Elevated lipase concentrations 3-to-4-fold greater than the upper normal limit is indicative of pancreatitis, however, the degree of elevations does not correlate with the severity of the disease ^{2, 3}.

In pancreatic dysfunction, lipase concentrations rise between 4 and 6 hours, peaking at 48 hours and returning to baseline within 8 to 14 days. It has a half-life of 6.7 to 13.7 hours in plasma. The half-life of amylase (another assay utilised in the diagnosis of pancreatic dysfunction) is less, however, lipase is filtered by the glomerulus and reabsorbed by the tubules which may contribute towards the longer half-life of lipase.

Lipase offers a few advantages over amylase including: a slightly better specificity, greater sensitivity for patients presenting late, due to the longer half-life, and greater sensitivity in alcoholic pancreatitis ⁴.

Furthermore, for prolonged longitudinal injuries, lipase activity tends to be more sensitive compared to amylase as lipase concentrations within the zymogen granules are approximately 4.5 times than those of amylase. Consequently, recurring injuries are more likely to be recognised due to the leakage of lipase into the bloodstream. Moreover, lipase concentrations are less affected by intestinal injury or renal dysfunction compared to amylase ².

Derived from zymogen granules of pancreatic acinar cells, lipase is involved in the digestion of lipids for the subsequent absorption in the small intestine ^{1, 2}. The pancreas is located in the anterior abdominal cavity adjacent to the liver, duodenum and stomach to allow the secretion of digestive enzymes into the small intestine, and to convert ingesta into absorbable lipids, carbohydrates and proteins. The exocrine pancreas provides a microenvironment for pancreatic islet cells. The pancreatic islet cells provide the embedded endocrine function of the pancreas which in turn enables the hepatic and peripheral tissues to modulate blood glucose levels and other functions ².