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Endogenous lipase activity in Caco-2 cells

J H Spalinger¹, E G Seidman, D Ménard

¹Division of Pediatric Gastroenterology and Nutrition, Centre de Recherche, Hôpital Ste-Justine, University of Montreal, 3175, Côte Ste-Catherine Rd, Montreal, Quebec H3T 1C5, Canada.

Biochimica Et Biophysica Acta

|August 26, 1998

Summary

Caco-2 cells possess endogenous lipase activity that hydrolyzes triglycerides, primarily in the cytosol. This lipase aids in fatty acid absorption, with added gastric lipase significantly enhancing uptake.

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Area of Science:

Cell Biology
Biochemistry
Gastroenterology

Background:

Dietary triglycerides require hydrolysis for absorption.
Caco-2 cells are a model for enterocyte lipid metabolism.
Endogenous lipase activity in Caco-2 cells was previously unreported.

Purpose of the Study:

Determine endogenous Caco-2 cell lipase activity.
Examine its triglyceride hydrolysis capacity.
Define its intracellular location.

Main Methods:

Utilized [1-14C]triolein to assay lipase activity.
Fractionated cell components to localize lipase.
Tested effects of various inhibitors and exogenous gastric lipase.

Main Results:

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Caco-2 cells exhibit endogenous lipase activity hydrolyzing triolein into fatty acids and monoglycerides.
Lipase activity is time- and concentration-dependent, primarily cytosolic.
Exogenous gastric lipase significantly enhanced triolein hydrolysis, fatty acid uptake, and lipid secretion.

Conclusions:

Caco-2 cells possess an endogenous lipase for cytosolic triglyceride hydrolysis.
Apical membrane and secreted lipase activities contribute to energy uptake.
Gastric lipase addition markedly boosts fatty acid uptake beyond endogenous activity.