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Adipocyte lipopolysaccharide binding protein ( LBP ) is linked to a specific lipidomic signature
Author(s) -
MorenoNavarrete José María,
Jové Mariona,
Padró Teresa,
Boada Jordi,
Ortega Francisco,
Ricart Wifredo,
Pamplona Reinald,
Badimón Lina,
PorteroOtín Manuel,
FernándezReal José Manuel
Publication year - 2017
Publication title -
obesity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.438
H-Index - 199
eISSN - 1930-739X
pISSN - 1930-7381
DOI - 10.1002/oby.21711
Subject(s) - lipidome , lipidomics , adipose tissue , sphingomyelin , chemistry , adipocyte , inflammation , medicine , endocrinology , adipose triglyceride lipase , biology , biochemistry , cholesterol , lipolysis
Objective Lipopolysaccharide binding protein (LBP) is part of a family of structurally and functionally related lipid transfer proteins. This study aimed to investigate the associations of LBP with the lipid composition of human adipose tissue. Methods Lipidomic analysis was performed in whole adipose tissue. To validate the associations found, LBP was knocked down (KD) in 3T3‐L1 adipocytes, and lipidomic profile was evaluated by nontargeted lipidomics. Results LBP gene expression was negatively associated with phosphatidylcholine, phosphatidylserine, and sphingomyelin relative abundance in vivo . LBP expression was also decreased in those samples with the highest docosahexanoic content, implicated in the resolution of inflammation. The KD of LBP (by ∼70%) led to sharp changes in the lipidome of adipocytes. Of note, specific plasmalogen species PE(O‐16:0/22:5), PE(38:2), odd chain glycerolipids, and cholesteryl linoleate were upregulated by LBP KD. In contrast, GM3 gangliosides, several ceramides, a triacylglycerol potentially containing arachidonate, and cholesteryl palmitate were downregulated by LBP KD. Conclusions LBP seems to play a role in the regulation of lipid composition of adipose tissue linked to resilience to inflammation.