Proteomics

Dataset Information

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Sites of aspirin-mediated lysine acetylation in HeLa cells


ABSTRACT: Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. Important to this function is its ability to irreversibly acetylate cyclooxygenases at active site serines. Aspirin has the potential to acetylate other amino-acid side-chains, leading to speculation that aspirin-mediated lysine acetylation could explain some of its drug actions or side-effects. Using a labeled form of aspirin, aspirin-d3, we identified over 12000 sites of lysine acetylation from cultured human cells. Although aspirin amplifies acetylation signals at thousands of sites, cells tolerate aspirin mediated acetylation very well unless endogenous deacetylases are inhibited. Apart from a limited number of cellular proteins that are substantially acetylated under endogenous conditions, aspirin mediated acetylation leads to a large increase in the acetylation of many proteins even although they remain at very low stoichiometry. This reinforces the idea that a major function of cellular deacetylases is the suppression of non-specific or non-enzymatic protein acetylation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Mike Tatham  

LAB HEAD: Ronald Thomas Hay

PROVIDER: PXD003530 | Pride | 2017-01-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20120227_MT_01.raw Raw
20120227_MT_02.raw Raw
20120227_MT_03.raw Raw
20120301_MT_Asp_D0.raw Raw
20120301_MT_Asp_D0_8ul.raw Raw
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Publications

A Proteomic Approach to Analyze the Aspirin-mediated Lysine Acetylome.

Tatham Michael H MH   Cole Christian C   Scullion Paul P   Wilkie Ross R   Westwood Nicholas J NJ   Stark Lesley A LA   Hay Ronald T RT  

Molecular & cellular proteomics : MCP 20161202 2


Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. Important to this function is its ability to irreversibly acetylate cyclooxygenases at active site serines. Aspirin has the potential to acetylate other amino acid side-chains, leading to the possibility that aspirin-mediated lysine acetylation could explain some of its as-yet unexplained drug actions or side-effects. Using isotopically labeled aspirin-d<sub>3</sub>, in combination with acetylated lysine pur  ...[more]

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