PXD032978

PXD032978 is an original dataset announced via ProteomeXchange.

Title	Analysis of HUVEC secretome and histone N-terminal acetylation after Notch activation
Description	Vasculature permeate our entire body and involved in homeostasis and progression of various disease. Endothelium is a backbone of cardiovascular system and endothelial disfunction is associated with most forms of cardiovascular disease from atherosclerosis to chronic heart failure. Decrease in shear stress, particularly due to disturbance of the blood flow by bends or vascular obstruction, lead to atherosclerosis and endothelial disfunction. Notch signaling may act as mechanosensor and assumed to be one of the central signal pathways associated with endothelial disfunction. Association of shear stress, Notch and endothelial dysfunction is well known, molecular mechanisms connected these factors still poorly understood. One might assume that long-term shear stress and dysregulation of Notch in endothelium cause changes in epigenomic profile. While epigenomic changes in shear stressed environment are known to be involved in endothelial disfunction, possible connection of Notch and epigenetic changes in endothelium has not yet been tested. Therefore, here we analyzed how activation of Notch signaling influence on histone code and secretome of endothelial cells in vitro. We found that activation of Notch increase level of N-acetylated forms of Histone 1: H1-0, H1-3, H1-4, H1-5, H1-10. These changes were also associated with changes in secretome profile of endothelium and might have broad biomedical significance in case of endothelial dysfunction.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:27:11.821.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD032978
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Arseniy Lobov
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	maXis; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2022-04-03 08:12:29	ID requested
1	2023-02-15 05:22:21	announced
⏵ 2	2023-11-14 08:27:12	announced	2023-11-14: Updated project metadata.

10.6019/PXD032978;

submitter keyword: LC-MSMS, histone,Notch pathway, N-terminal acetylation, endothelium, timsToF, HUVEC

Anna B. Malashicheva
contact affiliation	Laboratory of regenerative biomedicine, Institute of cytology of the Russian Academy of Science
contact email	amalashicheva@gmail.com
lab head
Arseniy Lobov
contact affiliation	Emmanuel Levy Lab, Dept. of Chemical and Structural Biology, Weizmann Institute of Science
contact email	arseniylobov@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD032978
     1. Label: PRIDE project
     2. Name: Analysis of HUVEC secretome and histone N-terminal acetylation after Notch activation