PXD008385

PXD008385 is an original dataset announced via ProteomeXchange.

Title	Obesity-mediated regulation of the cardiac acetylome
Description	Lysine residues undergo diverse and reversible post-translational modifications including acetylation. Acetylation of lysine residues have traditionally been studied as epigenetic modifiers of histone tails within chromatin that provides an important mechanism for regulating gene expression. In the heart, histone acetylation acts as a key regulator of cardiac remodeling and function. However, recent studies have shown that thousands of proteins (~4,500) can be acetylated at multiple acetylation sites (~15,000 sites). These data suggest that the acetylome rivals phosphorylation in prevalence as a post-translational modification. Based on this, we examined the impact of obesity on the regulation of lysine acetylation in the left ventricle of male c57BL/6J mice. We report that obesity contributed to a significant increase in heart enlargement and fibrosis. Of interest, immunoblot analysis demonstrated that lysine acetylation was markedly altered in response to diet-induced obesity and that this phenomena was cardiac tissue specific. Mass spectral analysis was performed in which 3264 proteins were identified in the left ventricle. Of these, 254 proteins were acetylated, 16 of which were significantly impacted by obesity. Ingenuity Pathway Analysis identified the Cardiovascular Disease network as significantly regulated by obesity, 54 of the 254 acetylated proteins impact this pathway. This network includes LIM domain-binding protein 3 (LDB3), aconitate hydratase (ACO2), and dihydrolipoyl dehydrogenase (DLD), which are all significantly impacted by obesity and known to regulate cardiac function. Combined, these findings suggest a critical role for the cardiac acetylome in obesity-mediated remodeling and ultimately have the potential to elucidate novel targets that regulate cardiac pathology.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:42:09.723.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD008385
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Craig Ulrich
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	TMT6plex; Oxidation; Acetyl; Carbamidomethyl
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-07 03:17:14	ID requested
1	2018-08-06 07:42:15	announced
⏵ 2	2024-10-22 04:42:17	announced	2024-10-22: Updated project metadata.

Romanick SS, Ulrich C, Schlauch K, Hostler A, Payne J, Woolsey R, Quilici D, Feng Y, Ferguson BS, Obesity-mediated regulation of cardiac protein acetylation: parallel analysis of total and acetylated proteins via TMT-tagged mass spectrometry. Biosci Rep, 38(5):(2018) [pubmed]

10.1042/bsr20180721;

10.6019/PXD008385;

curator keyword: Biological, Biomedical

submitter keyword: Mouse, Heart, Cardiovascular Disease, Acetylation

Craig Ulrich
contact affiliation	Department of Pharmacology, University of Nevada, Reno School of Medicine
contact email	culrich@medicine.nevada.edu
lab head
Craig Ulrich
contact affiliation	Pharmacology
contact email	culrich@med.unr.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008385
     1. Label: PRIDE project
     2. Name: Obesity-mediated regulation of the cardiac acetylome