title: Adipocyte protein modification by Krebs cycle intermediates and fumarate ester-derived succination.
abstract: Protein succination, the non-enzymatic modification of cysteine residues by fumarate, is distinguishable from succinylation, an enzymatic reaction forming an amide bond between lysine residues and succinyl-CoA. Treatment of adipocytes with 30 mM glucose significantly increases protein succination with only a small change in succinylation. Protein succination may be significantly increased intracellularly after treatment with fumaric acid esters, however, the ester must be removed by saponification to permit 2SC-antibody detection of the fumarate adduct.
authors.affiliation: Department of Pharmacology, Physiology and Neuroscience, University of South Carolina School of Medicine, 6439 Garners Ferry Road, VA Bldg 1, 3rd Floor, D16, Columbia, SC, 29208, USA.
authors.forename: Allison M
authors.initials: AM
authors.lastname: Manuel
authors.forename: Norma
authors.initials: N
authors.lastname: Frizzell
mesh_terms: D016475:3T3 Cells; D017667:Adipocytes / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D002952:Citric Acid Cycle / Q000187:drug effects; D003545:Cysteine / Q000378:metabolism; D005650:Fumarates / Q000494:pharmacology*; D005947:Glucose / Q000378:metabolism; D051379:Mice; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D011506:Proteins / Q000378:metabolism*
chemical_list: D005650:Fumarates; D011506:Proteins; D005947:Glucose; D003545:Cysteine