4.4 Article

Adipocyte protein modification by Krebs cycle intermediates and fumarate ester-derived succination

Journal

AMINO ACIDS
Volume 45, Issue 5, Pages 1243-1247

Publisher

SPRINGER WIEN
DOI: 10.1007/s00726-013-1568-z

Keywords

Succination; S-(2-succino)cysteine; Succinylation; Acetylation; Fumarate; Ester; Glutathione

Funding

  1. University of South Carolina Undergraduate Research Office
  2. American Diabetes Association [1-11-JF-13]
  3. National Institute of Diabetes and Digestive and Kidney Diseases [DK-19971]

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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.

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