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Готові списки джерел за темами / Intracellular lipid-binding protein / Статті в журналах

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Статті в журналах з теми "Intracellular lipid-binding protein"

Автор: Grafiati

Опубліковано: 11 березня 2023

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1

Soffientini, Ugo, and Annette Graham. "Intracellular cholesterol transport proteins: roles in health and disease." Clinical Science 130, no. 21 (2016): 1843–59. http://dx.doi.org/10.1042/cs20160339.

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Effective cholesterol homoeostasis is essential in maintaining cellular function, and this is achieved by a network of lipid-responsive nuclear transcription factors, and enzymes, receptors and transporters subject to post-transcriptional and post-translational regulation, whereas loss of these elegant, tightly regulated homoeostatic responses is integral to disease pathologies. Recent data suggest that sterol-binding sensors, exchangers and transporters contribute to regulation of cellular cholesterol homoeostasis and that genetic overexpression or deletion, or mutations, in a number of these

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2

Voelker, Dennis R. "Genetic analysis of intracellular aminoglycerophospholipid traffic." Biochemistry and Cell Biology 82, no. 1 (2004): 156–69. http://dx.doi.org/10.1139/o03-075.

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Inter- and intramembrane phospholipid transport processes are central features of membrane biogenesis and homeostasis. Relatively recent successes in the molecular genetic analysis of aminoglycerophospholipid transport processes in both yeast and mammalian cells are now providing important new information defining specific protein and lipid components that participate in these reactions. Studies focused on phosphatidylserine (PtdSer) transport to the mitochondria reveal that the process is regulated by ubiquitination. In addition, a specific mutation disrupts PtdSer transport between mitochond

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3

Voilquin, Laetitia, Massimo Lodi, Thomas Di Mattia, et al. "STARD3: A Swiss Army Knife for Intracellular Cholesterol Transport." Contact 2 (January 2019): 251525641985673. http://dx.doi.org/10.1177/2515256419856730.

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Intracellular cholesterol transport is a complex process involving specific carrier proteins. Cholesterol-binding proteins, such as the lipid transfer protein steroidogenic acute regulatory-related lipid transfer domain-3 (STARD3), are implicated in cholesterol movements between organelles. Indeed, STARD3 modulates intracellular cholesterol allocation by reducing it from the plasma membrane and favoring its passage from the endoplasmic reticulum (ER) to endosomes, where the protein is localized. STARD3 interacts with ER-anchored partners, notably vesicle-associated membrane protein-associated

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4

Matsumura, Yoshihiro, Nobuhiro Ban, and Nobuya Inagaki. "Aberrant catalytic cycle and impaired lipid transport into intracellular vesicles in ABCA3 mutants associated with nonfatal pediatric interstitial lung disease." American Journal of Physiology-Lung Cellular and Molecular Physiology 295, no. 4 (2008): L698—L707. http://dx.doi.org/10.1152/ajplung.90352.2008.

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The ATP-binding cassette transporter ABCA3 mediates uptake of choline-phospholipids into intracellular vesicles and is essential for surfactant metabolism in lung alveolar type II cells. We have shown previously that ABCA3 mutations in fatal surfactant deficiency impair intracellular localization or ATP hydrolysis of ABCA3 protein. However, the mechanisms underlying the less severe phenotype of patients with ABCA3 mutation are unclear. In this study, we characterized ABCA3 mutant proteins identified in pediatric interstitial lung disease (pILD). E292V (intracellular loop 1), E690K (adjacent to

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5

Lee, Hyo-Geun, Yu-An Lu, Jun-Geon Je, et al. "Effects of Ethanol Extracts from Grateloupia elliptica, a Red Seaweed, and Its Chlorophyll Derivative on 3T3-L1 Adipocytes: Suppression of Lipid Accumulation through Downregulation of Adipogenic Protein Expression." Marine Drugs 19, no. 2 (2021): 91. http://dx.doi.org/10.3390/md19020091.

