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Biochemical Aspects of Nickel Hypersensitivity: Factors Determining Allergenic Action
Published in Jurij J. Hostýnek, Howard I. Maibach, Nickel and the Skin, 2019
Baldassarré Santucci, Emanuela Camera, Mauro Picardo
Nickel is the 24th most abundant element in the earth’s crust. Its whole-body load is comparable to that of trace elements such as manganese, cobalt, and molybdenum, which are involved in enzymatic or coenzymatic activities (IARC, 1984; Mracussen, 1960). In humans, nickel’s essential status remains to be established (Nielsen and Sandstead, 1974). The presence of the ion in several important catalyst enzymes such as urease, methylcoenzyme M reductase, hydrogenase, and carbon monoxide dehydrogenase seems to suggest that trace levels of the metal are necessary for several biological processes (Hausinger, 1992; Thauer, 2001).
Boron, Manganese, Molybdenum, Nickel, Silicon and Vanadium
Published in Judy A. Driskell, Ira Wolinsky, Sports Nutrition, 2005
Nickel is essential for some lower forms of life where it participates in hydrolysis and redox reactions, regulates gene expression and stabilizes certain structures. In these roles, nickel forms ligands with sulfur, nitrogen and oxygen, and exists in oxidation states 3+, 2+ and 1+. In lower forms of life, nickel has been identified as an essential component of six different enzymes: urease, hydrogenase, carbon monoxide dehydrogenase, methyl-coenzyme M reductase, Ni-superoxide dismutase and glyoxalase I.108 Interestingly, the substrates or products for all these enzymes are dissolved gases: hydrogen, carbon monoxide, carbon dioxide, methane, oxygen and ammonia.
Breathomics and its Application for Disease Diagnosis: A Review of Analytical Techniques and Approaches
Published in Raquel Cumeras, Xavier Correig, Volatile organic compound analysis in biomedical diagnosis applications, 2018
David J. Beale, Oliver A. H. Jones, Avinash V. Karpe, Ding Y. Oh, Iain R. White, Konstantinos A. Kouremenos, Enzo A. Palombo
Owing to the complexity of the VOCs expelled through breath, breathomics-based research can inform on the different stages of infection (i.e., early-to-intermediate), allowing more time for diagnosis and treatment of infections. For example, there has been recent progress in the detection of infectious diseases with higher social impacts such as tuberculosis, especially in developing countries. Maiga et al. (2014) utilized the conversion of isotopic 13CO to 13CO2 by the pathogen Mycobacterium bovis in rabbit populations. The testing indicated that detection of CO2 generated through the activity of mycobacterial carbon monoxide dehydrogenase (CODH) had the potential to provide rapid and non-invasive diagnosis of tuberculosis (Maiga et al. 2014). While this study demonstrated the preclinical breath analysis of Mycobacterium bovis in rabbit populations, if developed further it could enable for cheaper and faster point-of-care diagnosis of tuberculosis within a clinical setting, which would augment and improve current pathology tests. Zhu et al. (2013b) extended breath single biomarker analysis further and used the entire ‘breathprint’ to diagnose acute Pseudomonas aeruginosa and Staphylococcus aureus lung infections in a mouse model. Such an approach that uses the entire ‘breathprint’ rather than single biomarkers enables volatile metabolites to be characterized and monitored during the course of infection, and potentially identify a suite of breath biomarkers that can be used in the diagnoses of pathogens at any point during the infection (Bean et al., 2015; Zhu et al., 2013a, 2013b).
Bile acid oxidation by Eggerthella lenta strains C592 and DSM 2243T
Published in Gut Microbes, 2018
Spencer C. Harris, Saravanan Devendran, Celia Méndez- García, Sean M. Mythen, Chris L. Wright, Christopher J. Fields, Alvaro G. Hernandez, Isaac Cann, Phillip B. Hylemon, Jason M. Ridlon
Prior surveys of the gut of wood-feeding cockroaches40 and acidic fen41 resulted in identification of Eggerthella as encoding a formyl-tetrahydrofolate synthase (fhs) gene, suggesting that Eggerthella may have acetogenic potential. Common to all acetogens are genes encoding acetyl-CoA synthase (ACS)/carbon monoxide dehydrogenase (CODH).42,43 We located a conserved cluster of genes (Elen_3026-3030; CAB18_RS02000-2010) in both E. lenta DSM 2243 and E. lenta C592 which encode 4Fe-4S hybrid cluster proteins which include ACS and CODH. Eggerthella sp. strain YY7918 was found to harbor a different gene cluster, annotated as encoding acsA (EGGYY_24090), ascB/cdhC (EGYY_24100), acsF (BAK45480) providing further genomic evidence that Eggerthella isolates encode WLP genes.