Pankreasamylase

Pankreasamylase, or pancreatic amylase, is a digestive enzyme produced by the exocrine pancreas. It catalyzes the hydrolysis of alpha-1,4-glycosidic bonds in starch and glycogen, aiding carbohydrate digestion in the small intestine. It is secreted by pancreatic acinar cells into the pancreatic juice, which is released into the duodenum via the pancreatic duct and maintained in an alkaline environment by bicarbonate.

It acts on starch to yield smaller oligosaccharides such as maltose and maltotriose and limit dextrins, which are further degraded by brush-border enzymes to glucose for absorption. Alpha-1,6 bonds are left to debranching enzymes in the intestinal lumen.

Genetics and isoforms: In humans, pancreatic amylase is encoded by the AMY2A and AMY2B genes and is distinct from salivary amylase, encoded by AMY1. The pancreatic enzymes are produced in the pancreas and secreted into the intestinal lumen.

Clinical significance: Serum or plasma pancreatic amylase is commonly measured in the evaluation of suspected acute pancreatitis; levels rise within a few hours, peak around 24 hours, and normalize within several days. Amylase testing is less specific than lipase for pancreatitis and can be elevated in other conditions such as salivary gland inflammation, renal failure, and certain intestinal disorders. Urinary amylase testing is an alternative in some settings.

Biochemistry and physiology: Pancreatic amylase is an enzyme in the digestive system that acts best at a neutral to slightly alkaline pH. In the intestinal lumen, it facilitates starch digestion in concert with other enzymes; dietary starch is ultimately broken down to glucose for absorption.