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This phenomenon is referred to as the incretin effect ( Figure 1 ) and gastric inhibitory peptide (GIP) ( GIP is a peptide of 42 amino acids belonging to the glucagon secretin family of peptides secreted from the K-cells of the upper intestine was earlier known to inhibit gastric acid secretion, so it was called gastric inhibitory peptide, but then later, it also showcased its efficacy on the pancreas by stimulating insulin secretion glucose dependently and was renamed as glucose-dependent insulinotropic peptide ( Both GLP-1 and GIP validate their functional role by binding to their specific receptors GLP-1R and GIPR, which belong to the G protein-coupled receptor family triggering adenylate cyclase activity and elevating the levels of intracellular cyclic adenosine monophosphate (C-AMP) in pancreatic -cells with the activation of protein kinase A (PKA) and exchange protein activated by C-AMP2 (EPAC2) involved in a broad range of intracellular actions such as altered ion channel activity, elevated cytosolic calcium levels which facilitate the fusion of insulin granules to the plasma membrane, and enhanced exocytosis of insulin-containing granules, contributing to the enhancement of insulin secretion in a glucose-dependent manner ( Crux of the matter: Dipeptidyl peptidase-IV The human gene dipeptidyl peptidase (DPP)-IV is located on chromosome 2 and encodes dipeptidyl peptidase IV, a serine protease, an enzyme located on epithelial as well as endothelial cells found to be expressed in varied tissues including the liver, gut, placenta, and kidney, causing the catalytic degradation and reduction in the half-lives of GLP-1 and GIP levels and further ensuing the perturbation of glucose homeostasis ( Figure 2 )