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

2021 ◽  
Vol 22 (19) ◽  
pp. 10460
Author(s):  
Laurie Frances ◽  
Geneviève Tavernier ◽  
Nathalie Viguerie
Keyword(s):  
Lipid Metabolism ◽  
Binding Proteins ◽  
Metabolic Diseases ◽  
Binding Protein ◽  
Lipid Binding ◽  
Retinol Binding Protein ◽  
Anatomical Site ◽  
Fatty Acid Binding ◽  
Obesity And Diabetes ◽  
Lipid Binding Proteins

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.

Lipid-binding proteins and lipoprotein lipase activity in human skeletal muscle: influence of physical activity and gender

2004 ◽  
Vol 97 (4) ◽  
pp. 1209-1218 ◽  
Author(s):  
Bente Kiens ◽  
Carsten Roepstorff ◽  
Jan F. C. Glatz ◽  
Arend Bonen ◽  
Peter Schjerling ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipoprotein Lipase ◽  
Binding Proteins ◽  
Mrna Level ◽  
Lipid Binding ◽  
Mrna Levels ◽  
Training Status ◽  
Fatty Acid Binding ◽  
Muscle Lipid ◽  
Lipid Binding Proteins

The protein and mRNA levels of several muscle lipid-binding proteins and the activity and mRNA level of muscle lipoprotein lipase (mLPL) were investigated in healthy, nonobese, nontrained (NT), moderately trained, and endurance-trained (ET) women and men. FAT/CD36 protein level was 49% higher ( P < 0.05) in women than in men, irrespective of training status, whereas FAT/CD36 mRNA was only higher ( P < 0.05) in women than in men in NT subjects (85%). Plasma membrane-bound fatty acid binding protein (FABPpm) content was higher in ET men compared with all other groups, whereas training status did not affect FABPpm content in women. FABPpm mRNA was higher ( P < 0.05) in NT women than in ET women and NT men. mLPL activity was not different between gender, but mLPL mRNA was 160% higher ( P < 0.001) in women than in men. mLPL activity was 48% higher ( P < 0.05) in ET than in NT subjects, irrespective of gender, in accordance with 49% higher ( P < 0.05) mLPL mRNA in ET than in NT subjects. A 90-min exercise bout induced an increase ( P < 0.05) in FAT/CD36 mRNA (∼25%) and FABPpm mRNA (∼15%) levels in all groups. The present study demonstrated that, in the NT state, women had higher muscle mRNA levels of several proteins related to muscle lipid metabolism compared with men. In the ET state, only the gender difference in mLPL mRNA persisted. FAT/CD36 protein in muscle was higher in women than in men, irrespective of training status. These findings may help explain gender differences in lipid metabolism and, furthermore, suggest that the balance between gene transcription, translation, and possibly breakdown of several proteins in muscle lipid metabolism depend on gender.

Insect Juvenile Hormone Binding Protein Shows Ancestral Fold Present in Human Lipid-Binding Proteins

2008 ◽  
Vol 377 (3) ◽  
pp. 870-881 ◽  
Author(s):  
Robert Kolodziejczyk ◽  
Grzegorz Bujacz ◽  
Michał Jakób ◽  
Andrzej Ożyhar ◽  
Mariusz Jaskolski ◽  
...  
Keyword(s):  
Juvenile Hormone ◽  
Binding Proteins ◽  
Binding Protein ◽  
Lipid Binding ◽  
Hormone Binding ◽  
Juvenile Hormone Binding Protein ◽  
Hormone Binding Protein ◽  
Lipid Binding Proteins

Cellular lipid binding proteins as facilitators and regulators of lipid metabolism

2002 ◽  
pp. 3-7 ◽  
Author(s):  
Jan F. C. Glatz ◽  
Joost J. F. P. Luiken ◽  
Marc van Bilsen ◽  
Ger J. van der Vusse
Keyword(s):  
Lipid Metabolism ◽  
Binding Proteins ◽  
Lipid Binding ◽  
Cellular Lipid ◽  
Lipid Binding Proteins

Predicting and Analyzing Lipid-Binding Proteins Using an Efficient Physicochemical Property Mining Method

2013 ◽  
Vol 421 ◽  
pp. 313-318
Author(s):  
Hui Ling Huang ◽  
Yi Fan Liou ◽  
Hua Chin Lee ◽  
Phasit Charoenkwan ◽  
Chao Di Chang ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Binding Proteins ◽  
Metabolic Diseases ◽  
Alpha Helix ◽  
Biochemical Properties ◽  
Lipid Binding ◽  
Support Vector ◽  
Data Set ◽  
Feature Vectors ◽  
Lipid Binding Proteins

