Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin

Sokolov, A. V.; Ageeva, K. V.; Cherkalina, Olga S.; Pulina, M. O.; Захарова, Е. М.; Prozorovskii, V. N.; Aksenov, D. V.; Vasilyev, V. B.; Панасенко, О. М.

doi:10.1016/j.chemphyslip.2010.02.002

Cited by 49 publications

(43 citation statements)

References 34 publications

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“…of 30 Ϯ 3% (n ϭ 12). These results are in accord with previous studies in which ceruloplasmin was found to inhibit accumulation of taurine chloramine by 40 -60% (24,36). When urate (100 M) was added to the reaction system to ensure that the enzyme could cycle via Compound II (37,38), the inhibitory effect of ceruloplasmin increased to 56 Ϯ 10% (n ϭ 3).…”

Section: Table 1 Identification Of Ceruloplasminsupporting

confidence: 81%

“…Previously, interactions between myeloperoxidase and lipoproteins in vitro and in plasma have been demonstrated (52)(53)(54). Compared with ceruloplasmin, these other proteins are likely to form minor associations with myeloperoxidase, as suggested recently (36).…”

Section: Discussionmentioning

confidence: 99%

“…Initially we used an assay that has previously been used to test whether ceruloplasmin inhibits the chlorination activity of myeloperoxidase (24,36). In this assay, myeloperoxidase and chloride are incubated with taurine, and the concentration of accumulated taurine chloramine formed is determined when about half of the added hydrogen peroxide has been consumed.…”

Section: Table 1 Identification Of Ceruloplasminmentioning

confidence: 99%

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Ceruloplasmin Is an Endogenous Inhibitor of Myeloperoxidase

Chapman

Mocatta

Shiva

et al. 2013

Journal of Biological Chemistry

120

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Background: Myeloperoxidase promotes oxidative stress during inflammation by producing hypochlorous acid. Results: Ceruloplasmin was a potent inhibitor of myeloperoxidase and slowed its activity in plasma from wild type mice compared with ceruloplasmin knock-out animals. Conclusion: Ceruloplasmin is a physiologically relevant inhibitor of myeloperoxidase. Significance: Ceruloplasmin will provide a protective shield against oxidant production by myeloperoxidase during inflammation.

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Section: Table 1 Identification Of Ceruloplasminsupporting

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Section: Table 1 Identification Of Ceruloplasminmentioning

confidence: 99%

See 1 more Smart Citation

Ceruloplasmin Is an Endogenous Inhibitor of Myeloperoxidase

Chapman

Mocatta

Shiva

et al. 2013

Journal of Biological Chemistry

120

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“…An increased level of Cl-Tyr, apparently a consequence of high plasma MPO levels ( 50,51 ), was also reported in plasma samples from dialysis patients ( 38,39 ). This observation prompted us to follow PTMs on apoB-100 isolated from plasma of hemodialysis patients who have high plasma MPO-LDL levels ( 25 ) interaction between LDL and MPO that differs from MPO interaction with high-density lipoprotein ( 34 ). An increase in the activity of MPO at the surface of LDL might indicate that native LDL enhances its own oxidation by MPO and that MPO activity could be underestimated in vitro and/or in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…MPO interacts preferentially with the protein moiety of native LDL ( 23,34 ). It is likely that the enzyme may interact in a similar manner with modifi ed LDL; we therefore studied whether this interaction is paralleled by changes in the activity of MPO.…”

Section: Activity and Structure Of Mpo At The Surface Of Ldlmentioning

confidence: 99%

Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100

Delporte

Boudjeltia

Noyon

et al. 2014

Journal of Lipid Research

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Over the past several years, considerable evidence has been obtained in support of the hypothesis that oxidants generated by the heme enzyme myeloperoxidase (MPO, EC1.11.2.2) play a key role in oxidation reaction of the artery wall. The enzyme, abundantly present in neutrophils and, to a lesser extent, in monocytes, is released during infl ammatory activation of immune cells. MPO produces hypochlorous acid (HOCl) by the reaction of hydrogen Abstract Oxidation of LDL by the myeloperoxidase (MPO)-H 2 O 2 -chloride system is a key event in the development of atherosclerosis. The present study aimed at investigating the interaction of MPO with native and modifi ed LDL and at revealing posttranslational modifi cations on apoB-100 (the unique apolipoprotein of LDL) in vitro and in vivo. Using amperometry, we demonstrate that MPO activity increases up to 90% when it is adsorbed at the surface of LDL. This phenomenon is apparently refl ected by local structural changes in MPO observed by circular dichroism. Using MS, we further analyzed in vitro modifi cations of apoB-100 by hypochlorous acid (HOCl) generated by the MPO-H 2 O 2 -chloride system or added as a reagent. A total of 97 peptides containing modifi ed residues could be identifi ed. Furthermore, differences were observed between LDL oxidized by reagent HOCl or HOCl generated by the MPO-H 2 O 2 -chloride system. Finally, LDL was isolated from patients with high cardiovascular risk to confi rm that our in vitro fi ndings are also relevant in vivo. We show that several HOCl-mediated modifi cations of apoB-100 identifi ed in vitro were also present on LDL isolated from patients who have increased levels of plasma MPO and MPO-modifi ed LDL. In conclusion, these data emphasize the specifi city of MPO to oxidize LDL. -Delporte,

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Altered Composition

2011

High‐Density Lipoproteins

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Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin

Cited by 49 publications

References 34 publications

Ceruloplasmin Is an Endogenous Inhibitor of Myeloperoxidase

Ceruloplasmin Is an Endogenous Inhibitor of Myeloperoxidase

Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100

Altered Composition

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