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Grateloupia elliptica (G. elliptica) is a red seaweed with antioxidant, antidiabetic, anticancer, anti-inflammatory, and anticoagulant activities. However, the anti-obesity activity of G. elliptica has not been fully investigated. Therefore, the effect of G. elliptica ethanol extract on the suppression of intracellular lipid accumulation in 3T3-L1 cells by Oil Red O staining (ORO) was evaluated. Among the eight red seaweeds tested, G. elliptica 60% ethanol extract (GEE) exhibited the highest inhibition of lipid accumulation. GEE was the only extract to successfully suppress lipid accumulation

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6

Titus, Amber R., Ellyse N. Ridgway, Rebecca Douglas, Elena Sánchez Brenes, Elizabeth K. Mann, and Edgar E. Kooijman. "The C-Terminus of Perilipin 3 Shows Distinct Lipid Binding at Phospholipid-Oil-Aqueous Interfaces." Membranes 11, no. 4 (2021): 265. http://dx.doi.org/10.3390/membranes11040265.

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Lipid droplets (LDs) are ubiquitously expressed organelles; the only intracellular organelles that contain a lipid monolayer rather than a bilayer. Proteins localize and bind to this monolayer as they do to intracellular lipid bilayers. The mechanism by which cytosolic LD binding proteins recognize, and bind, to this lipid interface remains poorly understood. Amphipathic α-helix bundles form a common motif that is shared between cytosolic LD binding proteins (e.g., perilipins 2, 3, and 5) and apolipoproteins, such as apoE and apoLp-III, found on lipoprotein particles. Here, we use pendant drop

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7

Scifres, Christina M., Baosheng Chen, D. Michael Nelson, and Yoel Sadovsky. "Fatty Acid Binding Protein 4 Regulates Intracellular Lipid Accumulation in Human Trophoblasts." Journal of Clinical Endocrinology & Metabolism 96, no. 7 (2011): E1083—E1091. http://dx.doi.org/10.1210/jc.2010-2084.

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8

Venkatachalam, Ananda B., Manoj B. Parmar, and Jonathan M. Wright. "Evolution of the duplicated intracellular lipid-binding protein genes of teleost fishes." Molecular Genetics and Genomics 292, no. 4 (2017): 699–727. http://dx.doi.org/10.1007/s00438-017-1313-5.

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9

Kane, Christopher D., Natalie Ribarik Coe, Benjamin Vanlandingham, Peter Krieg, and David A. Bernlohr. "Expression, Purification, and Ligand-Binding Analysis of Recombinant Keratinocyte Lipid-Binding Protein (MAL-1), an Intracellular Lipid-Binding Protein Found Overexpressed in Neoplastic Skin Cells†." Biochemistry 35, no. 9 (1996): 2894–900. http://dx.doi.org/10.1021/bi952476e.

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10

Péresse, Tiphaine, David Kovacs, Mélody Subra, et al. "Molecular and cellular dissection of the oxysterol-binding protein cycle through a fluorescent inhibitor." Journal of Biological Chemistry 295, no. 13 (2020): 4277–88. http://dx.doi.org/10.1074/jbc.ra119.012012.

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ORPphilins are bioactive natural products that strongly and selectively inhibit the growth of some cancer cell lines and are proposed to target intracellular lipid-transfer proteins of the oxysterol-binding protein (OSBP) family. These conserved proteins exchange key lipids, such as cholesterol and phosphatidylinositol 4-phosphate (PI(4)P), between organelle membranes. Among ORPphilins, molecules of the schweinfurthin family interfere with intracellular lipid distribution and metabolism, but their functioning at the molecular level is poorly understood. We report here that cell line sensitivit

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11

Herreros, Judit, Tony Ng, and Giampietro Schiavo. "Lipid Rafts Act as Specialized Domains for Tetanus Toxin Binding and Internalization into Neurons." Molecular Biology of the Cell 12, no. 10 (2001): 2947–60. http://dx.doi.org/10.1091/mbc.12.10.2947.

