A methionine/aspartate-rich synthetic peptide delineated from N-terminal region of nucleophosmin protein effectively protects against cadmium-induced toxicity

• Published in: Environment international Vol. 199; p. 109443
• Main Authors: Yan, Rui, Tan, Heng Wee, Zhao, Xiao-Yun, Wu, Jia-Yi, Zhong, Qiu-Hua, Wang, Xiu-Yun, Cai, Na-Li, Xu, Yan-Ming, Lau, Andy T.Y.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 01.05.2025; Elsevier
• Subjects: affinity chromatography; Animals; Anti-Cd; apoptosis; Apoptosis - drug effects; Aspartic Acid; blood; cadmium; Cadmium - toxicity; Cd toxicity; Cd-IMAC; cytotoxicity; environment; environmental health; heavy metals; Humans; inflammation; liver; Methionine; Mice; NPM1; Nuclear Proteins - chemistry; Nuclear Proteins - metabolism; Nucleolar stress; Nucleophosmin; Peptides; synthetic peptides; Cd-IMAC; Nucleolar stress; Anti-Cd; NPM1; Cd toxicity

[Display omitted] •NPM1 is a novel Cd-binding protein.•Cd binds to the M/D-rich region (MEDSMDMDM) of NPM1 and triggers nucleolar stress.•Cd induces nucleoplasmic translocation of NPM1 and inhibits rRNA biogenesis.•Synthetic M/D-rich peptide mitigates Cd toxicity in cells and at animal levels. Cadmi...