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Characterization of the proteome of cytoplamic lipid droplets in enterocytes in response to dietary fat
Author(s) -
D'Aquila Theresa,
Sirohi Devika,
Kuhn Richard J.,
Buhman Kimberly K.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1020.3
Subject(s) - biochemistry , lipid droplet , lipid metabolism , proteome , fatty acid binding protein , apolipoprotein b , biology , chemistry , cholesterol , gene
Cytoplasmic lipid droplets (CLDs) are present and dynamically regulated in enterocytes, the absorptive cells of the intestine, in response to dietary fat. CLDs have a neutral lipid core surrounded by a phospholipid monolayer with associated proteins that have diverse cellular functions. The objective of this study was to determine the proteome of CLDs in enterocytes following a high fat dietary challenge. We isolated enterocytes from C57BL6 mice, two hours after a 200 μl olive oil gavage. The CLD fraction was isolated via sucrose gradient ultracentrifugation and analyzed by HPLC MS/MS. We identified 280 proteins in the CLD fraction representing proteins involved in diverse cellular functions including lipid and glucose metabolism. Lipid metabolism proteins identified include: perilipin 3, abhydrolase domain containing 8, acyl CoA synthetase 5, intestinal fatty acid binding protein (fabp), liver fabp, apolipoprotein AIV, and phospholipase c. Glucose metabolism proteins identified include: glucose 1,6 bisphosphate synthase, glycogen phosphorylase, and pyruvate kinase. The proteome of CLDs in enterocytes following a high fat dietary challenge highlights key proteins involved in the process of dietary fat absorption.