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Chen, Y.* ; Liu, Y.* ; Lan, T.H.* ; Qin, W.* ; Zhu, Y.* ; Qin, K.* ; Gao, J.* ; Wang, H.* ; Hou, X.* ; Chen, N.* ; Friedmann Angeli, J.P.F. ; Conrad, M. ; Wang, C.*

Quantitative profiling of protein carbonylations in ferroptosis by an aniline-derived probe.

J. Am. Chem. Soc. 140, 4712-4720 (2018)
Verlagsversion Forschungsdaten DOI
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Ferroptosis is a regulated form of necrotic cell death implicated in carcinogenesis and neurodegeneration that is driven by phospholipid peroxidation. Lipid-derived electrophiles (LDEs) generated during this process can covalently modify proteins ("carbonylation") and affect their functions. Here we report the development of a quantitative chemoproteomic method to profile carbonylations in ferroptosis by an aniline-derived probe. Using the method, we established a global portrait of protein carbonylations in ferroptosis with >400 endogenously modified proteins and for the first time, identified >20 residue sites with endogenous LDE modifications in ferroptotic cells. Specifically, we discovered and validated a novel cysteine site of modification on voltage-dependent anion-selective channel protein 2 (VDAC2) that might play an important role in sensitizing LDE signals and mediating ferroptosis. Our results will contribute to the understanding of ferroptotic signaling and pathogenesis and provide potential biomarkers for ferroptosis detection.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
ISSN (print) / ISBN 0002-7863
e-ISSN 1520-5126
Quellenangaben Band: 140, Heft: 13, Seiten: 4712-4720 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Begutachtungsstatus Peer reviewed