Gastroenterology

Gastroenterology

Volume 105, Issue 3, September 1993, Pages 876-888
Gastroenterology

Secretion and contribution to lipolysis of gastric and pancreatic lipases during a test meal in humans

https://doi.org/10.1016/0016-5085(93)90908-UGet rights and content

Abstract

Background: The aim of this study was to quantitatively evaluate the relative contributions to in vivo lipolysis of gastric and pancreatic lipases. Methods: Gastric and pancreatic lipase secretions were measured, and their respective levels were determined in duodenal fluid during the digestion of a liquid test meal in healthy volunteers. Gastric lipase activity was clearly distinguished from that of pancreatic lipase by using both a specific enzymatic assay and an enzyme-linked immunosorbent assay. Lipolysis products were monitored throughout the digestion period. Results: On a weight basis, the ratio of pancreatic lipase to gastric lipase total secretory outputs was found to be around four after 3 hours of digestion. The level of gastric hydrolysis was calculated to be 10% ± 1% of the acyl chains released from the meal triglycerides. Gastric lipase remained active in the duodenum where it might still hydrolyze 7.5% of the triglyceride acyl chains. Conclusions: Globally during the whole digestion period, gastric lipase might hydrolyze 17.5% of the triglyceride acyl chains. In other words, gastric lipase might hydrolyze 1 acyl chain of 4, which need to be hydrolyzed for a complete intestinal absorption of monoglycerides and free fatty acids resulting from the degradation of two triglyceride molecules.

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    This research was performed with the help of financial support from the Jouveinal Laboratories (Drs. Claude Bénicourt and JeanLouis Junien) and from the European Communities' BRIDGE-T-Lipase program (contract BIOT-CT91-0274 [DTEE]).

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