MK, Timofeeva AM, Maksimenko LV, Gashnikova NM et al. Catalase Activity of IgG and κκ-IgG, λλ-IgG, and κλ-IgG Subfractions in HIV-Infected Patients and Healthy Donors. Frontiers in Bioscience - Landmark. 2024 May;29(5). doi: 10.31083/j.fbl2905191

Author

Tolmacheva, Anna S. ; Sedykh, Sergey E. ; Onvumere, Margarita K. et al. / Catalase Activity of IgG and κκ-IgG, λλ-IgG, and κλ-IgG Subfractions in HIV-Infected Patients and Healthy Donors. In: Frontiers in Bioscience - Landmark. 2024 ; Vol. 29, No. 5.

BibTeX

@article{2048c265f55c4fb8963c8fa8d8ffaf4b,
title = "Catalase Activity of IgG and κκ-IgG, λλ-IgG, and κλ-IgG Subfractions in HIV-Infected Patients and Healthy Donors",
abstract = "Background: Human immunodeficiency virus (HIV) infection is associated with pronounced oxidative stress, leading to the development of various virus-associated pathologies. A wealth of evidence suggests that, along with canonical enzymes of reactive oxygen species regulation, human blood contains antibodies with peroxidase, superoxide dismutase, and catalase activities. Here we show that the catalase activity of IgGs and their κκ-IgG, λλ-IgG, and κλ-IgG subfractions of HIV-infected individuals is significantly different compared to the healthy donors. Methods: Protein G-Sepharose sorbent was used to resolve IgG from blood of healthy donors and HIV-infected patients by affinity chromatography. Subfractions of κκ-IgG, λλ-IgG, and κλ-IgG were separated from IgGs samples of each group by affinity chromatography on sorbents containing immobilized antibodies to κ or λ light human chains. The IgG catalase activity level was measured spectrophotometrically by evaluating the decrease in optical density (A240) due to hydrogen peroxide decomposition. Results: The relative catalase activity of antibodies from HIV-infected patients (kcat = (1.41 ± 0.92) × 103 min−1, 95% CI: [1.01–1.81]) was statistically significant, 1.6 times higher (p = 0.014) compared to apparently healthy donors ((0.86 ± 0.49) × 103, 95% CI: [0.69–1.03]). The activity level of κκ-IgG HIV-infected patients ((0.44 ± 0.04) × 103 min−1) was 1.4 times higher than that of λλ-IgGs ((0.31 ± 0.025) × 103 min−1), the opposite was observed for κκ-IgGs from apparently healthy donors, which activity ((0.17 ± 0.015) × 103 min−1) was 3.1 times lower compared to λλ-IgGs ((0.53 ± 0.045) × 103 min−1). Conclusions: Thus, the data obtained may indicate that IgG with increased catalase activity may prevent harmful processes arising from oxidative stress in HIV-infected patients, acting as an additional natural molecular mechanism of regulation of hydrogen peroxide level.",
keywords = "HIV, IgG, antibodies, autoimmunity, catalase activity, catalytic antibodies, oxidative stress",
author = "Tolmacheva, {Anna S.} and Sedykh, {Sergey E.} and Onvumere, {Margarita K.} and Timofeeva, {Anna M.} and Maksimenko, {Lada V.} and Gashnikova, {Natalya M.} and Nevinsky, {Georgy A.}",
note = "22-15-00103/ Russian Science Foundation 121031300041-4/ Russian State funded budget project of ICBFM SB RAS",
year = "2024",
month = may,
doi = "10.31083/j.fbl2905191",
language = "русский",
volume = "29",
journal = "Frontiers in Bioscience - Landmark",
issn = "2768-6701",
publisher = "Frontiers in Bioscience",
number = "5",

}

RIS

TY - JOUR

T1 - Catalase Activity of IgG and κκ-IgG, λλ-IgG, and κλ-IgG Subfractions in HIV-Infected Patients and Healthy Donors

AU - Tolmacheva, Anna S.

AU - Sedykh, Sergey E.

AU - Onvumere, Margarita K.

AU - Timofeeva, Anna M.

AU - Maksimenko, Lada V.

AU - Gashnikova, Natalya M.

AU - Nevinsky, Georgy A.

