Protein tyrosine nitration in a proteome has sensitive biological effects. Many reactive oxygen/nitrogen species (ROS, RNS) generated in human tissues and cells in different pathophysiological conditions mutually act in an ordered chemical reaction system, and exert their roles in the entire process of a disease from preclinical to clinical phases, and from occurrence, development, diagnosis, therapy to prognosis of a disease. Among them, superoxide and nitric oxide react quickly to generate peroxynitrate that is an in vivo main nitrating reagent to induce the nitration of tyrosine residue in a protein. Protein tyrosine nitration results in the shift of the phenolic pKa value from ~10 for tyrosine to the physiological pH range ~7.1 for nitrotyrosine. The nitro group as an electron-withdrawing group causes the decrease of the electrondensity of the phenolic ring of a tyrosine residue in a protein. Thus, if protein nitration occurs within the interacting region between an enzyme-substrate, receptor-ligand, antigen-antibody, or dimerization region, the decreased electron-density could diminish the interaction intensity (enzyme-substrate, receptor-ligand, antigen-antibody, or dimerization) to affect the functions of that protein. Protein tyrosine nitration also competes the same tyrosine residue site with phosphorylation within a tyrosine kinase phosphorylation motif to affect the signal transduction. Moreover, the discovery of putative denitrase in a cell or tissue demonstrates that biological protein tyrosine nitration could be a specific, dynamic, and reversible process between nitration and denitration. Therefore, protein tyrosine nitration in a biological system has extensively biological functions, which is not only a pathological consequence and a stable biomarker of oxidative/nitrative injuries to detect onset, progression, and therapeutic efficacy of a disease, but also alters protein functions to involve multiple biological processes such as redox signaling and neurotransmission, and associate multiple pathophysiological processes such as tumorigenesis, inflammation-related diseases, aging and aging-related diseases, neurodegenerative disease, cardiovascular disease, kidney disease, and diabetes. Clarification of protein tyrosine nitration benefits insights into novel pathological mechanisms of a disease and discovery of effective biomarker and therapeutic target, which provides numerous promising and potential in the field of medicine. This special issue is collecting research articles and review articles to discuss this very interesting topic regarding potential of protein tyrosine nitration in medicine.
Professor Xianquan ZhanGuest Editor
two dimensional gel electrophoresis
Submission Deadline: 30 October 2018
Manuscripts should be submitted online through ScholarOne Manuscripts for Med One © Clarivate Analytics. Please visit Guide for Authors before submitting a manuscript. Authors are encouraged to submit a paper as soon as it is ready and don’t need to wait until the deadline. Submissions will be sent to peer-review in order of arrival. Accepted papers will be published continuously in Med One and then gathered together on the special issue webpage. We welcome Research articles, Review papers and Short Communications. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
1. Pradip Mascharak
Distinguished Professor of Chemistry and Biochemistry University of California, Santa Cruz, CA, USA
2. Dimitrios Tsikas
Hannover Medical School, Germany
3. Matyas Mink
University of Szeged, Szeged, Hungary
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Key Laboratory of Cancer Proteomics of Chinese Ministry of Health, Xiangya Hospital, Central South University