The Maillard reaction, a chemical reaction between amino acids and sugars, is exploited to produce flavorful food ubiquitously, from the baking industry to our everyday lives. However, the Maillard reaction also occurs in all cells, from prokaryotes to eukaryotes, forming Advanced Glycation End-products (AGEs). AGEs are a heterogeneous group of compounds resulting from the irreversible reaction between biomolecules and &#
x3b1;-dicarbonyls (&#
x3b1;-DCs), including methylglyoxal (MGO), an unavoidable byproduct of anaerobic glycolysis and lipid peroxidation. We previously demonstrated that <i>Caenorhabditis elegans</i> mutants lacking the <i>
glod-4</i> glyoxalase enzyme displayed enhanced accumulation of &#
x3b1;-DCs, reduced lifespan, increased neuronal damage, and touch hypersensitivity. Here, we demonstrate that <i>
glod-4</i> mutation increased food intake and identify that MGO-derived hydroimidazolone, MG-H1, is a mediator of the observed increase in food intake. RNAseq analysis in <i>
glod-4</i> knockdown worms identified upregulation of several neurotransmitters and feeding genes. Suppressor screening of the overfeeding phenotype identified the <i>
tdc-1</i>-tyramine-<i>
tyra-2/ser-2</i> signaling as an essential pathway mediating AGEs (MG-H1) induced feeding in <i>
glod-4</i> mutants. We also identified the <i>
elt-3</i> GATA transcription factor as an essential upstream regulator for increased feeding upon accumulation of AGEs by partially controlling the expression of <i>
tdc-1</i> gene. Further, the lack of either <i>
tdc-1</i> or <i>
tyra-2/ser-2</i> receptors suppresses the reduced lifespan and rescues neuronal damage observed in <i>
glod-4</i> mutants. Thus, in <i>C. elegans,</i> we identified an <i>
elt-3</i> regulated tyramine-dependent pathway mediating the toxic effects of MG-H1 AGE. Understanding this signaling pathway may help understand hedonistic overfeeding behavior observed due to modern AGEs-rich diets.