Quantitative Phosphoproteomics of the Angiotensin AT
angiotensin receptors
apoptosis
endothelial cells
histone deacetylase 1
phosphoproteomics
Journal
Hypertension (Dallas, Tex. : 1979)
ISSN: 1524-4563
Titre abrégé: Hypertension
Pays: United States
ID NLM: 7906255
Informations de publication
Date de publication:
11 2022
11 2022
Historique:
pubmed:
10
9
2022
medline:
19
11
2022
entrez:
9
9
2022
Statut:
ppublish
Résumé
Angiotensin AT Phosphorylation status of human aortic endothelial cells after stimulation with C21 (1 µM; 0, 1, 3, 5, 20 minutes) was determined utilizing time-resolved quantitative phosphoproteomics. Specific changes in protein phosphorylation and acetylation were confirmed by Western Blotting. Functional tests included resazurin assay for cell proliferation, and caspase 3/7 luminescence assay or FACS analysis of annexin V expression for apoptosis. AT Contrary to the prevailing view that AT
Sections du résumé
BACKGROUND
Angiotensin AT
METHODS
Phosphorylation status of human aortic endothelial cells after stimulation with C21 (1 µM; 0, 1, 3, 5, 20 minutes) was determined utilizing time-resolved quantitative phosphoproteomics. Specific changes in protein phosphorylation and acetylation were confirmed by Western Blotting. Functional tests included resazurin assay for cell proliferation, and caspase 3/7 luminescence assay or FACS analysis of annexin V expression for apoptosis.
RESULTS
AT
CONCLUSIONS
Contrary to the prevailing view that AT
Identifiants
pubmed: 36082664
doi: 10.1161/HYPERTENSIONAHA.121.18620
doi:
Substances chimiques
compound 21
RC2V4W0EYC
Tumor Suppressor Protein p53
0
Histones
0
Receptor, Angiotensin, Type 2
0
Phosphoric Monoester Hydrolases
EC 3.1.3.2
Serine
452VLY9402
Angiotensins
0
HDAC1 protein, human
EC 3.5.1.98
Histone Deacetylase 1
EC 3.5.1.98
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM