Measurements for sulfide-mediated inhibition of myeloperoxidase activity

1Citations
Citations of this article
10Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Oxidative stress-alleviating and inflammation-mediatory functions of hydrogen sulfide were reported to be key features of its biological actions. However, the underlying molecular mechanisms of these biological observations are not fully understood. In conditions where sulfide was proposed to be protective against oxidative stress- or inflammation-induced tissue damage (e.g., reperfusion injury, atherosclerosis, vascular inflammation), the reactive oxidant-producing function of a key neutrophil enzyme, myeloperoxidase, was reported to be a protagonist on the detrimental side. We recently described favorable interactions between sulfide and myeloperoxidase and proposed that the potent inhibition of myeloperoxidase activities could contribute to sulfide’s beneficial functions in a number of cardiovascular pathologies. Our chapter is dedicated to aid future studies and drug development endeavors in this area by providing methodological guidance on how to assess the inhibitory potential of sulfide on myeloperoxidase enzymatic activities in isolated protein systems, in neutrophil homogenates, and in live neutrophil preparations.

Cite

CITATION STYLE

APA

Garai, D., Pálinkás, Z., Balla, J., Kettle, A. J., & Nagy, P. (2019). Measurements for sulfide-mediated inhibition of myeloperoxidase activity. In Methods in Molecular Biology (Vol. 2007, pp. 179–203). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9528-8_14

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free