-
Clinical Chemistry and Laboratory... Jul 2023Detection of hemoglobin (Hb) and red blood cells in urine (hematuria) is characterized by a large number of pitfalls. Clinicians and laboratory specialists must be... (Review)
Review
Detection of hemoglobin (Hb) and red blood cells in urine (hematuria) is characterized by a large number of pitfalls. Clinicians and laboratory specialists must be aware of these pitfalls since they often lead to medical overconsumption or incorrect diagnosis. Pre-analytical issues (use of vacuum tubes or urine tubes containing preservatives) can affect test results. In routine clinical laboratories, hematuria can be assayed using either chemical (test strips) or particle-counting techniques. In cases of doubtful results, Munchausen syndrome or adulteration of the urine specimen should be excluded. Pigmenturia (caused by the presence of dyes, urinary metabolites such as porphyrins and homogentisic acid, and certain drugs in the urine) can be easily confused with hematuria. The peroxidase activity (test strip) can be positively affected by the presence of non-Hb peroxidases (e.g. myoglobin, semen peroxidases, bacterial, and vegetable peroxidases). Urinary pH, haptoglobin concentration, and urine osmolality may affect specific peroxidase activity. The implementation of expert systems may be helpful in detecting preanalytical and analytical errors in the assessment of hematuria. Correcting for dilution using osmolality, density, or conductivity may be useful for heavily concentrated or diluted urine samples.
Topics: Humans; Hematuria; Peroxidase; Hemoglobins; Erythrocytes; Osmolar Concentration
PubMed: 37079906
DOI: 10.1515/cclm-2023-0260 -
Handbook of Experimental Pharmacology 2021Myeloperoxidase participates in innate immune defense mechanism through formation of microbicidal reactive oxidants and diffusible radical species. A unique activity is...
Myeloperoxidase participates in innate immune defense mechanism through formation of microbicidal reactive oxidants and diffusible radical species. A unique activity is its ability to use chloride as a cosubstrate with hydrogen peroxide to generate chlorinating oxidants such as hypochlorous acid, a potent antimicrobial agent. However, chronic MPO activation can lead to indiscriminate protein modification causing tissue damage, and has been associated with chronic inflammatory diseases, atherosclerosis, and acute cardiovascular events. This has attracted considerable interest in the development of therapeutically useful MPO inhibitors. Today, based on the profound knowledge of structure and function of MPO and its biochemical and biophysical differences with the other homologous human peroxidases, various rational and high-throughput screening attempts were performed in developing specific irreversible and reversible inhibitors. The most prominent candidates as well as MPO inhibitors already studied in clinical trials are introduced and discussed.
Topics: Humans; Hydrogen Peroxide; Oxidation-Reduction; Peroxidase
PubMed: 33372235
DOI: 10.1007/164_2020_388 -
ACS Nano Jul 2023Nanozymes constitute an emerging class of nanomaterials with enzyme-like characteristics. Over the past 15 years, more than 1200 nanozymes have been developed, and they... (Review)
Review
Nanozymes constitute an emerging class of nanomaterials with enzyme-like characteristics. Over the past 15 years, more than 1200 nanozymes have been developed, and they have demonstrated promising potentials in broad applications. With the diversification and complexity of its applications, traditional empirical and trial-and-error design strategies no longer meet the requirements for efficient nanozyme design. Thanks to the rapid development of computational chemistry and artificial intelligence technologies, first-principles methods and machine-learning algorithms are gradually being adopted as a more efficient and easier means to assist nanozyme design. This review focuses on the potential elementary reaction mechanisms in the rational design of nanozymes, including peroxidase (POD)-, oxidase (OXD)-, catalase (CAT)-, superoxide dismutase (SOD)-, and hydrolase (HYL)-like nanozymes. The activity descriptors are introduced, with the aim of providing further guidelines for nanozyme active material screening. The computing- and data-driven approaches are thoroughly reviewed to give a proposal on how to proceed with the next-generation paradigm rational design. At the end of this review, personal perspectives on the prospects and challenges of the rational design of nanozymes are put forward, hoping to promote the further development of nanozymes toward superior application performance in the future.
Topics: Artificial Intelligence; Catalysis; Nanostructures; Peroxidase; Peroxidases
PubMed: 37399457
DOI: 10.1021/acsnano.3c04378 -
Free Radical Biology & Medicine Mar 2022Heme-containing peroxidases catalyze the oxidation of a variety of substrates by consuming hydrogen peroxide (HO), and play diversified roles in physiology and pathology... (Review)
Review
Heme-containing peroxidases catalyze the oxidation of a variety of substrates by consuming hydrogen peroxide (HO), and play diversified roles in physiology and pathology including innate immunity, the synthesis of thyroid hormone and the extracellular matrix, as well as the pathogenesis of several inflammatory diseases. Peroxidasin (PXDN), also known as Vascular Peroxidase-1 (VPO1), is a newly identified peroxidase and expresses in multiple cells and tissues including cardiovascular system and the lung. Recent studies imply its roles in the innate immunity, cardiovascular physiology and diseases, and extracellular matrix formation. Studies on the role of PXDN in human diseases are entering a new and exciting stage, and this review provides the insights into this emerging field of PXDN.
