PXD003655

PXD003655 is an original dataset announced via ProteomeXchange.

Title	Half-lives of aspirin-mediated lysine acetylations
Description	Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. An important property of aspirin is its ability to acetylate multiple cellular proteins with some pharmacological functions explicable by the irreversible acetylation of cyclooxygenases at active site serine residues. We have used a labeled form of aspirin, aspirin-d3 to acetylate proteins in cultured human cells, and unambiguously identified over 12000 sites of acetylation, using acetylated lysine peptide enrichment combined with mass-spectrometry-based proteomics. Aspirin increases lysine acetylation occupancy of the majority of detected endogenous sites, but leaves almost unchanged a small group that are already highly acetylated. We show that cells are remarkably tolerant of this acetylation insult unless endogenous deacetylases are inhibited. This work raises the possibility that rather than single protein effects, some of the clinical features of aspirin may be the consequence of multiple concurrent protein modifications, and that combining aspirin with lysine deacetylase inhibitors may have important medical implications.
HostingRepository	PRIDE
AnnounceDate	2019-03-05
AnnouncementXML	Submission_2019-03-05_02:52:18.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mike Tatham
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-02-17 02:36:35	ID requested
⏵ 1	2019-03-05 02:52:20	announced

Tatham MH, Cole C, Scullion P, Wilkie R, Westwood NJ, Stark LA, Hay RT, A Proteomic Approach to Analyze the Aspirin-mediated Lysine Acetylome. Mol Cell Proteomics, 16(2):310-326(2017) [pubmed]

curator keyword: Biomedical

submitter keyword: Aspirin, lysine, acetylation

Ronald Thomas Hay
contact affiliation	School of Life Sciences University of Dundee
contact email	r.t.hay@dundee.ac.uk
lab head
Mike Tatham
contact affiliation	University of Dundee
contact email	m.tatham@dundee.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD003655
     1. Label: PRIDE project
     2. Name: Half-lives of aspirin-mediated lysine acetylations