Nitration is a posttranslational modification of tyrosine residues of proteins mediated by peroxynitrite (ONOO(-)). It commonly occurs in neurological and pathological disorders, which involve nitric oxide (NO)-mediated oxidative stress. Nitration of tyrosine or tyrosyl groups of a protein modulates protein function and initiates signal transduction pathways, which lead to alternation of cellular metabolism and functions. Because of its apparent significance, there is an increasing urge to identify nitrated proteins as a bridge to expand our understanding of their involvement in different biological processes. This chapter describes strategies that could be used for rapid screening and detection of nitrated proteins, subsequent resolution, and identification of nitrated proteins and peptides using proteomic technologies. These include two-dimensional gel electrophoresis coupled with Western blotting and matrix-assisted laser desorption/ionization time of flight mass spectrometry, as well as liquid chromatography-linked tandem mass spectrometry.
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http://dx.doi.org/10.1016/S0076-6879(07)00802-6 | DOI Listing |
Alzheimers Dement
December 2024
Glenn Biggs Institute for Alzheimer's & Neurodegenerative Diseases, University of Texas Health Sciences Center at San Antonio, San Antonio, TX, USA.
Background: Lewy bodies (LBs), characterized by intraneuronal inclusions of misfolded alpha-synuclein (α-syn) protein, are the pathological hallmark of Parkinson's disease (PD) and dementia with Lewy bodies (DLB). Because this protein is phosphorylated at serine-129 in 90% of LBs, its phosphorylation is considered a crucial pathogenic event in LB formation and disease development. Here, we present a unique brain autopsy case of a DLB patient with widespread LBs that were negative for phosphorylated-α-syn, challenging traditional diagnostic criteria.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science & Technology, Wuhan, 430074, PR China. Electronic address:
The amyloid aggregation of hIAPP and the increased level of oxidative stress are closely related to the occurrence and development of type 2 diabetes (T2D). Protein tyrosine nitration is a common post-translational modification under oxidative stress conditions. We previously found that tyrosine nitrated hIAPP (3-NT-hIAPP) has higher cytotoxicity than wild type hIAPP.
View Article and Find Full Text PDFFree Radic Biol Med
December 2024
Dept. of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark. Electronic address:
Acta Neuropathol
December 2024
Paul Flechsig Institute - Centre of Neuropathology and Brain Research, University of Leipzig, Liebigstraße 19, 04103, Leipzig, Germany.
Cell Commun Signal
December 2024
Department of Biophysics, National Institute of Mental Health and Neurosciences, Institute of National Importance, Bengaluru, Karnataka, 560029, India.
Background: A key factor in the propagation of α-synuclein pathology is the compromised protein quality control system. Variations in membrane association and astrocytic uptake between different α-synuclein forms suggest differences in exocytosis or membrane cleavage, potentially impacting the secretome's influence on dopaminergic neurons. We aimed to understand differences in protein degradation mechanisms of astrocytes for both wild-type (WT) and mutant forms of α-synuclein, specifically during periods of reduced degradation efficiency.
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