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Pancreatic lipase
Pancreatic lipase–colipase complex with inhibitor 1LPB.png
Cartoon diagram of human pancreatic lipase (colored by secondary structure: alpha helices in red, beta sheets in yellow, and random coil in green) in complex with pig colipase (colored blue) and a small molecule inhibitor (upper left). From PDB 1LPB.
Identifiers
Symbol PNLIP
Entrez 5406
HUGO 9155
OMIM 246600
RefSeq NM_000936
UniProt P16233
Other data
EC number 3.1.1.3
Locus Chr. 10 q26.1

Pancreatic lipase is an enzyme (more specifically, a lipase) secreted from the pancreas that uses hydrolysis to break apart fat molecules. Bile salts secreted from the liver and stored in gallbladder are released into the duodenum where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids, 1 monoglyceride and glycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal. This protein belongs to pancreatic lipase family.

Unlike some pancreatic enzymes like trypsin which are first secreted in the inactive form (e.g. trypsinogen), pancreatic lipase is secreted as the active enzyme.

Diagnostic importance

Pancreatic lipase is secreted into the duodenum through the duct system of the pancreas. Normally its concentration of serum is very low. The basic pancreatic lipase used to digest the fat droplets is Streapsin, found in the intestinal lumen. Under extreme disruption of pancreatic function, such as pancreatitis or pancreatic adenocarcinoma, the pancreas may begin to autolyse and release pancreatic enzymes into serum. Thus, through measurement of serum concentration of pancreatic lipase, pancreatitis can be diagnosed.

See also

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