Oxidative Post-translational Modifications Accelerate Proteolytic Degradation of Calprotectin.

ABSTRACT: Oxidative post-translational modifications affect the structure and function of many biomolecules. Herein we examine the biophysical and functional consequences of oxidative post-translational modifications to human calprotectin (CP, S100A8/S100A9 oligomer, MRP8/MRP14 oligomer, calgranulins A/B oligomer). This abundant metal-sequestering protein contributes to innate immunity by starving invading microbial pathogens of transition metal nutrients in the extracellular space. It also participates in the inflammatory response. Despite many decades of study, little is known about the fate of CP at sites of infection and inflammation. We present compelling evidence for methionine oxidation of CP in vivo, supported by using ¹⁵N-labeled CP-Ser (S100A8(C42S)/S100A9(C3S)) to monitor for a

SUBMITTER: Stephan JR 

PROVIDER: S-EPMC6534964 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature