{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Eligini S"],"funding":["Italian Ministry of Health"],"pagination":["496"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8005028"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(3)"],"pubmed_abstract":["The exposure of human endothelial cells to 3-morpholinosydnonimine (SIN-1) induced the expression of cyclooxygenase-2 (COX-2) in a dose- and time-dependent manner. Interestingly, after a prolonged incubation (>8 h) several proteoforms were visualized by Western blot, corresponding to different states of glycosylation of the protein. This effect was specific for SIN-1 that generates peroxynitrite and it was not detected with other nitric oxide-donors. Metabolic labeling experiments using <sup>35</sup>S or cycloheximide suggested that the formation of hypoglycosylated COX-2 was dependent on de novo synthesis of the protein rather than the deglycosylation of the native protein. Moreover, SIN-1 reduced the activity of the hexokinase, the enzyme responsible for the first step of glycolysis. The"],"journal":["Antioxidants (Basel, Switzerland)"],"pubmed_title":["Cyclooxygenase-2 Glycosylation Is Affected by Peroxynitrite in Endothelial Cells: Impact on Enzyme Activity and Degradation."],"pmcid":["PMC8005028"],"funding_grant_id":["Ricerca Corrente RC 2019 MPP1A ID 2755301"],"pubmed_authors":["Altomare A","Banfi C","Eligini S","Colli S","Habib A","Aldini G"],"additional_accession":[]},"is_claimable":false,"name":"Cyclooxygenase-2 Glycosylation Is Affected by Peroxynitrite in Endothelial Cells: Impact on Enzyme Activity and Degradation.","description":"The exposure of human endothelial cells to 3-morpholinosydnonimine (SIN-1) induced the expression of cyclooxygenase-2 (COX-2) in a dose- and time-dependent manner. Interestingly, after a prolonged incubation (>8 h) several proteoforms were visualized by Western blot, corresponding to different states of glycosylation of the protein. This effect was specific for SIN-1 that generates peroxynitrite and it was not detected with other nitric oxide-donors. Metabolic labeling experiments using <sup>35</sup>S or cycloheximide suggested that the formation of hypoglycosylated COX-2 was dependent on de novo synthesis of the protein rather than the deglycosylation of the native protein. Moreover, SIN-1 reduced the activity of the hexokinase, the enzyme responsible for the first step of glycolysis. The","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2026-07-16T22:45:24.014Z","creation":"2025-05-29T21:42:02.66Z"},"accession":"S-EPMC8005028","cross_references":{"pubmed":["33806920"],"doi":["10.3390/antiox10030496"]}}