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Review
. 2021 Sep 28;22(19):10460.
doi: 10.3390/ijms221910460.

Adipose-Derived Lipid-Binding Proteins: The Good, the Bad and the Metabolic Diseases

Laurie Frances  1   2 , Geneviève Tavernier  1   2 , Nathalie Viguerie  1   2
Affiliations
Review

Adipose-Derived Lipid-Binding Proteins: The Good, the Bad and the Metabolic Diseases

Laurie Frances et al. Int J Mol Sci. .

Abstract

Adipose tissue releases a large range of bioactive factors called adipokines, many of which are involved in inflammation, glucose homeostasis and lipid metabolism. Under pathological conditions such as obesity, most of the adipokines are upregulated and considered as deleterious, due to their pro-inflammatory, pro-atherosclerotic or pro-diabetic properties, while only a few are downregulated and would be designated as beneficial adipokines, thanks to their counteracting properties against the onset of comorbidities. This review focuses on six adipose-derived lipid-binding proteins that have emerged as key factors in the development of obesity and diabetes: Retinol binding protein 4 (RBP4), Fatty acid binding protein 4 (FABP4), Apolipoprotein D (APOD), Lipocalin-2 (LCN2), Lipocalin-14 (LCN14) and Apolipoprotein M (APOM). These proteins share structural homology and capacity to bind small hydrophobic molecules but display opposite effects on glucose and lipid metabolism. RBP4 and FABP4 are positively associated with metabolic syndrome, while APOD and LCN2 are ubiquitously expressed proteins with deleterious or beneficial effects, depending on their anatomical site of expression. LCN14 and APOM have been recently identified as adipokines associated with healthy metabolism. Recent findings on these lipid-binding proteins exhibiting detrimental or protective roles in human and murine metabolism and their involvement in metabolic diseases are also discussed.

Keywords: adipokine; adipose tissue; apolipoprotein; calycin; cardiovascular disease; diabetes; lipocalin; metabolic syndrome.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic structures of the lipocalin and fatty acid binding protein family (adapted from [4]). (A) Lipocalin structure. The β-strands forming the β-barrel are represented as arrows labeled A–H and the loops as circular lines labeled L1–L7. The short N-terminus 310-helix and the C-terminus α-helix and short β-strand are also represented. Grey background represents hydrogen bonds between strands. Dotted squares surround the three structurally conserved regions of kernel lipocalins. (B) Fatty acid binding protein structure. The β-strands are represented as arrows labeled A–J and the loops as circular lines labeled L1–L9. Two conserved α-helixes in loop L1 are shown as α1 and α2. The N-terminus 310-helix and the C-terminus are also represented. Grey background represents hydrogen bonds between strands.
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