Characterization of the proteome of cytoplasmic lipid droplets in mouse enterocytes after a dietary fat challenge

• Published in: PloS one Vol. 10; no. 5; p. e0126823
• Main Authors: D'Aquila, Theresa, Sirohi, Devika, Grabowski, Jeffrey M, Hedrick, Victoria E, Paul, Lake N, Greenberg, Andrew S, Kuhn, Richard J, Buhman, Kimberly K
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 18.05.2015; Public Library of Science (PLoS)
• Subjects: Absorption; Animals; Apolipoprotein A; Apolipoproteins A - metabolism; Carrier Proteins - metabolism; Coenzyme A Ligases - metabolism; Confocal; Diet; Dietary fat; Dietary Fats - administration & dosage; Droplets; Drosophila; Electron microscopy; Energy storage; Enterocytes; Enterocytes - metabolism; Enterocytes - ultrastructure; Essential nutrients; Fat metabolism; Fatty acids; Identification; Insects; Laboratory animals; Lipid Droplets - metabolism; Lipid Droplets - ultrastructure; Lipid Metabolism; Lipids; Localization; Male; Metabolic Networks and Pathways; Metabolic pathways; Metabolism; Mice; Mice, Inbred C57BL; Microscopy, Electron, Transmission; Models, Biological; Nutrients; Nutrition research; Oils & fats; Perilipin-3; Physiological aspects; Physiological research; Proteins; Proteome - metabolism; Proteomes; Regulators; Rodents; Small intestine; Storage; Sucrose; Triglycerides - metabolism
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0126823

Dietary fat absorption by the small intestine is a multistep process that regulates the uptake and delivery of essential nutrients and energy. One step of this process is the temporary storage of dietary fat in cytoplasmic lipid droplets (CLDs). The storage and mobilization of dietary fat is thought to be regulated by proteins that associate with the CLD; however, mechanistic details of this process are currently unknown. In this study we analyzed the proteome of CLDs isolated from enterocytes harvested from the small intestine of mice following a dietary fat challenge. In this analysis we identified 181 proteins associated with the CLD fraction, of which 37 are associated with known lipid related metabolic pathways. We confirmed the localization of several of these proteins on or around the CLD through confocal and electron microscopy, including perilipin 3, apolipoprotein A-IV, and acyl-CoA synthetase long-chain family member 5. The identification of the enterocyte CLD proteome provides new insight into potential regulators of CLD metabolism and the process of dietary fat absorption.