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Tetanus (TeNT) is a zinc protease that blocks neurotransmission by cleaving the synaptic protein vesicle-associated membrane protein/synaptobrevin. Although its intracellular catalytic activity is well established, the mechanism by which this neurotoxin interacts with the neuronal surface is not known. In this study, we characterize p15s, the first plasma membrane TeNT binding proteins and we show that they are glycosylphosphatidylinositol-anchored glycoproteins in nerve growth factor (NGF)-differentiated PC12 cells, spinal cord cells, and purified motor neurons. We identify p15 as neuronal Th

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12

Kitamata, Manabu, Takehiko Inaba, and Shiro Suetsugu. "The roles of the diversity of amphipathic lipids in shaping membranes by membrane-shaping proteins." Biochemical Society Transactions 48, no. 3 (2020): 837–51. http://dx.doi.org/10.1042/bst20190376.

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Lipid compositions of cells differ according to cell types and intracellular organelles. Phospholipids are major cell membrane lipids and have hydrophilic head groups and hydrophobic fatty acid tails. The cellular lipid membrane without any protein adapts to spherical shapes, and protein binding to the membrane is thought to be required for shaping the membrane for various cellular events. Until recently, modulation of cellular lipid membranes was initially shown to be mediated by proteins recognizing lipid head groups, including the negatively charged ones of phosphatidylserine and phosphoino

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13

Park, Jeong-Eun, Suk-Heung Oh, and Youn-Soo Cha. "Lactobacillus plantarumLG42 Isolated from Gajami Sik-Hae Inhibits Adipogenesis in 3T3-L1 Adipocyte." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/460927.

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We investigated whether lactic acid bacteria isolated from gajami sik-hae (GLAB) are capable of reducing the intracellular lipid accumulation by downregulating the expression of adipogenesis-related genes in differentiated 3T3-L1 cells. The GLAB,Lactobacillus plantarumLG42, significantly decreased the intracellular triglyceride storage and the glycerol-3-phosphate dehydrogenase (GPDH) activity in a dose-dependent manner. mRNA expression of transcription factors like peroxisome proliferator-activated receptor (PPAR)γand CCAAT/enhancer-binding protein (C/EBP)αinvolved in adipogenesis was markedl

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14

Shigematsu, Hideki, Takashi Ebihara, Yasuko Yanagida, Tetsuya Haruyama, Eiry Kobatake, and Masuo Aizawa. "Site-directed lipid modification of IgG-binding protein by intracellular bacterial lipoprotein process." Journal of Biotechnology 75, no. 1 (1999): 23–31. http://dx.doi.org/10.1016/s0168-1656(99)00134-0.

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15

Peretti, Diego, Nili Dahan, Eyal Shimoni, Koret Hirschberg, and Sima Lev. "Coordinated Lipid Transfer between the Endoplasmic Reticulum and the Golgi Complex Requires the VAP Proteins and Is Essential for Golgi-mediated Transport." Molecular Biology of the Cell 19, no. 9 (2008): 3871–84. http://dx.doi.org/10.1091/mbc.e08-05-0498.

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Lipid transport between intracellular organelles is mediated by vesicular and nonvesicular transport mechanisms and is critical for maintaining the identities of different cellular membranes. Nonvesicular lipid transport between the endoplasmic reticulum (ER) and the Golgi complex has been proposed to affect the lipid composition of the Golgi membranes. Here, we show that the integral ER–membrane proteins VAP-A and VAP-B affect the structural and functional integrity of the Golgi complex. Depletion of VAPs by RNA interference reduces the levels of phosphatidylinositol-4-phosphate (PI4P), diacy

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16

Wahlmüller, Felix Christof, Barbora Sokolikova, Daniela Rieger, and Margarethe Geiger. "New lipid interaction partners stimulate the inhibition of activated protein C by cell-penetrating protein C inhibitor." Thrombosis and Haemostasis 111, no. 01 (2014): 41–52. http://dx.doi.org/10.1160/th13-06-0478.

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SummaryProtein C inhibitor (PCI, SerpinA5) is a heparin-binding serpin which can penetrate through cellular membranes. Selected negatively charged phospholipids like unsaturated phosphatidylserine and oxidised phosphatidylethanolamine bind to PCI and stimulate its inhibitory activity towards different proteases. The interaction of phospholipids with PCI might also alter the lipid distribution pattern of blood cells and influence the remodelling of cellular membranes. Here we showed that PCI is an additional binding partner of phosphatidic acid (PA), cardiolipin (CL), and phosphoinositides (PIP

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17

FAIRN, Gregory D., and Christopher R. McMASTER. "Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein-related protein 1 short) in the regulation of vesicular transport." Biochemical Journal 387, no. 3 (2005): 889–96. http://dx.doi.org/10.1042/bj20041915.

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The ORPs (oxysterol-binding-protein-related proteins) constitute an enigmatic family of intracellular lipid receptors that are related through a shared lipid binding domain. Emerging evidence suggests that ORPs relate lipid metabolism to membrane transport. Current data imply that the yeast ORP Kes1p is a negative regulator of Golgi-derived vesicular transport mediated by the essential phosphatidylinositol/phosphatidylcholine transfer protein Sec14p. Inactivation of Kes1p function allows restoration of growth and vesicular transport in cells lacking Sec14p function, and Kes1p function in this

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18

Backer, Jonathan M. "New methods for capturing the mystery lipid, PtdIns5P." Biochemical Journal 428, no. 3 (2010): e1-e2. http://dx.doi.org/10.1042/bj20100688.

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The enormous versatility of phosphatidylinositol as a mediator of intracellular signalling is due to its variable phosphorylation on every combination of the 3′, 4′ and 5′ positions, as well as an even more complex range of phosphorylated products when inositol phosphate is released by phospholipase C activity. The phosphoinositides are produced by distinct enzymes in distinct intracellular membranes, and recruit and regulate downstream signalling proteins containing binding domains [PH (pleckstrin homology), PX (Phox homology), FYVE etc.] that are relatively specific for these lipids. Specifi

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19

Xu, Hongliang, Ann V. Hertzel, Kaylee A. Steen, Qigui Wang, Jill Suttles, and David A. Bernlohr. "Uncoupling Lipid Metabolism from Inflammation through Fatty Acid Binding Protein-Dependent Expression of UCP2." Molecular and Cellular Biology 35, no. 6 (2015): 1055–65. http://dx.doi.org/10.1128/mcb.01122-14.

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Chronic inflammation in obese adipose tissue is linked to endoplasmic reticulum (ER) stress and systemic insulin resistance. Targeted deletion of the murine fatty acid binding protein (FABP4/aP2) uncouples obesity from inflammation although the mechanism underlying this finding has remained enigmatic. Here, we show that inhibition or deletion of FABP4/aP2 in macrophages results in increased intracellular free fatty acids (FFAs) and elevated expression of uncoupling protein 2 (UCP2) without concomitant increases in UCP1 or UCP3. Silencing of UCP2 mRNA in FABP4/aP2-deficient macrophages negated

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20

Rutledge, Angela C., Qiaozhu Su, and Khosrow Adeli. "Apolipoprotein B100 biogenesis: a complex array of intracellular mechanisms regulating folding, stability, and lipoprotein assemblyThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 2 (2010): 251–67. http://dx.doi.org/10.1139/o09-168.

