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Adipocyte protein modification by Krebs cycle intermediates and fumarate ester-derived succination.
Manuel, Allison M; Frizzell, Norma.
Affiliation
  • Manuel AM; 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.
Amino Acids ; 45(5): 1243-7, 2013 Nov.
Article in En | MEDLINE | ID: mdl-23892396
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Citric Acid Cycle / Adipocytes / Fumarates Limits: Animals Language: En Journal: Amino Acids Journal subject: BIOQUIMICA Year: 2013 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Citric Acid Cycle / Adipocytes / Fumarates Limits: Animals Language: En Journal: Amino Acids Journal subject: BIOQUIMICA Year: 2013 Document type: Article Affiliation country: