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Article ; Online: Loss of L-FABP, SCP-2/SCP-x, or both induces hepatic lipid accumulation in female mice.

Martin, Gregory G / Atshaves, Barbara P / Landrock, Kerstin K / Landrock, Danilo / Schroeder, Friedhelm / Kier, Ann B

2015 Volume 580, Page(s) 41–49

Abstract: Although roles for both sterol carrier protein-2/sterol carrier protein-x (SCP-2/SCP-x) and liver fatty acid binding protein (L-FABP) have been proposed in hepatic lipid accumulation, individually ablating these genes has been complicated by concomitant ... ...

Abstract	Although roles for both sterol carrier protein-2/sterol carrier protein-x (SCP-2/SCP-x) and liver fatty acid binding protein (L-FABP) have been proposed in hepatic lipid accumulation, individually ablating these genes has been complicated by concomitant alterations in the other gene product(s). For example, ablating SCP2/SCP-x induces upregulation of L-FABP in female mice. Therefore, the impact of ablating SCP-2/SCP-x (DKO) or L-FABP (LKO) individually or both together (TKO) was examined in female mice. Loss of SCP-2/SCP-x (DKO, TKO) more so than loss of L-FABP alone (LKO) increased hepatic total lipid and total cholesterol content, especially cholesteryl ester. Hepatic accumulation of nonesterified long chain fatty acids (LCFA) and phospholipids occurred only in DKO and TKO mice. Loss of SCP-2/SCP-x (DKO, TKO) increased serum total lipid primarily by increasing triglycerides. Altered hepatic level of proteins involved in cholesterol uptake, efflux, and/or secretion was observed, but did not compensate for the loss of L-FABP, SCP-2/SCP-x or both. However, synergistic responses were not seen with the combinatorial knock out animals-suggesting that inhibiting SCP-2/SCP-x is more correlative with hepatic dysfunction than L-FABP. The DKO- and TKO-induced hepatic accumulation of cholesterol and long chain fatty acids shared significant phenotypic similarities with non-alcoholic fatty liver disease (NAFLD).
MeSH term(s)	Animals ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cholesterol/blood ; Cholesterol Esters/blood ; Disease Models, Animal ; Fatty Acid-Binding Proteins/deficiency ; Fatty Acid-Binding Proteins/genetics ; Fatty Acids, Nonesterified/blood ; Female ; Gene Deletion ; Gene Expression ; Lipid Metabolism/genetics ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Non-alcoholic Fatty Liver Disease/genetics ; Non-alcoholic Fatty Liver Disease/metabolism ; Non-alcoholic Fatty Liver Disease/pathology ; Phospholipids/blood ; Triglycerides/blood
Chemical Substances	Carrier Proteins ; Cholesterol Esters ; Fabp1 protein, mouse ; Fatty Acid-Binding Proteins ; Fatty Acids, Nonesterified ; Phospholipids ; Triglycerides ; sterol carrier proteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2015-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2015.06.009
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Article ; Online: Effect of liver fatty acid binding protein (L-FABP) gene ablation on lipid metabolism in high glucose diet (HGD) pair-fed mice.

McIntosh, Avery L / Atshaves, Barbara P / Martin, Gregory G / Landrock, Danilo / Milligan, Sherrelle / Landrock, Kerstin K / Huang, Huan / Storey, Stephen M / Mackie, John / Schroeder, Friedhelm / Kier, Ann B

Biochimica et biophysica acta. Molecular and cell biology of lipids

2019 Volume 1864, Issue 7, Page(s) 985–1004

Abstract: Liver fatty acid binding protein (L-FABP) is the major fatty acid binding/"chaperone" protein in hepatic cytosol. Although fatty acids can be derived from the breakdown of dietary fat and glucose, relatively little is known regarding the impact of L-FABP ...

Abstract	Liver fatty acid binding protein (L-FABP) is the major fatty acid binding/"chaperone" protein in hepatic cytosol. Although fatty acids can be derived from the breakdown of dietary fat and glucose, relatively little is known regarding the impact of L-FABP on phenotype in the context of high dietary glucose. Potential impact was examined in wild-type (WT) and Lfabp gene ablated (LKO) female mice fed either a control or pair-fed high glucose diet (HGD). WT mice fed HGD alone exhibited decreased whole body weight gain and weight gain/kcal food consumed-both as reduced lean tissue mass (LTM) and fat tissue mass (FTM). Conversely, LKO alone increased weight gain, lean tissue mass, and fat tissue mass while decreasing serum β-hydroxybutyrate (indicative of hepatic fatty acid oxidation)-regardless of diet. Both LKO alone and HGD alone significantly altered the serum lipoprotein profile and increased triacylglycerol (TG), but in HGD mice the LKO did not further exacerbate serum TG content. HGD had little effect on hepatic lipid composition in WT mice, but prevented the LKO-induced selective increase in hepatic phospholipid, free-cholesterol and cholesteryl-ester. Taken together, these findings suggest that high glucose diet diminished the effects of LKO on the whole body and lipid phenotype of these mice.
MeSH term(s)	Animals ; Cholesterol/metabolism ; Diet ; Fatty Acid-Binding Proteins/deficiency ; Fatty Acid-Binding Proteins/genetics ; Female ; Glucose/pharmacology ; Lipid Metabolism ; Liver/metabolism ; Mice ; Phospholipids/metabolism ; Triglycerides/metabolism ; Weight Gain
Chemical Substances	Fatty Acid-Binding Proteins ; Phospholipids ; Triglycerides ; Cholesterol (97C5T2UQ7J) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2019-03-22
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2019.03.009
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Article ; Online: Plin2 inhibits cellular glucose uptake through interactions with SNAP23, a SNARE complex protein.

Senthivinayagam, Subramanian / McIntosh, Avery L / Moon, Kenneth C / Atshaves, Barbara P

PloS one

2013 Volume 8, Issue 9, Page(s) e73696

Abstract: Although a link between excess lipid storage and aberrant glucose metabolism has been recognized for many years, little is known what role lipid storage droplets and associated proteins such as Plin2 play in managing cellular glucose levels. To address ... ...

Abstract	Although a link between excess lipid storage and aberrant glucose metabolism has been recognized for many years, little is known what role lipid storage droplets and associated proteins such as Plin2 play in managing cellular glucose levels. To address this issue, the influence of Plin2 on glucose uptake was examined using 2-NBD-Glucose and [(3)H]-2-deoxyglucose to show that insulin-mediated glucose uptake was decreased 1.7- and 1.8-fold, respectively in L cell fibroblasts overexpressing Plin2. Conversely, suppression of Plin2 levels by RNAi-mediated knockdown increased 2-NBD-Glucose uptake several fold in transfected L cells and differentiated 3T3-L1 cells. The effect of Plin2 expression on proteins involved in glucose uptake and transport was also examined. Expression of the SNARE protein SNAP23 was increased 1.6-fold while levels of syntaxin-5 were decreased 1.7-fold in Plin2 overexpression cells with no significant changes observed in lipid droplet associated proteins Plin1 or FSP27 or with the insulin receptor, GLUT1, or VAMP4. FRET experiments revealed a close proximity of Plin2 to SNAP23 on lipid droplets to within an intramolecular distance of 51 Å. The extent of targeting of SNAP23 to lipid droplets was determined by co-localization and co-immunoprecipitation experiments to show increased partitioning of SNAP23 to lipid droplets when Plin2 was overexpressed. Taken together, these results suggest that Plin2 inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets. In summary, the current study for the first time provides direct evidence for the role of Plin2 in mediating cellular glucose uptake.
MeSH term(s)	3T3-L1 Cells ; Animals ; Biological Transport/drug effects ; Carbocyanines/chemistry ; Carbocyanines/metabolism ; Cytochalasin B/pharmacology ; Cytoplasmic Granules/metabolism ; Deoxyglucose/metabolism ; Deoxyglucose/pharmacokinetics ; Fibroblasts/cytology ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Fluorescence Resonance Energy Transfer ; Glucose/metabolism ; Glucose/pharmacokinetics ; Glucose Transporter Type 1/metabolism ; Immunoblotting ; Insulin/pharmacology ; L Cells ; Lipids/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Microscopy, Confocal ; Models, Biological ; Perilipin-2 ; Protein Binding ; Qb-SNARE Proteins/genetics ; Qb-SNARE Proteins/metabolism ; Qc-SNARE Proteins/genetics ; Qc-SNARE Proteins/metabolism ; RNA Interference
Chemical Substances	Carbocyanines ; Glucose Transporter Type 1 ; Insulin ; Lipids ; Membrane Proteins ; Perilipin-2 ; Plin2 protein, mouse ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; Slc2a1 protein, mouse ; Snap23 protein, mouse ; cyanine dye 3 ; cyanine dye 5 ; Cytochalasin B (3CHI920QS7) ; Deoxyglucose (9G2MP84A8W) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2013-09-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0073696
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Article ; Online: Intracellular lipid droplets contain dynamic pools of sphingomyelin: ADRP binds phospholipids with high affinity.

McIntosh, Avery L / Storey, Stephen M / Atshaves, Barbara P

Lipids

2010 Volume 45, Issue 6, Page(s) 465–477

Abstract: During the last several years, intracellular lipid droplets have become the focus of intense study. No longer an inert bystander, the lipid droplet is now known as a dynamic organelle contributing lipids to many cellular events. However, while the ... ...

Abstract	During the last several years, intracellular lipid droplets have become the focus of intense study. No longer an inert bystander, the lipid droplet is now known as a dynamic organelle contributing lipids to many cellular events. However, while the dynamics of cholesterol efflux from both the plasma membrane and lipid droplets have been studied, less is known regarding the efflux of sphingomyelin from these membranes. In order to address this issue, sphingomyelin efflux kinetics and binding affinities from different intracellular pools were examined. When compared to the plasma membrane, lipid droplets had a smaller exchangeable sphingomyelin efflux pool and the time required to efflux that pool was significantly shorter. Fluorescence binding assays revealed that proteins in the plasma membrane and lipid droplet pool bound sphingomyelin with high affinity. Further characterization identified adipose differentiation-related protein (ADRP) as one of the sphingomyelin binding proteins in the lipid droplet fraction and revealed that ADRP demonstrated saturable binding to 6-((N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-hexanoyl)sphingosyl-phosphocholine (NBD-sphingomyelin) and also 2-(6-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-1-hexadecanoyl-sn-glycero-3-phosphocholine (NBD-phosphatidylcholine) with binding affinities in the nanomolar range. Taken together, these results suggest that lipid droplet associated proteins such as ADRP may play a significant role in regulating the intracellular distribution of phospholipids and lipids in general. Overall, insights from the present work suggest new and important roles for lipid droplets and ADRP in phospholipid metabolism.
MeSH term(s)	4-Chloro-7-nitrobenzofurazan/analogs & derivatives ; 4-Chloro-7-nitrobenzofurazan/analysis ; 4-Chloro-7-nitrobenzofurazan/chemistry ; 4-Chloro-7-nitrobenzofurazan/metabolism ; Animals ; Binding Sites ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Cells, Cultured ; Lipid Metabolism ; Lipids/chemistry ; Membrane Proteins/metabolism ; Mice ; Microscopy, Fluorescence ; Perilipin-2 ; Phosphatidylcholines/chemistry ; Phosphatidylcholines/metabolism ; Phospholipids/metabolism ; Sphingomyelins/analysis ; Sphingomyelins/chemistry ; Sphingomyelins/metabolism
Chemical Substances	2-(6-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-1-hexadecanoylglycero-3-phosphocholine ; Lipids ; Membrane Proteins ; N-4-nitrobenzo-2-oxa-1,3-diazoleaminocaproyl sphingosylphosphorylcholine ; Perilipin-2 ; Phosphatidylcholines ; Phospholipids ; Plin2 protein, mouse ; Sphingomyelins ; 4-Chloro-7-nitrobenzofurazan (EQF2794IRE)
Language	English
Publishing date	2010-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	241539-2
ISSN	1558-9307 ; 0024-4201
ISSN (online)	1558-9307
ISSN	0024-4201
DOI	10.1007/s11745-010-3424-1
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Article ; Online: Relative contributions of L-FABP, SCP-2/SCP-x, or both to hepatic biliary phenotype of female mice.

Martin, Gregory G / Landrock, Danilo / Landrock, Kerstin K / Howles, Philip N / Atshaves, Barbara P / Kier, Ann B / Schroeder, Friedhelm

Archives of biochemistry and biophysics

2015 Volume 588, Page(s) 25–32

Abstract: Both sterol carrier protein-2/sterol carrier protein-x (SCP-2/SCP-x) and liver fatty acid binding protein (L-FABP) have been proposed to function in hepatobiliary bile acid metabolism/accumulation. To begin to address this issue, the impact of ablating L- ...

Abstract	Both sterol carrier protein-2/sterol carrier protein-x (SCP-2/SCP-x) and liver fatty acid binding protein (L-FABP) have been proposed to function in hepatobiliary bile acid metabolism/accumulation. To begin to address this issue, the impact of ablating L-FABP (LKO) or SCP-2/SCP-x (DKO) individually or both together (TKO) was examined in female mice. Biliary bile acid levels were decreased in LKO, DKO, and TKO mice; however, hepatic bile acid concentration was decreased in LKO mice only. In contrast, biliary phospholipid level was decreased only in TKO mice, while biliary cholesterol levels were unaltered regardless of phenotype. The loss of either or both genes increased hepatic expression of the major bile acid synthetic enzymes (CYP7A1 and/or CYP27A1). Loss of L-FABP and/or SCP-2/SCP-x genes significantly altered the molecular composition of biliary bile acids, but not the proportion of conjugated/unconjugated bile acids or overall bile acid hydrophobicity index. These data suggested that L-FABP was more important in hepatic retention of bile acids, while SCP-2/SCP-x more broadly affected biliary bile acid and phospholipid levels.
MeSH term(s)	Animals ; Bile Acids and Salts/chemistry ; Bile Acids and Salts/metabolism ; Biliary Tract/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cholesterol/metabolism ; Fatty Acid-Binding Proteins/deficiency ; Fatty Acid-Binding Proteins/genetics ; Fatty Acid-Binding Proteins/metabolism ; Female ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Phenotype ; Phospholipids/metabolism
Chemical Substances	Bile Acids and Salts ; Carrier Proteins ; Fabp1 protein, mouse ; Fatty Acid-Binding Proteins ; Phospholipids ; sterol carrier proteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2015-11-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2015.10.018
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Article ; Online: Structural and functional assessment of perilipin 2 lipid binding domain(s).

Najt, Charles P / Lwande, Joel S / McIntosh, Avery L / Senthivinayagam, Subramanian / Gupta, Shipra / Kuhn, Leslie A / Atshaves, Barbara P

Biochemistry

2014 Volume 53, Issue 45, Page(s) 7051–7066

Abstract: Although perilipin 2 (Plin2) has been shown to bind lipids with high affinity, the Plin2 lipid binding site has yet to be defined. This is of interest since Plin2's affinity for lipids has been suggested to be important for lipid droplet biogenesis and ... ...

Abstract	Although perilipin 2 (Plin2) has been shown to bind lipids with high affinity, the Plin2 lipid binding site has yet to be defined. This is of interest since Plin2's affinity for lipids has been suggested to be important for lipid droplet biogenesis and intracellular triacylglycerol accumulation. To define these regions, mouse Plin2 and several deletion mutants expressed as recombinant proteins and in mammalian cells were assessed by molecular modeling, fluorescence binding, circular dichroic, and fluorescence resonance energy transfer techniques to identify the structural and functional requirements for lipid binding. Major findings of this study indicate (1) the N-terminal PAT domain does not bind cholesterol or stearic acid; (2) Plin2 residues 119-251, containing helix α4, the α-β domain, and part of helix α6 form a Plin3-like cleft found to be important for highest affinity lipid binding; (3) both stearic acid and cholesterol interact favorably with the Plin2 cleft formed by conserved residues in helix α6 and adjacent strands, which is common to all the active lipid-binding constructs; and (4) discrete targeting of the Plin2 mutants to lipid droplets supports Plin2 containing two independent, nonoverlapping lipid droplet targeting domains in its central and C-terminal sequences. Thus, the current work reveals specific domains responsible for Plin2-lipid interactions that involves the protein's lipid binding and targeting functions.
MeSH term(s)	Animals ; Binding Sites/physiology ; Membrane Lipids/chemistry ; Membrane Lipids/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/physiology ; Mice ; Perilipin-2 ; Protein Structure, Secondary ; Protein Structure, Tertiary
Chemical Substances	Membrane Lipids ; Membrane Proteins ; Perilipin-2 ; Plin2 protein, mouse
Language	English
Publishing date	2014-11-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi500918m
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Article ; Online: Ablating L-FABP in SCP-2/SCP-x null mice impairs bile acid metabolism and biliary HDL-cholesterol secretion.

Martin, Gregory G / Atshaves, Barbara P / Landrock, Kerstin K / Landrock, Danilo / Storey, Stephen M / Howles, Philip N / Kier, Ann B / Schroeder, Friedhelm

American journal of physiology. Gastrointestinal and liver physiology

2014 Volume 307, Issue 11, Page(s) G1130–43

Abstract: On the basis of their abilities to bind bile acids and/or cholesterol, the physiological role(s) of liver fatty acid-binding protein (L-FABP) and sterol carrier protein (SCP) 2/SCP-x (SCP-2/SCP-x) gene products in biliary bile acid and cholesterol ... ...

Abstract	On the basis of their abilities to bind bile acids and/or cholesterol, the physiological role(s) of liver fatty acid-binding protein (L-FABP) and sterol carrier protein (SCP) 2/SCP-x (SCP-2/SCP-x) gene products in biliary bile acid and cholesterol formation was examined in gene-ablated male mice. L-FABP (LKO) or L-FABP/SCP-2/SCP-x [triple-knockout (TKO)] ablation markedly decreased hepatic bile acid concentration, while SCP-2/SCP-x [double-knockout (DKO)] ablation alone had no effect. In contrast, LKO increased biliary bile acid, while DKO and TKO had no effect on biliary bile acid levels. LKO and DKO also altered biliary bile acid composition to increase bile acid hydrophobicity. Furthermore, LKO and TKO decreased hepatic uptake and biliary secretion of high-density lipoprotein (HDL)-derived 22-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-23,24-bisnor-5-cholen-3β-ol (NBD-cholesterol), while DKO alone had no effect. Finally, LKO and, to a lesser extent, DKO decreased most indexes contributing to cholesterol solubility in biliary bile. These results suggest different, but complementary, roles for L-FABP and SCP-2/SCP-x in biliary bile acid and cholesterol formation. L-FABP appears to function more in hepatic retention of bile acids as well as hepatic uptake and biliary secretion of HDL-cholesterol. Conversely, SCP-2/SCP-x may function more in formation and biliary secretion of bile acid, with less impact on hepatic uptake or biliary secretion of HDL-cholesterol.
MeSH term(s)	Animals ; Bile/metabolism ; Bile Acids and Salts/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/physiology ; Cholesterol/metabolism ; Cholesterol, HDL/metabolism ; Fatty Acid-Binding Proteins/genetics ; Fatty Acid-Binding Proteins/physiology ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Phospholipids/metabolism
Chemical Substances	Bile Acids and Salts ; Carrier Proteins ; Cholesterol, HDL ; Fabp1 protein, mouse ; Fatty Acid-Binding Proteins ; Phospholipids ; sterol carrier proteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2014-10-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603840-2
ISSN	1522-1547 ; 0193-1857
ISSN (online)	1522-1547
ISSN	0193-1857
DOI	10.1152/ajpgi.00209.2014
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Article ; Online: The phospholipid monolayer associated with perilipin-enriched lipid droplets is a highly organized rigid membrane structure.

Storey, Stephen M / McIntosh, Avery L / Senthivinayagam, Subramanian / Moon, Kenneth C / Atshaves, Barbara P

American journal of physiology. Endocrinology and metabolism

2011 Volume 301, Issue 5, Page(s) E991–E1003

Abstract: The significance of lipid droplets (LD) in lipid metabolism, cell signaling, and membrane trafficking is increasingly recognized, yet the role of the LD phospholipid monolayer in LD protein targeting and function remains unknown. To begin to address this ...

Abstract	The significance of lipid droplets (LD) in lipid metabolism, cell signaling, and membrane trafficking is increasingly recognized, yet the role of the LD phospholipid monolayer in LD protein targeting and function remains unknown. To begin to address this issue, two populations of LD were isolated by ConA sepharose affinity chromatography: 1) functionally active LD enriched in perilipin, caveolin-1, and several lipolytic proteins, including ATGL and HSL; and 2) LD enriched in ADRP and TIP47 that contained little to no lipase activity. Coimmunoprecipitation experiments confirmed the close association of caveolin and perilipin and lack of interaction between caveolin and ADRP, in keeping with the separation observed with the ConA procedure. The phospholipid monolayer structure was evaluated to reveal that the perilipin-enriched LD exhibited increased rigidity (less fluidity), as shown by increased cholesterol/phospholipid, Sat/Unsat, and Sat/MUFA ratios. These results were confirmed by DPH-TMA, NBD-cholesterol, and NBD-sphingomyelin fluorescence polarization studies. By structure and organization, the perilipin-enriched LD most closely resembled the adipocyte PM. In contrast, the ADRP/TIP47-enriched LD contained a more fluid monolayer membrane, reflecting decreased polarizations and lipid order based on phospholipid fatty acid analysis. Taken together, results indicate that perilipin and associated lipolytic enzymes target areas in the phospholipid monolayer that are highly organized and rigid, similar in structure to localized areas of the PM where cholesterol and fatty acid uptake and efflux occur.
MeSH term(s)	Adipocytes/chemistry ; Adipocytes/metabolism ; Animals ; Carrier Proteins/metabolism ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cell Membrane Structures/chemistry ; Cell Membrane Structures/metabolism ; Cells, Cultured ; Chromatography, Affinity ; Cytoplasmic Vesicles/chemistry ; Cytoplasmic Vesicles/metabolism ; Lipid Metabolism/physiology ; Male ; Membrane Fluidity/physiology ; Mice ; Mice, Inbred C57BL ; Perilipin-1 ; Phospholipids/chemistry ; Phospholipids/metabolism ; Phosphoproteins/metabolism ; Subcellular Fractions/chemistry ; Subcellular Fractions/metabolism
Chemical Substances	Carrier Proteins ; Perilipin-1 ; Phospholipids ; Phosphoproteins
Language	English
Publishing date	2011-08-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603841-4
ISSN	1522-1555 ; 0193-1849
ISSN (online)	1522-1555
ISSN	0193-1849
DOI	10.1152/ajpendo.00109.2011
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Article ; Online: Plin2 inhibits cellular glucose uptake through interactions with SNAP23, a SNARE complex protein.

Subramanian Senthivinayagam / Avery L McIntosh / Kenneth C Moon / Barbara P Atshaves

PLoS ONE, Vol 8, Iss 9, p e

2013 Volume 73696

Abstract	Although a link between excess lipid storage and aberrant glucose metabolism has been recognized for many years, little is known what role lipid storage droplets and associated proteins such as Plin2 play in managing cellular glucose levels. To address this issue, the influence of Plin2 on glucose uptake was examined using 2-NBD-Glucose and [(3)H]-2-deoxyglucose to show that insulin-mediated glucose uptake was decreased 1.7- and 1.8-fold, respectively in L cell fibroblasts overexpressing Plin2. Conversely, suppression of Plin2 levels by RNAi-mediated knockdown increased 2-NBD-Glucose uptake several fold in transfected L cells and differentiated 3T3-L1 cells. The effect of Plin2 expression on proteins involved in glucose uptake and transport was also examined. Expression of the SNARE protein SNAP23 was increased 1.6-fold while levels of syntaxin-5 were decreased 1.7-fold in Plin2 overexpression cells with no significant changes observed in lipid droplet associated proteins Plin1 or FSP27 or with the insulin receptor, GLUT1, or VAMP4. FRET experiments revealed a close proximity of Plin2 to SNAP23 on lipid droplets to within an intramolecular distance of 51 Å. The extent of targeting of SNAP23 to lipid droplets was determined by co-localization and co-immunoprecipitation experiments to show increased partitioning of SNAP23 to lipid droplets when Plin2 was overexpressed. Taken together, these results suggest that Plin2 inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets. In summary, the current study for the first time provides direct evidence for the role of Plin2 in mediating cellular glucose uptake.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Liver-specific loss of Perilipin 2 alleviates diet-induced hepatic steatosis, inflammation, and fibrosis.

Najt, Charles P / Senthivinayagam, Subramanian / Aljazi, Mohammad B / Fader, Kelly A / Olenic, Sandra D / Brock, Julienne R L / Lydic, Todd A / Jones, A Daniel / Atshaves, Barbara P

American journal of physiology. Gastrointestinal and liver physiology

2016 Volume 310, Issue 9, Page(s) G726–38

Abstract: Hepatic inflammation and fibrosis are key elements in the pathogenesis of nonalcoholic steatohepatitis (NASH), a progressive liver disease initiated by excess hepatic lipid accumulation. Lipid droplet protein Perilipin 2 (Plin2) alleviates dietary- ... ...

Abstract	Hepatic inflammation and fibrosis are key elements in the pathogenesis of nonalcoholic steatohepatitis (NASH), a progressive liver disease initiated by excess hepatic lipid accumulation. Lipid droplet protein Perilipin 2 (Plin2) alleviates dietary-induced hepatic steatosis when globally ablated; however, its role in the progression of NASH remains unknown. To investigate this further, we challenged Plin2 liver-specific knockout mice (designated L-KO) and their respective wild-type (WT) controls with a methionine-choline-deficient (MCD) diet for 15 days to induce a NASH phenotype of increased hepatic triglyceride levels through impaired phosphatidylcholine (PC) synthesis and very-low-density lipoprotein (VLDL) secretion. Results on liver weights, body weights, fat tissue mass, and histology in WT and L-KO mice fed the MCD diet revealed signs of hepatic steatosis, fibrosis, and inflammation; however, these effects were blunted in L-KO mice. In addition, levels of PC and VLDL were unchanged, and hepatic steatosis was reduced in L-KO mice fed the MCD diet, due in part to an increase in remodeling of PE to PC via the enzyme phosphatidylethanolamine N-methyltransferase (PEMT). These mice also exhibited decreased hepatic expression of proinflammatory markers cyclooxygenase 2, IL-6, TNF-α, IL-1β, and reduced expression of endoplasmic reticulum (ER) stress proteins C/EBP homologous protein and cleaved caspase-1. Taken together, these results suggest that Plin2 liver-specific ablation alleviates diet-induced hepatic steatosis and inflammation via a PEMT-mediated mechanism that involves compensatory changes in proteins involved in phospholipid remodeling, inflammation, and ER stress that work to alleviate diet-induced NASH. Overall, these findings support a role for Plin2 as a target for NASH therapy.
MeSH term(s)	Animals ; CCAAT-Enhancer-Binding Proteins/genetics ; CCAAT-Enhancer-Binding Proteins/metabolism ; Caspase 1/genetics ; Caspase 1/metabolism ; Choline Deficiency/complications ; Cytokines/genetics ; Cytokines/metabolism ; Lipoproteins, LDL/metabolism ; Liver/metabolism ; Liver Cirrhosis/etiology ; Liver Cirrhosis/genetics ; Liver Cirrhosis/metabolism ; Methionine/deficiency ; Mice ; Mice, Inbred C57BL ; Non-alcoholic Fatty Liver Disease/etiology ; Non-alcoholic Fatty Liver Disease/genetics ; Non-alcoholic Fatty Liver Disease/metabolism ; Perilipin-2/genetics ; Perilipin-2/metabolism ; Phosphatidylcholines/metabolism ; Phosphatidylethanolamine N-Methyltransferase/metabolism ; Triglycerides/metabolism
Chemical Substances	CCAAT-Enhancer-Binding Proteins ; Cytokines ; Lipoproteins, LDL ; Perilipin-2 ; Phosphatidylcholines ; Plin2 protein, mouse ; Triglycerides ; Methionine (AE28F7PNPL) ; PEMT protein, mouse (EC 2.1.1.17) ; Phosphatidylethanolamine N-Methyltransferase (EC 2.1.1.17) ; Caspase 1 (EC 3.4.22.36)
Language	English
Publishing date	2016--01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603840-2
ISSN	1522-1547 ; 0193-1857
ISSN (online)	1522-1547
ISSN	0193-1857
DOI	10.1152/ajpgi.00436.2015
Database	MEDical Literature Analysis and Retrieval System OnLINE

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