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Apolipoprotein B100 (apoB) is a large amphipathic lipid-binding protein that is synthesized by hepatocytes and used to assemble and stabilize very low density lipoproteins (VLDL). It may have been derived through evolution from other lipid-associating proteins such as microsomal triglyceride transfer protein or vitellogenin. The correct folding of apoB requires assistance from chaperone proteins in co-translational lipidation, disulfide bond formation, and glycosylation. Any impairment in these processes results in co-translational targeting of the misfolded apoB molecule for proteasomal degra

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21

Schindler, Maria, Mareike Pendzialek, Alexander Navarrete Santos, et al. "Maternal Diabetes Leads to Unphysiological High Lipid Accumulation in Rabbit Preimplantation Embryos." Endocrinology 155, no. 4 (2014): 1498–509. http://dx.doi.org/10.1210/en.2013-1760.

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According to the “developmental origin of health and disease” hypothesis, the metabolic set points of glucose and lipid metabolism are determined prenatally. In the case of a diabetic pregnancy, the embryo is exposed to higher glucose and lipid concentrations as early as during preimplantation development. We used the rabbit to study the effect of maternal diabetes type 1 on lipid accumulation and expression of lipogenic markers in preimplantation blastocysts. Accompanied by elevated triglyceride and glucose levels in the maternal blood, embryos from diabetic rabbits showed a massive intracell

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22

Nossoni, Zahra, Zahra Assar, Ipek Yapici, et al. "Structures of holo wild-type human cellular retinol-binding protein II (hCRBPII) bound to retinol and retinal." Acta Crystallographica Section D Biological Crystallography 70, no. 12 (2014): 3226–32. http://dx.doi.org/10.1107/s1399004714023839.

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Cellular retinol-binding proteins (CRBPs) I and II, which are members of the intracellular lipid-binding protein (iLBP) family, are retinoid chaperones that are responsible for the intracellular transport and delivery of both retinol and retinal. Although structures of retinol-bound CRBPI and CRBPII are known, no structure of a retinal-bound CRBP has been reported. In addition, the retinol-bound human CRBPII (hCRBPII) structure shows partial occupancy of a noncanonical conformation of retinol in the binding pocket. Here, the structure of retinal-bound hCRBPII and the structure of retinol-bound

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23

Jo, Youngah, Isamu Z. Hartman, and Russell A. DeBose-Boyd. "Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet–associated endoplasmic reticulum membranes." Molecular Biology of the Cell 24, no. 3 (2013): 169–83. http://dx.doi.org/10.1091/mbc.e12-07-0564.

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Sterol-induced binding to Insigs in endoplasmic reticulum (ER) membranes triggers ubiquitination of the cholesterol biosynthetic enzyme 3-hydroxy-3-methylglutaryl CoA reductase. This ubiquitination, which is mediated by Insig-associated ubiquitin ligases gp78 and Trc8, is obligatory for extraction of reductase from lipid droplet–associated ER membranes into the cytosol for proteasome-mediated, ER-associated degradation (ERAD). In this study, we identify lipid droplet–associated, ancient, ubiquitous protein-1 (Aup1) as one of several proteins that copurify with gp78. RNA interference (RNAi) stu

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24

Chen, Wentao, Jiajia Dong, Lars Plate, et al. "Arylfluorosulfates Inactivate Intracellular Lipid Binding Protein(s) through Chemoselective SuFEx Reaction with a Binding Site Tyr Residue." Journal of the American Chemical Society 138, no. 23 (2016): 7353–64. http://dx.doi.org/10.1021/jacs.6b02960.

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25

Lee, Hyo-Geun, Hyun-Soo Kim, Jun-Geon Je, et al. "Lipid Inhibitory Effect of (−)-loliolide Isolated from Sargassum horneri in 3T3-L1 Adipocytes: Inhibitory Mechanism of Adipose-Specific Proteins." Marine Drugs 19, no. 2 (2021): 96. http://dx.doi.org/10.3390/md19020096.

