New ProteomeXchange dataset PXD062929

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Dear ProteomeXchange subscriber, a new ProteomeXchange dataset is being announced. To see more information, click here:

https://proteomecentral.proteomexchange.org/dataset/PXD062929

Summary of dataset

Status: new
Identifier: PXD062929
HostingRepository: MassIVE
Species: Homo sapiens, Mus musculus
Title: High-throughput chemical proteomics workflow for profiling protein citrullination dynamics
Submitter: Rebecca Meelker Gonzalez
LabHead: Dr. Chien-Yun Lee
Description: Citrullination is a post-translational modification implicated in autoimmune and inflammatory diseases but remains challenging to analyze biochemically. Its low stoichiometry and the lack of enrichment tools have hindered its global and site-specific profiling. Here, we developed a high-throughput chemical proteomics workflow for citrullination profiling with enhanced sensitivity and specificity. This workflow employs glyoxal-based derivatization of citrullinated peptides, followed by a click reaction with a biotin conjugate, featuring a cleavable linker that enhances peptide recovery and following identification. We examined the derivatization efficiency using synthetic citrullinated peptides and demonstrated its sensitivity and reproducibility in complex biological samples. Mouse brain digest samples were then used for direct comparison to existent enrichment tools. Dose-dependent ionomycin treatments of isolated neutrophils from fresh blood allowed us to profile citru
llination during neutrophil extracellular trap (NET) formation. Known and novel sites on different histone proteins, as well as structural proteins mediating nuclear and cytoskeletal reorganization, were found to be regulated. These findings illuminate citrullination dynamics in NET formation and establish a platform for exploring its roles in diverse systems.

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