N1 - 22-15-00103/ Russian Science Foundation 121031300041-4/ Russian State funded budget project of ICBFM SB RAS

PY - 2024/5

Y1 - 2024/5

N2 - Background: Human immunodeficiency virus (HIV) infection is associated with pronounced oxidative stress, leading to the development of various virus-associated pathologies. A wealth of evidence suggests that, along with canonical enzymes of reactive oxygen species regulation, human blood contains antibodies with peroxidase, superoxide dismutase, and catalase activities. Here we show that the catalase activity of IgGs and their κκ-IgG, λλ-IgG, and κλ-IgG subfractions of HIV-infected individuals is significantly different compared to the healthy donors. Methods: Protein G-Sepharose sorbent was used to resolve IgG from blood of healthy donors and HIV-infected patients by affinity chromatography. Subfractions of κκ-IgG, λλ-IgG, and κλ-IgG were separated from IgGs samples of each group by affinity chromatography on sorbents containing immobilized antibodies to κ or λ light human chains. The IgG catalase activity level was measured spectrophotometrically by evaluating the decrease in optical density (A240) due to hydrogen peroxide decomposition. Results: The relative catalase activity of antibodies from HIV-infected patients (kcat = (1.41 ± 0.92) × 103 min−1, 95% CI: [1.01–1.81]) was statistically significant, 1.6 times higher (p = 0.014) compared to apparently healthy donors ((0.86 ± 0.49) × 103, 95% CI: [0.69–1.03]). The activity level of κκ-IgG HIV-infected patients ((0.44 ± 0.04) × 103 min−1) was 1.4 times higher than that of λλ-IgGs ((0.31 ± 0.025) × 103 min−1), the opposite was observed for κκ-IgGs from apparently healthy donors, which activity ((0.17 ± 0.015) × 103 min−1) was 3.1 times lower compared to λλ-IgGs ((0.53 ± 0.045) × 103 min−1). Conclusions: Thus, the data obtained may indicate that IgG with increased catalase activity may prevent harmful processes arising from oxidative stress in HIV-infected patients, acting as an additional natural molecular mechanism of regulation of hydrogen peroxide level.

AB - Background: Human immunodeficiency virus (HIV) infection is associated with pronounced oxidative stress, leading to the development of various virus-associated pathologies. A wealth of evidence suggests that, along with canonical enzymes of reactive oxygen species regulation, human blood contains antibodies with peroxidase, superoxide dismutase, and catalase activities. Here we show that the catalase activity of IgGs and their κκ-IgG, λλ-IgG, and κλ-IgG subfractions of HIV-infected individuals is significantly different compared to the healthy donors. Methods: Protein G-Sepharose sorbent was used to resolve IgG from blood of healthy donors and HIV-infected patients by affinity chromatography. Subfractions of κκ-IgG, λλ-IgG, and κλ-IgG were separated from IgGs samples of each group by affinity chromatography on sorbents containing immobilized antibodies to κ or λ light human chains. The IgG catalase activity level was measured spectrophotometrically by evaluating the decrease in optical density (A240) due to hydrogen peroxide decomposition. Results: The relative catalase activity of antibodies from HIV-infected patients (kcat = (1.41 ± 0.92) × 103 min−1, 95% CI: [1.01–1.81]) was statistically significant, 1.6 times higher (p = 0.014) compared to apparently healthy donors ((0.86 ± 0.49) × 103, 95% CI: [0.69–1.03]). The activity level of κκ-IgG HIV-infected patients ((0.44 ± 0.04) × 103 min−1) was 1.4 times higher than that of λλ-IgGs ((0.31 ± 0.025) × 103 min−1), the opposite was observed for κκ-IgGs from apparently healthy donors, which activity ((0.17 ± 0.015) × 103 min−1) was 3.1 times lower compared to λλ-IgGs ((0.53 ± 0.045) × 103 min−1). Conclusions: Thus, the data obtained may indicate that IgG with increased catalase activity may prevent harmful processes arising from oxidative stress in HIV-infected patients, acting as an additional natural molecular mechanism of regulation of hydrogen peroxide level.

KW - HIV

KW - IgG

KW - antibodies

KW - autoimmunity

KW - catalase activity

KW - catalytic antibodies

KW - oxidative stress

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85194391363&origin=inward&txGid=58cc2a3ba93976ab4bb4578f60981dd5

UR - https://www.mendeley.com/catalogue/6b6834f1-6de1-37ea-b7ba-45b8ee9c9668/

U2 - 10.31083/j.fbl2905191

DO - 10.31083/j.fbl2905191

M3 - статья

C2 - 38812328

VL - 29

JO - Frontiers in Bioscience - Landmark

JF - Frontiers in Bioscience - Landmark

SN - 2768-6701

IS - 5

ER -

ID: 61042662