Topics: Animals; Deoxyribonucleosides; Extracellular Matrix Proteins; Humans; Hydrogen Peroxide; Mammals; Peroxidase; Peroxidases; Purine Nucleosides; Peroxidasin
PubMed: 35219848
DOI: 10.1016/j.freeradbiomed.2022.02.026 -
Nanoscale Aug 2023In recent years, nanozymes have attracted enormous attention due to their effectiveness in promoting various catalytic reactions. To date, thousands of nanozymes have... (Review)
Review
In recent years, nanozymes have attracted enormous attention due to their effectiveness in promoting various catalytic reactions. To date, thousands of nanozymes have been discovered, including oxidase-like nanozymes, peroxidase-like nanozymes, and catalase-like nanozymes, covering noble metal, transition metal, and carbon nanomaterials. These nanozymes have been widely applied in various fields, including environmental protection, biosensing and nanomedicine. There are many reviews about this rising star being used in analytical chemistry. However, few works about nanozymes were related to cancer therapy. In this study, we comprehensively summarize the latest research advances on the strategies for cancer therapy based on different nanozymes. With traditional cancer treatment (including chemotherapy, radiotherapy, phototherapy), nanozyme catalytic therapy exhibited a synergistic effect for limiting the growth of tumors. Opportunities and trends for nanozymes in future cancer therapy are also discussed.
Topics: Nanostructures; Peroxidase; Peroxidases; Catalysis; Carbon; Neoplasms
PubMed: 37462391
DOI: 10.1039/d3nr01976d -
The Science of the Total Environment Feb 2022The fast-growing consumer demand drives industrial process intensification, which subsequently creates a significant amount of waste. These products are discharged into... (Review)
Review
The fast-growing consumer demand drives industrial process intensification, which subsequently creates a significant amount of waste. These products are discharged into the environment and can affect the quality of air, degrade water streams, and alter soil characteristics. Waste materials may contain polluting agents that are especially harmful to human health and the ecosystem, such as the synthetic dyes, phenolic agents, polycyclic aromatic hydrocarbons, volatile organic compounds, polychlorinated biphenyls, pesticides and drug substances. Peroxidases are a class oxidoreductases capable of performing a wide variety of oxidation reactions, ranging from reactions driven by radical mechanisms, to oxygen insertion into CH bonds, and two-electron substrate oxidation. This versatility in the mode of action presents peroxidases as an interesting alternative in cleaning the environment. Herein, an effort has been made to describe mechanisms governing biochemical process of peroxidase enzymes while referring to HO/substrate stoichiometry and metabolite products. Plant peroxidases including horseradish peroxidase (HRP), soybean peroxidase (SBP), turnip and bitter gourd peroxidases have revealed notable biocatalytic potentialities in the degradation of toxic products. On the other hand, an introduction on the role played by ligninolytic enzymes such as manganese peroxidase (MnP) and lignin peroxidase (LiP) in the valorization of lignocellulosic materials is addressed. Moreover, sensitivity and selectivity of peroxidase-based biosensors found use in the quantitation of constituents and the development of diagnostic kits. The general merits of peroxidases and some key prospective applications have been outlined as concluding remarks.
Topics: Biodegradation, Environmental; Coloring Agents; Ecosystem; Humans; Hydrogen Peroxide; Lignin; Peroxidase; Peroxidases
PubMed: 34852426
DOI: 10.1016/j.scitotenv.2021.150500 -
Biomolecules Jul 2021Nanomaterial-mediated cancer therapeutics is a fast developing field and has been utilized in potential clinical applications. However, most effective therapies, such as... (Review)
Review
Nanomaterial-mediated cancer therapeutics is a fast developing field and has been utilized in potential clinical applications. However, most effective therapies, such as photodynamic therapy (PDT) and radio therapy (RT), are strongly oxygen-dependent, which hinders their practical applications. Later on, several strategies were developed to overcome tumor hypoxia, such as oxygen carrier nanomaterials and oxygen generated nanomaterials. Among these, oxygen species generation on nanozymes, especially catalase (CAT) mimetic nanozymes, convert endogenous hydrogen peroxide (HO) to oxygen (O) and peroxidase (POD) mimetic nanozymes converts endogenous HO to water (HO) and reactive oxygen species (ROS) in a hypoxic tumor microenvironment is a fascinating approach. The present review provides a detailed examination of past, present and future perspectives of POD mimetic nanozymes for effective oxygen-dependent cancer phototherapeutics.
