Identification of Malonylation, Succinylation, and Glutarylation in Serum Proteins of Acute Myocardial Infarction Patients

Abstract

Purpose: To identify protein malonylation, succinylation, and glutarylation in human and rat serum.

Experimental design: Immunoprecipitation coupled with MS/MS is employed to compare the relative abundance of malonylation, succinylation, and glutarylation of serum protein in acute myocardial infarction human and rat.

Results: One hundred thirty and 48 unique malonylated, succinylated, or glutarylated peptides are found in human and rat serum, respectively. Succinylation is the most predominant modification. The most modified protein is albumin. Abundance of serum protein succinylation and glutarylation is significantly (p < 0.05) lower in the peripheral serum of ST-segment elevation myocardial infarction patients compared with healthy volunteers, which is also observed in acute myocardial infarction rats.

Conclusions and clinical relevance: Malonylation, succinylation, and glutarylation widely exist in mammalian serum proteins, and may reveal novel mechanism of acute myocardial infarction.

Keywords: glutarylation; malonylation; succinylation.