Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase

Sakamaki, Kazuhiro; Tomonaga, Masanori; Tsukui, Kazuo; Nagata, Shinji

doi:10.1016/s0021-9258(19)84781-6

Cited by 86 publications

(6 citation statements)

References 40 publications

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“…This enzyme is located in eosinophils and is considered mainly responsible for generating hypobromous acid to assist in microbial killing. Eosinophil peroxidase shares approximately 70% amino acid sequence homology with MPO [ 14 ].…”

Section: Myeloperoxidase – a Historical Timeline To The Presentmentioning

confidence: 99%

The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery

Siraki

2021

Redox Biology

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This review provides a practical guide to myeloperoxidase (MPO) and presents to the reader the diversity of its presence in biology. The review provides a historical background, from peroxidase activity to the discovery of MPO, to its role in disease and drug development. MPO is discussed in terms of its necessity, as specific individuals lack MPO expression. An underlying theme presented throughout brings up the question of the benefit and burden of MPO activity. Enzyme structure is discussed, including accurate masses and glycosylation sites. The catalytic cycle of MPO and its corresponding pathways are presented, with a discussion of the importance of the redox couples of the different states of MPO. Cell lines expressing MPO are discussed and practically summarized for the reader, and locations of MPO (primary and secondary) are provided. Useful methods of MPO detection are discussed, and how these can be used for studying disease processes are implied through the presentation of MPO as a biomarker. The presence of MPO in neutrophil extracellular traps is presented, and the activators of the former are provided. Lastly, the transition from drug metabolism to a target for drug development is where the review concludes.

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Section: Myeloperoxidase – a Historical Timeline To The Presentmentioning

confidence: 99%

The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery

Siraki

2021

Redox Biology

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“…Thereby, hypohalous acids are formed (HOX). Alternatively, com-EPO and MPO share 61% identical amino acid residues (20), and an even higher homology can be found among the active site related residues. Together with lactoperoxidase and thyroid peroxidase, EPO and MPO are members of the mammalian peroxidase superfamily.…”

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confidence: 99%

Spectral and Kinetic Studies on the Formation of Eosinophil Peroxidase Compound I and Its Reaction with Halides and Thiocyanate^†

et al. 2000

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Compound I of peroxidases takes part in both the peroxidation and the halogenation reaction. This study for the first time presents transient kinetic measurements of the formation of compound I of human eosinophil peroxidase (EPO) and its reaction with halides and thiocyanate, using the sequential-mixing stopped-flow technique. Addition of 1 equiv of hydrogen peroxide to native EPO leads to complete formation of compound I. At pH 7 and 15 degrees C, the apparent second-order rate constant is (4.3 +/- 0.4) x 10(7) M(-1) s(-1). The rate for compound I formation by hypochlorous acid is (5.6 +/- 0.7) x 10(7) M(-1) s(-1). EPO compound I is unstable and decays to a stable intermediate with a compound II-like spectrum. At pH 7, the two-electron reduction of compound I to the native enzyme by thiocyanate has a second-order rate constant of (1.0 +/- 0. 5) x 10(8) M(-1) s(-1). Iodide [(9.3 +/- 0.7) x 10(7) M(-1) s(-1)] is shown to be a better electron donor than bromide [(1.9 +/- 0.1) x 10(7) M(-1) s(-1)], whereas chloride oxidation by EPO compound I is extremely slow [(3.1 +/- 0.3) x 10(3) M(-1) s(-1)]. The pH dependence studies suggest that a protonated form of compound I is more competent in oxidizing the anions. The results are discussed in comparison with those of the homologous peroxidases myeloperoxidase and lactoperoxidase and with respect to the role of EPO in host defense and tissue injury.

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“…The homologous mammalian peroxidase family comprises myeloperoxidase (MPO), lactoperoxidase (LPO), eosinophil peroxidase (EPO), and thyroid peroxidase (TPO). MPO shares respectively 61, 70, and 47% identical residues with these peroxidases, − and an even higher homology can be found among the active site related residues. MPO differs significantly from other peroxidases in its unusual spectral features , and its unique ability to catalyze the oxidation of chloride by hydrogen peroxide to form the potent oxidant and bactericidal agent hypochlorous acid .…”

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confidence: 99%

Difference Fourier Transform Infrared Evidence for Ester Bonds Linking the Heme Group in Myeloperoxidase, Lactoperoxidase, and Eosinophil Peroxidase

et al. 1997

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Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase

Cited by 86 publications

References 40 publications

The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery

The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery

Spectral and Kinetic Studies on the Formation of Eosinophil Peroxidase Compound I and Its Reaction with Halides and Thiocyanate^†

Difference Fourier Transform Infrared Evidence for Ester Bonds Linking the Heme Group in Myeloperoxidase, Lactoperoxidase, and Eosinophil Peroxidase

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Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase

Cited by 86 publications

References 40 publications

The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery

The many roles of myeloperoxidase: From inflammation and immunity to biomarkers, drug metabolism and drug discovery

Spectral and Kinetic Studies on the Formation of Eosinophil Peroxidase Compound I and Its Reaction with Halides and Thiocyanate†

Difference Fourier Transform Infrared Evidence for Ester Bonds Linking the Heme Group in Myeloperoxidase, Lactoperoxidase, and Eosinophil Peroxidase

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Spectral and Kinetic Studies on the Formation of Eosinophil Peroxidase Compound I and Its Reaction with Halides and Thiocyanate^†