Quantitative Protein Sulfenic Acid Analysis Identifies Platelet Releasate-Induced Activation of Integrin β2 on Monocytes via NADPH Oxidase

• DOI: 10.1021/acs.jproteome.6b00212
• Publication Date: 2016-10-03T13:40:14Z
• Authors: Ru Li; Cordula Klockenbusch; Liwen Lin; Honghui Jiang; Shujun Lin; Juergen Kast
• Keywords: Sulfenic acid

Physiological stimuli such as thrombin, or pathological lysophosphatidic acid (LPA), activate platelets. The activated platelets bind to monocytes through P-selectin-PSGL-1 interactions but also release the contents of their granules, commonly called "platelet releasate". It is known that in contact with platelet releasate produce reactive oxygen species (ROS). Reversible cysteine oxidation by ROS considered be a potential regulator protein function. In previous study, we used THP-1 monocytic cells exposed LPA- thrombin-induced and modified biotin switch assay unravel biological processes are influenced reversible oxidation. To gain better understanding redox regulation atherosclerosis, have now altered selectively quantify sulfenic acid, subpopulation Using arsenite reducing agent assay, were able 1161 proteins, which more than 100 sites identified. Bioinformatics analysis quantified highlighted relevant, previously missed process monocyte transendothelial migration, included integrin β2. Flow cytometry validated activation LFA-1 (αLβ2) Mac-1 (αMβ2), two subfamilies β2 complexes, on human primary following treatment. was mediated from NADPH oxidase (NOX) activation. Production independent interaction. Our results proved powerful tool ability reveal new regulatory mechanisms identify therapeutic targets.