The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Measuring Myeloperoxidase Activity in Biological Samples
Open accessAbstract
BACKGROUND: Enzymatic activity measurements of the highly oxidative enzyme myeloperoxidase (MPO), which is implicated in many diseases, are widely used in the literature, but often suffer from nonspecificity and lack of uniformity. Thus, validation and standardization are needed to establish a robust method that is highly specific, sensitive, and reproducible for assaying MPO activity in biological samples. PRINCIPAL FINDINGS: We found conflicting results between in vivo molecular MR imaging of MPO, which measures extracellular activity, and commonly used in vitro MPO activity assays. Thus, we established and validated a protocol to obtain extra- and intracellular MPO from murine organs. To validate the MPO activity assays, three different classes of MPO activity assays were used in spike and recovery experiments. However, these assay methods yielded inconsistent results, likely because of interfering substances and other peroxidases present in tissue extracts. To circumvent this, we first captured MPO with an antibody. The MPO activity of the resultant samples was assessed by ADHP and validated against samples from MPO-knockout mice in murine disease models of multiple sclerosis, steatohepatitis, and myocardial infarction. We found the measurements performed using this protocol to be highly specific and reproducible, and when performed using ADHP, to be highly sensitive over a broad range. In addition, we found that intracellular MPO activity correlated well with tissue neutrophil content, and can be used as a marker to assess neutrophil infiltration in the tissue. CONCLUSION: We validated a highly specific and sensitive assay protocol that should be used as the standard method for all MPO activity assays in biological samples. We also established a method to obtain extra- and intracellular MPO from murine organs. Extracellular MPO activity gives an estimate of the oxidative stress in inflammatory diseases, while intracellular MPO activity correlates well with tissue neutrophil content. A detailed step-by-step protocol is provided.
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Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Identification of splenic reservoir monocytes and their deployment to inflammatory sites
Swirski, F. K., Nahrendorf, M., Etzrodt, M., Wildgruber, M., Cortez-Retamozo, V., Panizzi, P., Figueiredo, J.-L., Kohler, R. H., Chudnovskiy, A., Waterman, P., et al. (2009) · Science · doi:10.1126/science.1175202 · Cited by 2,221
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Prognostic Value of Myeloperoxidase in Patients with Chest Pain
Brennan, M.-L., Penn, M. S., Van Lente, F., Nambi, V., Shishehbor, M. H., Aviles, R. J., Goormastic, M., Pepoy, M. L., McErlean, E. S., Topol, E. J., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa035003 · Cited by 1,070
Association Between Myeloperoxidase Levels and Risk of Coronary Artery Disease
Zhang, R. (2001) · JAMA · doi:10.1001/jama.286.17.2136 · Cited by 918
Assay method for myeloperoxidase in human polymorphonuclear leukocytes
Suzuki, K., Ota, H., Sasagawa, S., Sakatani, T., & Fujikura, T. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90019-2 · Cited by 899
Metzler, K. D., Fuchs, T. A., Nauseef, W. M., Reumaux, D., Roesler, J., Schulze, I., Wahn, V., Papayannopoulos, V., & Zychlinsky, A. (2011) · Blood · doi:10.1182/blood-2010-06-290171 · Cited by 774
Cellular and extracellular myeloperoxidase in pyogenic inflammation
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Cited by
Zhou, Y., Li, P., Goodwin, A. J., Cook, J. A., Halushka, P. V., Chang, E., Zingarelli, B., & Fan, H. (2019) · Critical Care · doi:10.1186/s13054-019-2339-3 · Cited by 293
Pulli, B., Ali, M., Iwamoto, Y., Zeller, M. W. G., Schob, S., Linnoila, J. J., & Chen, J. W. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2014.6108 · Cited by 143
Self-citationHaskamp, S., Bruns, H., Hahn, M., Hoffmann, M., Gregor, A., Löhr, S., Hahn, J., Schauer, C., Ringer, M., Flamann, C., et al. (2020) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2020.07.001 · Cited by 84
Ceuleers, H., Hanning, N., Heirbaut, J., Van Remoortel, S., Joossens, J., Van Der Veken, P., Francque, S. M., De bruyn, M., Lambeir, A., De Man, J. G., et al. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14396 · Cited by 49
Mello, B. S. F., Chaves Filho, A. J. M., Custódio, C. S., Cordeiro, R. C., Miyajima, F., de Sousa, F. C. F., Vasconcelos, S. M. M., de Lucena, D. F., & Macedo, D. (2018) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2018.04.009 · Cited by 45
Metadata
- Authors
- Pulli, B., Ali, M., Forghani, R., Schob, S., Hsieh, K. L. C., Wojtkiewicz, G., Linnoila, J. J., & Chen, J. W.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-07-05
- Volume
- 8
- Issue
- 7
- Pages
- e67976
- ISSN
- 1932-6203 (ISSN-L)
- OpenAlex
- W2101116633
- Cited by
- 381
- References
- 46
- FWCI
- 9.60
- Type
- journal article
- Language
- en
- Open access
- gold
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