title: Protein tyrosine nitration of 15-hydroxy prostaglandin dehydrogenase in the human mast cell line LAD2.
abstract: Mast cells (MC) play a pivotal role in allergic inflammation and nitric oxide (NO) is known to regulate MC function. One mechanism of NO mediated actions is the post-translational modification protein tyrosine nitration mediated by reactive nitrogen species. In this study we identified targets for nitration in the human mast cell line LAD2 after treatment with a nitric oxide donor and with peroxynitrite. Using two dimensional gel electrophoresis and western blot analyses with monoclonal and polyclonal antibodies we identified 15-hydroxy prostaglandin dehydrogenase (PGDH), a major prostaglandin catabolizing enzyme, as a target for nitration in LAD2. This is the first report on expression of this enzyme in MC and also the first report that PGDH is a target of protein tyrosine nitration. Since MC synthesize and metabolize many prostaglandins including prostaglandin E(2), the major substrate for PGDH, nitration of this prostaglandin catabolizing enzyme is likely functionally significant.
authors.affiliation: Pulmonary Research Group, Department of Medicine, University of Alberta, Edmonton, Canada.
authors.forename: Yokananth
authors.initials: Y
authors.lastname: Sekar
authors.forename: A Dean
authors.initials: AD
authors.lastname: Befus
mesh_terms: D002460:Cell Line; D006801:Humans; D006911:Hydroxyprostaglandin Dehydrogenases / Q000378:metabolism*; D008407:Mast Cells / Q000187:drug effects / Q000378:metabolism*; D009569:Nitric Oxide / Q000378:metabolism; D020030:Nitric Oxide Donors / Q000494:pharmacology; D030421:Peroxynitrous Acid / Q000494:pharmacology; D011499:Protein Processing, Post-Translational; D026422:S-Nitrosoglutathione / Q000494:pharmacology; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D020030:Nitric Oxide Donors; D030421:Peroxynitrous Acid; D009569:Nitric Oxide; D014443:Tyrosine; D026422:S-Nitrosoglutathione; D006911:Hydroxyprostaglandin Dehydrogenases; C035859:15-hydroxyprostaglandin dehydrogenase