<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Eligini S</submitter><funding>Italian Ministry of Health</funding><pagination>496</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8005028</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(3)</volume><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 &lt;sup>35&lt;/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</pubmed_abstract><journal>Antioxidants (Basel, Switzerland)</journal><pubmed_title>Cyclooxygenase-2 Glycosylation Is Affected by Peroxynitrite in Endothelial Cells: Impact on Enzyme Activity and Degradation.</pubmed_title><pmcid>PMC8005028</pmcid><funding_grant_id>Ricerca Corrente RC 2019 MPP1A ID 2755301</funding_grant_id><pubmed_authors>Altomare A</pubmed_authors><pubmed_authors>Banfi C</pubmed_authors><pubmed_authors>Eligini S</pubmed_authors><pubmed_authors>Colli S</pubmed_authors><pubmed_authors>Habib A</pubmed_authors><pubmed_authors>Aldini G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Cyclooxygenase-2 Glycosylation Is Affected by Peroxynitrite in Endothelial Cells: Impact on Enzyme Activity and Degradation.</name><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 &lt;sup>35&lt;/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</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Mar</publication><modification>2026-07-16T22:45:24.014Z</modification><creation>2025-05-29T21:42:02.66Z</creation></dates><accession>S-EPMC8005028</accession><cross_references><pubmed>33806920</pubmed><doi>10.3390/antiox10030496</doi></cross_references></HashMap>