In regards to informational content, the proteome is more complex than the transcriptome and genome [1]. As such, the regulation of the quality and function of proteins are essential to cellular homeostasis. Under both physiological and pathophysiological conditions, the activation of cellular signaling pathways relies heavily on reversible posttranslational modifications (PTMs) for controlling the function and stability of proteins [2]. PTMs are established and removed in a highly dynamic manner and exist in many different forms and flavors, such as glycosylation, phosphorylation, SUMOylation, and methylation, to name a few [3]. The purpose of this review article is to provide a brief overview of glycation, a process by which dicarbonyls react nonenzymatically with amino groups of proteins to form advanced glycation end-products (AGEs) [4]. We will also discuss emerging data demonstrating that the protein deglycase DJ-1 (PARK7) serves to oppose glycation in the heart.