Dataset Information

Mouse Heart 2 day Ischemia/Reperfusion Surgery - Mass Spectrometry

ABSTRACT: Quantitative mass spectrometry of mouse hearts (left ventricle) 2 days after ischemia/reperfusion or sham surgery.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart

DISEASE(S): Cardiovascular System Disease

SUBMITTER: Frank Stein

LAB HEAD: Mirko Völkers

PROVIDER: PXD035154 | Pride | 2025-01-30

REPOSITORIES: pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Bert_171212_P0503_MR_MV_Pool1_fr1.raw	Raw
	Bert_171212_P0503_MR_MV_Pool1_fr10.raw	Raw
	Bert_171212_P0503_MR_MV_Pool1_fr11.raw	Raw
	Bert_171212_P0503_MR_MV_Pool1_fr12.raw	Raw
	Bert_171212_P0503_MR_MV_Pool1_fr2.raw	Raw

Items per page:

1 - 5 of 56

Publications

Transient Inhibition of Translation Improves Cardiac Function After Ischemia/Reperfusion by Attenuating the Inflammatory Response.

Hofmann Christoph C Serafin Adrian A Schwerdt Ole M OM Fischer Johannes J Sicklinger Florian F Younesi Fereshteh S FS Byrne Nikole J NJ Meyer Ingmar S IS Malovrh Ellen E Sandmann Clara C Sandmann Clara C Jürgensen Lonny L Kamuf-Schenk Verena V Stroh Claudia C Löwenthal Zoe Z Finke Daniel D Boileau Etienne E Beisaw Arica A Bugger Heiko H Rettel Mandy M Stein Frank F Katus Hugo A HA Jakobi Tobias T Frey Norbert N Leuschner Florian F Völkers Mirko M

Circulation 20240829 16

<h4>Background</h4>The myocardium adapts to ischemia/reperfusion (I/R) by changes in gene expression, determining the cardiac response to reperfusion. mRNA translation is a key component of gene expression. It is largely unknown how regulation of mRNA translation contributes to cardiac gene expression and inflammation in response to reperfusion and whether it can be targeted to mitigate I/R injury.<h4>Methods</h4>To examine translation and its impact on gene expression in response to I/R, we mea ...[more]

PMID: 39206545

Similar Datasets

Project description:Ubiquitination of proteins is central to protein homeostasis and other cellular processes including DNA repair, vesicular transport, cell-division etc. The process of ubiquitination is conserved from yeast to humans and is carried out by the sequential action of three enzymes: E1, E2 and E3. There are an estimated >600 E3 ligases in humans that execute ubiquitination of specific target proteins in a spatio-temporal manner to elicit desired signaling effects. Here, we developed a simple, proximity-based labeling method to selectively biotinylate substrates of a given ubiquitin ligase. Our method exploits the proximity and the relative orientation of the E3-ligase catalytic domain with respect to ubiquitin observed in the enzymatic intermediate-state structures of E3-E2~Ub. By fusing the biotin ligase BirA and an Avi-tag variant to the candidate E3 ligase and ubiquitin, respectively, we were able to specifically enrich the bona fide substrates and potential new substrates of the ligase using a one-step Streptavidin pulldown under denaturing conditions. As proof-of-principle, we applied our method, which we named Ub-POD, to the RING E3 ligase Rad18. Rad18 ubiquitinates DNA-sliding clamp PCNA upon UV-induced DNA damage. We identified PCNA and several other critical players in the DNA damage repair pathway in a single Ub-POD experiment. We further discovered an unintended but important application of Ub-POD, where we were able to pin down the cellular localization of Rad18- mediated ubiquitination to the damaged DNA nuclear puncta through Streptavidin immunofluorescence. We also applied our method to TRAF6, another RING ubiquitin ligase involved in TNF signaling, successfully identifying known and potentially new substrates. Finally, we adapted our method to the U-box type E3 ubiquitin ligase CHIP to demonstrate that we can identify substrates of two major classes of mammalian ubiquitin ligases. We anticipate that our method and principle could be widely adapted to all classes of ubiquitin ligases to identify substrates and localize the cellular site(s) of ubiquitination.