Profiling of lysine-acetylated proteins in human urine.
A biomarker is a measurable indicator associated with changes in physiological state or disease. In contrast to the blood which is under homeostatic controls, urine reflects changes in the body earlier and more sensitively, and is therefore a better biomarker source. Lysine acetylation is an abundant and highly regulated post-translational modification. It plays a pivotal role in modulating diverse biological processes and is associated with various important diseases. Enrichment or visualization of proteins with specific post-translational modifications provides a method for sampling the urinary proteome and reducing sample complexity. In this study, we used anti-acetyllysine antibody-based immunoaffinity enrichment combined with high-resolution mass spectrometry to profile lysine-acetylated proteins in normal human urine. A total of 629 acetylation sites on 315 proteins were identified, including some very low-abundance proteins. This is the first proteome-wide characterization of lysine acetylation proteins in normal human urine. Our dataset provides a useful resource for the further discovery of lysine-acetylated proteins as biomarkers in urine.
['Qin|Weiwei|W|', 'Wang|Ting|T|', 'Huang|He|H|', 'Gao|Youhe|Y|']
D000107:Acetylation D000328:Adult D000595:Amino Acid Sequence D002851:Chromatography, High Pressure Liquid D005260:Female D006801:Humans D008239:Lysine D008297:Male D011485:Protein Binding D011499:Protein Processing, Post-Translational D020543:Proteome D040901:Proteomics D053719:Tandem Mass Spectrometry D059349:Urine Specimen Collection
urine lysine acetylation post-translational modification