Proteomics

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Aspirin reshapes acetylomes in inflammatory and cancer cells via CoA-dependent and –independent pathways


ABSTRACT: We used a deuterium-labeled aspirin (D-aspirin) together with mass spectrometry-based acetylomic analysis, termed “DAcMS”, to investigate the landscape of protein acetylation induced by aspirin. And we further demonstrated that aspirin acetylates proteins through both acetyl-CoA-dependent and -independent pathways, and the accessible lysine residues at the protein surface are major acetylation targets of aspirin.

ORGANISM(S): Homo Sapiens Mus Musculus

SUBMITTER: Yaoyang Zhang  

PROVIDER: PXD017220 | iProX | Tue Jan 21 00:00:00 GMT 2020

REPOSITORIES: iProX

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Aspirin Reshapes Acetylomes in Inflammatory and Cancer Cells via CoA-Dependent and CoA-Independent Pathways.

Guo Lin L   Gao Jing J   Gao Yang Y   Zhu Zhengjiang Z   Zhang Yaoyang Y  

Journal of proteome research 20200124 2


Aspirin, or acetylsalicylic acid (ASA), is the most widely used medication to relieve pain, fever, and inflammation. Recent studies have revealed new benefits of aspirin, including reduction of heart attack and stroke, anticancer, and life extension. Despite the profound effects of aspirin, the mechanism of its action remains to be elucidated. Here, we used deuterium-labeled aspirin (D-aspirin) together with mass spectrometry-based acetylomic analysis, termed DAcMS, to investigate the landscape  ...[more]

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