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.

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