Lipid-binding proteinsjoin many important biological processes. Lipid-binding proteins are highly related to diseases, such as metabolic diseases, cancer and autoimmune diseases. The existed studies of predictinglipid-binding functions or predictinglipid-binding sites, but notidentify the lipid-binding proteins ornot lipid-binding proteins.This study purpose a systematic approach to identify a small set of physicochemical and biochemical properties in AAindex database to design support vector machine (SVM) based classifier for predicting and analyzing lipid-binding proteins. The merits of this study are three-fold: First, we establish a data set of lipid-binding proteins collected from SwissProt utilizing the gene ontology (GO) annotation terms. Secondly, utilize an efficient genetic algorithm based optimization method IBCGA to select an informative set of feature vectors of representing sequences from the viewpoint of machine learning. Thirdly, analyze the selected feature vectors to identify the related physicochemical properties which may affect the binding mechanism oflipid-binding proteins. In this study, to overcome the unbalanced dataset problem caused from the number of putative negative dataset (537,346) being almost 530 times to that of positive dataset (1,053), a dataset determining technique is proposed.Then the dataset is applied to make a high performance classifier. The prediction accuracy of independent test is 77.75% using 18 properties. The selected 18 properties may divide into 6 groupings:alpha and turn propensities, beta propensity, Composition, Hydrophobicity, Physicochemical properties and other properties.Hydrophobicity and alpha-helix are most relative to lipid-binding protein.

scholarly journals The role of sterol carrier protein2 and other hepatic lipid-binding proteins in bile-acid biosynthesis

1986 ◽  
Vol 238 (3) ◽  
pp. 879-884 ◽  
Author(s):  
B Lidström-Olsson ◽  
K Wikvall
Keyword(s):  
Bile Acid ◽  
Binding Proteins ◽  
Glutathione Transferase ◽  
Lipid Binding ◽  
Regulatory Function ◽  
Acid Biosynthesis ◽  
Fatty Acid Binding ◽  
Bile Acid Biosynthesis ◽  
Lipid Binding Proteins

The ability of different lipid-binding proteins in liver cytosol to affect enzyme activities in bile-acid biosynthesis was studied in whole microsomes (microsomal fractions) and mitochondria and in purified enzyme systems. Sterol carrier protein2 stimulated the 7 alpha-hydroxylation of cholesterol and the 12 alpha-hydroxylation of 5 beta-cholestane-3 alpha, 7 alpha-diol in microsomes and the 26-hydroxylation of cholesterol in mitochondria 2-3-fold. It also stimulated the oxidation of 5-cholestene-3 beta, 7 alpha-diol into 7 alpha-hydroxy-4-cholesten-3-one in microsomes. The stimulatory effect of sterol carrier protein2 was much less with purified cholesterol 7 alpha- and 26-hydroxylase systems than with microsomes and mitochondria. No stimulatory effect of sterol carrier protein2 was observed with purified 12 alpha-hydroxylase and 3 beta-hydroxy-delta 5-C27-steroid oxidoreductase. Sterol carrier protein (fatty-acid-binding protein), ‘DEAE-peak I protein’ [Dempsey, McCoy, Baker, Dimitriadou-Vafiadou, Lorsbach & Howards (1981) J. Biol. Chem. 256, 1867-1873], ligandin (glutathione transferase B) and serum albumin had no marked stimulatory effects in either crude or in purified systems. The results suggest that sterol carrier protein2 facilitates the introduction of the less-polar substrates in bile-acid biosynthesis to the membrane-bound enzymes in crude systems in vitro. The broad substrate specificity appears, however, not to be consistent with a specific regulatory function for sterol carrier protein2 in bile-acid biosynthesis.

scholarly journals Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode

2019 ◽  
Vol 39 (7) ◽  
Author(s):  
Marina Ibáñez-Shimabukuro ◽  
M. Florencia Rey-Burusco ◽  
Mads Gabrielsen ◽  
Gisela R. Franchini ◽  
Alan Riboldi-Tunnicliffe ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Binding Proteins ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Structural Features ◽  
Lipid Binding ◽  
Head Group ◽  
Resonance Spectroscopy ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

AbstractIntracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid ligand in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes.

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