Effect of Collection Tube Type and Preanalytical Handling on Myeloperoxidase Concentrations

Shih, Jessie; Datwyler, Saul A.; Hsu, Stephen; Matias, Matthew S.; Pacenti, David P.; Lueders, Christian; Mueller, Christian; Danne, O.; Möckel, Martin

doi:10.1373/clinchem.2007.101568

Cited by 65 publications

(56 citation statements)

References 13 publications

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“…was similar for citrate and EDTA and more pronounced for heparin. These results are in agreement with previous studies showing higher total MPO contents in heparin plasma and serum than in citrate and EDTA plasma [28,29]. The SIEFED method allows reliable quantification of MPO activity from 0.156 to 10 mU/mL, what corresponds to 0.78-50 ng/mL pure MPO.…”

Section: Discussionsupporting

confidence: 92%

A new easy method for specific measurement of active myeloperoxidase in human biological fluids and tissue extracts

Franck

Kohnen

Boudjeltia³

et al. 2009

Talanta

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a b s t r a c tThe SIEFED ("Specific Immunological Extraction Followed by Enzymatic Detection") method already developed for the specific detection of the activity of equine myeloperoxidase (MPO) was adapted for the specific measurement of active human MPO in biological fluids or tissue extracts. The method consists of the extraction of MPO from aqueous solutions by immobilized anti-MPO antibodies followed by a washing (to eliminate the extraction medium and the biological fluid with their possible interfering molecules) and the measurement of the activity of MPO with a detection system containing a fluorogenic substrate, H 2 O 2 and nitrite ions as reaction enhancer. The SIEFED was applied to study active MPO in human biological fluids (plasma, bronchoalveolar lavage fluid and supernatant from carotids extracts). The SIEFED for human MPO has a sensitivity limit of 0.080 mU/mL and showed good precision with intra-and inter-assay coefficients of variation below 10 and 20% respectively within a broad range of MPO activities establish from 0.156 to 473 mU/mL. The SIEFED for human MPO will be useful for the specific detection of active MPO in complex fluids and can be complementary to an ELISA to determine an active/total MPO ratio in healthy volunteers and patients especially in case of chronic or acute inflammatory diseases.

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Section: Discussionsupporting

confidence: 92%

A new easy method for specific measurement of active myeloperoxidase in human biological fluids and tissue extracts

Franck

Kohnen

Boudjeltia³

et al. 2009

Talanta

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“…Overall, our findings for a heterogeneous group of patients who presented to an inner-city hospital with symptoms of ischemia suggest that MPO is a powerful predictor of cardiovascular risk, as has previously been shown in moderate-to highrisk ACS patients (4 -6 ). This study used EDTA plasma samples, in which MPO concentrations have been shown to be stable (13,14 ). Earlier studies that found higher MPO concentrations used serum or heparinized plasma samples, and the assays may have been prone to preanalytical stability problems caused by inadequate samplecollection procedures that led to inaccurate biomarker results.…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have shown that heparin increases the plasma MPO concentration when used in vivo or in vitro, whereas MPO concentrations appear to be stable in EDTAcontaining plasma (13,14 ).…”

confidence: 99%

Myeloperoxidase Improves Risk Stratification in Patients with Ischemia and Normal Cardiac Troponin I Concentrations

Apple¹,

Smith

Pearce

et al. 2011

Clinical Chemistry

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“…For example, the plasma concentration of MPO increases with time if human whole blood is kept at room temperature prior to plasma preparation, collection, and storage [120]. In addition, several studies have reported heparin plasma to contain more MPO protein than EDTA plasma [120][121][122][123], possibly due to ex vivo 'release' of MPO from blood cells/matrix by heparin [124]. This interpretation is supported by the observation that intravenous administration of heparin mobilizes MPO from vascular compartments, yielding higher values compared to baseline plasma concentrations, especially in patients with CAD [125].…”

Section: Detection Of Mpo Proteinmentioning

confidence: 99%

The roles of myeloperoxidase in coronary artery disease and its potential implication in plaque rupture

et al. 2016

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Atherosclerosis is the main pathophysiological process underlying coronary artery disease (CAD). Acute complications of atherosclerosis, such as myocardial infarction, are caused by the rupture of vulnerable atherosclerotic plaques, which are characterized by thin, highly inflamed, and collagen-poor fibrous caps. Several lines of evidence mechanistically link the heme peroxidase myeloperoxidase (MPO), inflammation as well as acute and chronic manifestations of atherosclerosis. MPO and MPO-derived oxidants have been shown to contribute to the formation of foam cells, endothelial dysfunction and apoptosis, the activation of latent matrix metalloproteinases, and the expression of tissue factor that can promote the development of vulnerable plaque. As such, detection, quantification and imaging of MPO mass and activity have become useful in cardiac risk stratification, both for disease assessment and in the identification of patients at risk of plaque rupture. This review summarizes the current knowledge about the role of MPO in CAD with a focus on its possible roles in plaque rupture and recent advances to quantify and image MPO in plasma and atherosclerotic plaques.

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Effect of Collection Tube Type and Preanalytical Handling on Myeloperoxidase Concentrations

Cited by 65 publications

References 13 publications

A new easy method for specific measurement of active myeloperoxidase in human biological fluids and tissue extracts

A new easy method for specific measurement of active myeloperoxidase in human biological fluids and tissue extracts

Myeloperoxidase Improves Risk Stratification in Patients with Ischemia and Normal Cardiac Troponin I Concentrations

The roles of myeloperoxidase in coronary artery disease and its potential implication in plaque rupture

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