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Gel LC-MS/MS analyses of MMP cleavage of tryptophanyl-tRNA synthetase

ABSTRACT: Tryptophanyl-tRNA synthetase was incubated by MMPs, cleavage products were resolved on SDS-PAGE. Cleavage products were trypsin digested and analyzed by LC-MS/MS.

INSTRUMENT(S): impact II

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Parker Jobin

LAB HEAD: Christopher Mark Overall

PROVIDER: PXD013217 | Pride | 2019-05-29

REPOSITORIES: Pride

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Matrix metalloproteinases inactivate the proinflammatory functions of secreted moonlighting tryptophanyl-tRNA synthetase.

Jobin Parker G PG Solis Nestor N Machado Yoan Y Bell Peter A PA Kwon Nam Hoon NH Kim Sunghoon S Overall Christopher M CM Butler Georgina S GS

The Journal of biological chemistry 20190719 35

Tryptophanyl-tRNA synthetase (WRS) is a cytosolic aminoacyl-tRNA synthetase essential for protein synthesis. WRS is also one of a growing number of intracellular proteins that are attributed distinct noncanonical "moonlighting" functions in the extracellular milieu. Moonlighting aminoacyl-tRNA synthetases regulate processes such as inflammation, but how these multifunctional enzymes are themselves regulated remains unclear. Here, we demonstrate that WRS is secreted from human macrophages, fibrob ...[more]

PMID: 31324718

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2008-06-15 | E-GEOD-7957 | biostudies-arrayexpress

Expression data from Pseudomonas aeruginosa exposed airway epithelium from C57Bl6 and MMP-7 and MMP-10 deficient mice.

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