Topics: Animals; Biomimetic Materials; Humans; Nanostructures; Neoplasms; Oxygen; Peroxidase; Photochemotherapy; Tumor Hypoxia; Tumor Microenvironment
PubMed: 34356639
DOI: 10.3390/biom11071015 -
Applied Microbiology and Biotechnology May 2021Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate... (Review)
Review
Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate spectrum accompanied by the only need for molecular oxygen as cosubstrate and production of hydrogen peroxide as sole by-product makes these enzymes very promising biocatalysts. AAOs were used in the synthesis of flavors, fragrances, and other high-value-added compounds and building blocks as well as in dye decolorization and pulp biobleaching. Furthermore, AAOs offer a huge potential as efficient suppliers of hydrogen peroxide for peroxidase- and peroxygenase-catalyzed reactions. A prerequisite for application as biocatalysts at larger scale is the production of AAOs in sufficient amounts. Heterologous expression of these predominantly fungal enzymes is, however, quite challenging. This review summarizes different approaches aiming at enhancing heterologous expression of AAOs and gives an update on substrates accepted by these promising enzymes as well as potential fields of their application. KEY POINTS: • Aryl-alcohol oxidases (AAOs) supply ligninolytic peroxidases with HO. • AAOs accept a broad spectrum of aromatic and aliphatic allylic alcohols. • AAOs are potential biocatalysts for the production of high-value-added bio-based chemicals.
Topics: Alcohol Oxidoreductases; Alcohols; Fungi; Hydrogen Peroxide; Lignin; Peroxidase; Peroxidases
PubMed: 33997930
DOI: 10.1007/s00253-021-11337-4 -
Journal of the American Chemical Society Jun 2023DNAzymes have been limited in application by their low catalytic rates. Here, we evolved a new peroxidase DNAzyme mSBDZ-X-3 through a directed evolution method based on...
DNAzymes have been limited in application by their low catalytic rates. Here, we evolved a new peroxidase DNAzyme mSBDZ-X-3 through a directed evolution method based on the capture of self-biotinylated DNA catalyzed by its intrinsic peroxidase activity. The mSBDX-X-3 DNAzyme has a parallel G-quadruplex structure and has more favorable catalytic properties than all previously reported peroxidase DNAzyme variants. We applied mSBDZ-X-3 in an aptamer-coupled proximity-based labeling proteomic assay to determine the proteins that bind to cell surface cancer biomarkers EpCAM and nucleolin. Confocal microscopy, western blot analysis, and LC-MS/MS showed that the hybrid DNAzyme aptamer-coupled proximity assay-labeled proteins associated with EpCAM and nucleolin within 6-12 min in fixed cancer cells. The labeled proteins were identified by mass spectrometry. This study provides a highly efficient peroxidase DNAzyme, a methodology for selection of such variants, and a method for its application in spatial proteomics using entirely nucleic acid-based tooling.
Topics: DNA, Catalytic; Peroxidase; Epithelial Cell Adhesion Molecule; Chromatography, Liquid; Proteomics; Tandem Mass Spectrometry; Peroxidases; Coloring Agents; Aptamers, Nucleotide; G-Quadruplexes; Hemin; Biosensing Techniques
PubMed: 37276197
DOI: 10.1021/jacs.3c02625 -
Zeitschrift Fur Naturforschung. C,... Jul 2022Point of care testing (PoCT) devices permit precise and rapid detection of disease-related biomarkers contributing to an early disease diagnosis and administration of an...
Point of care testing (PoCT) devices permit precise and rapid detection of disease-related biomarkers contributing to an early disease diagnosis and administration of an appropriate treatment. The enzyme myeloperoxidase (MPO) is a relevant biomarker for infection and inflammation events assessment; however its direct electrochemical quantification is hindered by the limited accessibility to the iron atom in its active center. Herein, such hindrance of the MPO biomolecule is overcome using the redox mediator 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS). The charge involved in the electrochemical reduction of the MPO-oxidized ABTS is correlated with the concentration of MPO. The use of ABTS allowed for the electrochemical assessment of a wide range of MPO concentrations (10-1000 nM) including those reported for wound infections, chronic obstructive pulmonary disease and early adverse cardiac events. The developed electroanalytical approach is rapid and inexpensive, and thus suitable for implementation in PoCT devices.
Topics: Biomarkers; Coloring Agents; Oxidation-Reduction; Peroxidase
PubMed: 35191282
DOI: 10.1515/znc-2021-0274