Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: Reciprocal effect on enzymatic properties

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Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: Reciprocal effect on enzymatic properties. / Sokolov, A.V.; Kostevich, V.A.; Zakharova, E.T.; Samygina, V.R.; Panasenko, O.M.; Vasilyev, V.B.

In: Free Radical Research, Vol. 49, No. 6, 2015, p. 800-811.

Research output: Contribution to journal › Article

BibTeX

@article{64a8b73db7da4baab7c3fe924b993107,

title = "Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: Reciprocal effect on enzymatic properties",

abstract = "Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) are involved in the development of halogenative stress during inflammation. We previously described a complex between MPO and ceruloplasmin (CP). Considering the high structural homology between MPO and EPO, we studied the latter's interaction with CP and checked whether EPO becomes inhibited in a complex with CP. Disc-electrophoresis and gel filtration showed that CP and EPO form a complex with the stoichiometry 1:1. Affinity chromatography of EPO on CP-agarose (150 mM NaCl, 10 mM Na-phosphate buffer, of pH 7.4) resulted in retention of EPO. EPO protects ceruloplasmin from limited proteolysis by plasmin. Only intact CP shifted the Soret band typical of EPO from 413 to 408 nm. The contact with CP likely causes changes in the heme pocket of EPO. Peroxidase activity of EPO with substrates such as guaiacol, orcinol, o-dianisidine, 4-chloro-1-naphtol, 3,3',5,5'-tetramethylbenzidine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) is inhibited by CP in a",

keywords = "ceruloplasmin, eosinophil peroxidase, halogenating activity, myeloperoxidase, protein–protein interaction",

author = "A.V. Sokolov and V.A. Kostevich and E.T. Zakharova and V.R. Samygina and O.M. Panasenko and V.B. Vasilyev",

year = "2015",

doi = "10.3109/10715762.2015.1005615",

language = "English",

volume = "49",

pages = "800--811",

journal = "Free Radical Research",

issn = "1071-5762",

publisher = "Informa Healthcare",

number = "6",

}

RIS

TY - JOUR

T1 - Interaction of ceruloplasmin with eosinophil peroxidase as compared to its interplay with myeloperoxidase: Reciprocal effect on enzymatic properties

AU - Sokolov, A.V.

AU - Kostevich, V.A.

AU - Zakharova, E.T.

AU - Samygina, V.R.

AU - Panasenko, O.M.

AU - Vasilyev, V.B.

PY - 2015

Y1 - 2015

N2 - Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) are involved in the development of halogenative stress during inflammation. We previously described a complex between MPO and ceruloplasmin (CP). Considering the high structural homology between MPO and EPO, we studied the latter's interaction with CP and checked whether EPO becomes inhibited in a complex with CP. Disc-electrophoresis and gel filtration showed that CP and EPO form a complex with the stoichiometry 1:1. Affinity chromatography of EPO on CP-agarose (150 mM NaCl, 10 mM Na-phosphate buffer, of pH 7.4) resulted in retention of EPO. EPO protects ceruloplasmin from limited proteolysis by plasmin. Only intact CP shifted the Soret band typical of EPO from 413 to 408 nm. The contact with CP likely causes changes in the heme pocket of EPO. Peroxidase activity of EPO with substrates such as guaiacol, orcinol, o-dianisidine, 4-chloro-1-naphtol, 3,3',5,5'-tetramethylbenzidine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) is inhibited by CP in a

AB - Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) are involved in the development of halogenative stress during inflammation. We previously described a complex between MPO and ceruloplasmin (CP). Considering the high structural homology between MPO and EPO, we studied the latter's interaction with CP and checked whether EPO becomes inhibited in a complex with CP. Disc-electrophoresis and gel filtration showed that CP and EPO form a complex with the stoichiometry 1:1. Affinity chromatography of EPO on CP-agarose (150 mM NaCl, 10 mM Na-phosphate buffer, of pH 7.4) resulted in retention of EPO. EPO protects ceruloplasmin from limited proteolysis by plasmin. Only intact CP shifted the Soret band typical of EPO from 413 to 408 nm. The contact with CP likely causes changes in the heme pocket of EPO. Peroxidase activity of EPO with substrates such as guaiacol, orcinol, o-dianisidine, 4-chloro-1-naphtol, 3,3',5,5'-tetramethylbenzidine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate) is inhibited by CP in a

KW - ceruloplasmin

KW - eosinophil peroxidase

KW - halogenating activity

KW - myeloperoxidase

KW - protein–protein interaction

U2 - 10.3109/10715762.2015.1005615

DO - 10.3109/10715762.2015.1005615

M3 - Article

VL - 49

SP - 800

EP - 811

JO - Free Radical Research

JF - Free Radical Research

SN - 1071-5762

IS - 6

ER -

ID: 3937744