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Proatherogenic modification of LDL by surface-bound myeloperoxidase. / Sokolov, A.V.; Kostevich, V.A.; Runova, O.L.; Gorudko, I.V.; Vasilyev, V.B.; Cherenkevich, S.N.; Panasenko, O.M.

In: Chemistry and Physics of Lipids, Vol. 180, 2014, p. 72-80.

Research output: Contribution to journal › Article

Harvard

Sokolov, AV, Kostevich, VA, Runova, OL, Gorudko, IV, Vasilyev, VB, Cherenkevich, SN & Panasenko, OM 2014, 'Proatherogenic modification of LDL by surface-bound myeloperoxidase.', Chemistry and Physics of Lipids, vol. 180, pp. 72-80. https://doi.org/10.1016/j.chemphyslip.2014.02.006

APA

Sokolov, A. V., Kostevich, V. A., Runova, O. L., Gorudko, I. V., Vasilyev, V. B., Cherenkevich, S. N., & Panasenko, O. M. (2014). Proatherogenic modification of LDL by surface-bound myeloperoxidase. Chemistry and Physics of Lipids, 180, 72-80. https://doi.org/10.1016/j.chemphyslip.2014.02.006

Vancouver

Sokolov AV, Kostevich VA, Runova OL, Gorudko IV, Vasilyev VB, Cherenkevich SN et al. Proatherogenic modification of LDL by surface-bound myeloperoxidase. Chemistry and Physics of Lipids. 2014;180:72-80. https://doi.org/10.1016/j.chemphyslip.2014.02.006

Author

Sokolov, A.V. ; Kostevich, V.A. ; Runova, O.L. ; Gorudko, I.V. ; Vasilyev, V.B. ; Cherenkevich, S.N. ; Panasenko, O.M. / Proatherogenic modification of LDL by surface-bound myeloperoxidase. In: Chemistry and Physics of Lipids. 2014 ; Vol. 180. pp. 72-80.

BibTeX

@article{00da6e00498f4ff89d8cad959f271e55,
title = "Proatherogenic modification of LDL by surface-bound myeloperoxidase.",
abstract = "One of the factors promoting oxidative/halogenating modification of low-density lipoproteins (LDL) is myeloperoxidase (MPO). We have shown previously that MPO binds to the LDL surfaces. The LDL-MPO complex is uncoupled in the presence of peptide EQIQDDCTGDED that corresponds to a fragment of apoB-100 (445-456). In this paper we studied how this peptide, as well as inhibitors and modulators of halogenating activity of MPO such as ceruloplasmin (CP), 4-aminobenzoic acid hydrazide (ABAH) and thiocyanate (SCN(-)) affect the accumulation of cholesterol and its esters in monocytes/macrophages after incubation with LDL subjected to different kinds of MPO-dependent oxidative/halogenating modification. In the presence of H2O2 and halides MPO causes stronger proatherogenic modification of LDL than exogenous reactive halogen species (HOCl and HOBr). Both monocytes, which differentiate into macrophages, and neutrophils secrete MPO in response to the presence of damaged LDL. The peptide EQIQDDCTGDED preventing interaction",
keywords = "Atherosclerosis, Cholesterol accumulation, Low density lipoproteins, Myeloperoxidase, Oxidative/halogenative stress, Reactive halogen species",
author = "A.V. Sokolov and V.A. Kostevich and O.L. Runova and I.V. Gorudko and V.B. Vasilyev and S.N. Cherenkevich and O.M. Panasenko",
year = "2014",
doi = "10.1016/j.chemphyslip.2014.02.006",
language = "English",
volume = "180",
pages = "72--80",
journal = "Chemistry and Physics of Lipids",
issn = "0009-3084",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Proatherogenic modification of LDL by surface-bound myeloperoxidase.

AU - Sokolov, A.V.

AU - Kostevich, V.A.

AU - Runova, O.L.

AU - Gorudko, I.V.

AU - Vasilyev, V.B.

AU - Cherenkevich, S.N.

AU - Panasenko, O.M.

PY - 2014

Y1 - 2014

N2 - One of the factors promoting oxidative/halogenating modification of low-density lipoproteins (LDL) is myeloperoxidase (MPO). We have shown previously that MPO binds to the LDL surfaces. The LDL-MPO complex is uncoupled in the presence of peptide EQIQDDCTGDED that corresponds to a fragment of apoB-100 (445-456). In this paper we studied how this peptide, as well as inhibitors and modulators of halogenating activity of MPO such as ceruloplasmin (CP), 4-aminobenzoic acid hydrazide (ABAH) and thiocyanate (SCN(-)) affect the accumulation of cholesterol and its esters in monocytes/macrophages after incubation with LDL subjected to different kinds of MPO-dependent oxidative/halogenating modification. In the presence of H2O2 and halides MPO causes stronger proatherogenic modification of LDL than exogenous reactive halogen species (HOCl and HOBr). Both monocytes, which differentiate into macrophages, and neutrophils secrete MPO in response to the presence of damaged LDL. The peptide EQIQDDCTGDED preventing interaction

AB - One of the factors promoting oxidative/halogenating modification of low-density lipoproteins (LDL) is myeloperoxidase (MPO). We have shown previously that MPO binds to the LDL surfaces. The LDL-MPO complex is uncoupled in the presence of peptide EQIQDDCTGDED that corresponds to a fragment of apoB-100 (445-456). In this paper we studied how this peptide, as well as inhibitors and modulators of halogenating activity of MPO such as ceruloplasmin (CP), 4-aminobenzoic acid hydrazide (ABAH) and thiocyanate (SCN(-)) affect the accumulation of cholesterol and its esters in monocytes/macrophages after incubation with LDL subjected to different kinds of MPO-dependent oxidative/halogenating modification. In the presence of H2O2 and halides MPO causes stronger proatherogenic modification of LDL than exogenous reactive halogen species (HOCl and HOBr). Both monocytes, which differentiate into macrophages, and neutrophils secrete MPO in response to the presence of damaged LDL. The peptide EQIQDDCTGDED preventing interaction

KW - Atherosclerosis

KW - Cholesterol accumulation

KW - Low density lipoproteins

KW - Myeloperoxidase

KW - Oxidative/halogenative stress

KW - Reactive halogen species

U2 - 10.1016/j.chemphyslip.2014.02.006

DO - 10.1016/j.chemphyslip.2014.02.006

M3 - Article

VL - 180

SP - 72

EP - 80

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

SN - 0009-3084

ER -

ID: 5779157