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Updated: May 29, 2026

Using Caco-2 Cells to Study Lipid Transport by the Intestine
Published on: August 20, 2015
BSSL and PLRP2: key enzymes for lipid digestion in the newborn examined using the Caco-2 cell line
Eva-Lotta Andersson1, Olle Hernell, Lars Bläckberg
1Department of Clinical Sciences/Pediatrics, Umeå University, S-901 85 Umeå, Sweden.
Insights
Bile salt-stimulated lipase (BSSL) and pancreatic lipase-related protein 2 (PLRP2) are key in neonatal intestinal fat digestion. These lipases work synergistically, enhancing fat absorption and reesterification in infants.
Area of Science:
- Gastroenterology and Nutrition
- Lipid Metabolism
- Neonatal Physiology
Background:
- Bile salt-stimulated lipase (BSSL) and pancreatic lipase-related protein 2 (PLRP2) are crucial pancreatic enzymes in early life.
- Their role in neonatal intestinal fat digestion requires further elucidation.
Purpose of the Study:
- To investigate the function of BSSL and PLRP2 in neonatal intestinal fat digestion.
- To determine if these lipases exhibit synergistic effects on triglyceride hydrolysis and absorption.
Main Methods:
- Utilized Caco-2 cells as a model for the small intestinal epithelium.
- Incubated purified human BSSL and PLRP2 with triglyceride substrates under infant-like bile salt conditions.
- Quantified free fatty acid absorption and reesterification into triglycerides.
Main Results:
- Both BSSL and PLRP2 effectively hydrolyzed triglycerides into free fatty acids and glycerol.
- A significant synergistic effect was observed between BSSL and PLRP2, increasing cellular uptake and reesterification by fourfold.
- Synergistic effects were also noted for retinyl ester hydrolysis, while cholesteryl ester hydrolysis showed an additive effect.
Conclusions:
- BSSL and PLRP2 are identified as key enzymes in neonatal intestinal fat digestion.
- Their synergistic action plays a critical role in infant fat absorption and nutrient utilization.
- Findings highlight differences in neonatal versus adult intestinal fat digestion, with implications for infant nutrition strategies.
Abstract:
In rodents, bile salt-stimulated lipase (BSSL) and pancreatic lipase-related protein 2 (PLRP2) are the dominant lipases expressed in the exocrine pancreas in early life when milk is the main food. The aim of the present study was to evaluate whether BSSL and PLRP2 are also key enzymes in neonatal intestinal fat digestion. Using Caco-2 cells as a model for the small intestinal epithelium, purified human enzymes were incubated in the apical compartment with substrates, bile salt composition and concentrations physiologic to newborn infants. Both BSSL and PLRP2 hydrolyzed triglycerides (TG) to free FA and glycerol. Released FA were absorbed by the cells and reesterfied to TG. Together, BSSL and PLRP2 had a synergistic effect, increasing cellular uptake and reesterification 4-fold compared with the sum of each lipase alone. A synergistic effect was also observed with retinyl ester as a substrate. PLRP2 hydrolyzed cholesteryl ester but not as efficiently as BSSL, and the two had an additive rather than synergistic effect. We conclude the key enzymes in intestinal fat digestion are different in newborns than later in life. Further studies are needed to fully understand this difference and its implication for designing optimal neonatal nutrition.
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