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Sargassum horneri (S. horneri) is a well-known brown seaweed widely distributed worldwide. Several biological activities of S. horneri have been reported. However, its effects on lipid metabolism and the underlying mechanisms remain elusive. In the present study, we examined the inhibitory effect of the active compound “(−)-loliolide ((6S,7aR)-6-hydroxy-4,4,7a-trimethyl-5,6,7,7a-tetrahydro-1-benzofuran-2(4H)-one (HTT))” from S. horneri extract on lipid accumulation in differentiated adipocytes. MTT assays demonstrated that (−)-loliolide is not toxic to 3T3-L1 adipocytes in a range of concentra

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26

Kang, Jin Ku, Ok-Hee Kim, June Hur, et al. "Increased intracellular Ca2+concentrations prevent membrane localization of PH domains through the formation of Ca2+-phosphoinositides." Proceedings of the National Academy of Sciences 114, no. 45 (2017): 11926–31. http://dx.doi.org/10.1073/pnas.1706489114.

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Insulin resistance, a key etiological factor in metabolic syndrome, is closely linked to ectopic lipid accumulation and increased intracellular Ca2+concentrations in muscle and liver. However, the mechanism by which dysregulated intracellular Ca2+homeostasis causes insulin resistance remains elusive. Here, we show that increased intracellular Ca2+acts as a negative regulator of insulin signaling. Chronic intracellular Ca2+overload in hepatocytes during obesity and hyperlipidemia attenuates the phosphorylation of protein kinase B (Akt) and its key downstream signaling molecules by inhibiting me

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27

Barrett, John, Nahid Saghir, Anna Timanova, Katie Clarke, and Peter M. Brophy. "Characterisation and Properties of an Intracellular Lipid-Binding Protein from the Tapeworm Moniezia expansa." European Journal of Biochemistry 250, no. 2 (1997): 269–75. http://dx.doi.org/10.1111/j.1432-1033.1997.0269a.x.

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Siarheyeva, Alena, and Frances J. Sharom. "The ABC transporter MsbA interacts with lipid A and amphipathic drugs at different sites." Biochemical Journal 419, no. 2 (2009): 317–28. http://dx.doi.org/10.1042/bj20081364.

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MsbA is an essential ABC (ATP-binding cassette) transporter involved in lipid A transport across the cytoplasmic membrane of Gram-negative bacteria. The protein has also been linked to efflux of amphipathic drugs. Purified wild-type MsbA was labelled stoichiometrically with the fluorescent probe MIANS [2-(4′-maleimidylanilino)naphthalene-6-sulfonic acid] on C315, which is located within the intracellular domain connecting transmembrane helix 6 and the nucleotide-binding domain. MsbA–MIANS displayed high ATPase activity, and its folding and stability were unchanged. The initial rate of MsbA lab

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Kim, Sou Hyun, Chawon Yun, Doyoung Kwon, Yun-Hee Lee, Jae-Hwan Kwak, and Young-Suk Jung. "Effect of Isoquercitrin on Free Fatty Acid-Induced Lipid Accumulation in HepG2 Cells." Molecules 28, no. 3 (2023): 1476. http://dx.doi.org/10.3390/molecules28031476.

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Liver metabolic disorders and oxidative stress are crucial factors in the development of nonalcoholic fatty liver disease (NAFLD); however, treatment strategies to combat NAFLD remain poorly established, presenting an important challenge that needs to be addressed. Herein, we aimed to examine the effect of isoquercitrin on lipid accumulation induced by exogenous free fatty acids (FFA) using HepG2 cells and elucidate the underlying molecular mechanism. The cells were exposed to 0.5 mM FFA to induce intracellular lipid accumulation, followed by co-treatment with isoquercitrin to confirm the pote

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Cheng, Kwan H., Angela Graf, Amber Lewis, Thuong Pham, and Aakriti Acharya. "Exploring Membrane Binding Targets of Disordered Human Tau Aggregates on Lipid Rafts Using Multiscale Molecular Dynamics Simulations." Membranes 12, no. 11 (2022): 1098. http://dx.doi.org/10.3390/membranes12111098.

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The self-aggregation of tau, a microtubule-binding protein, has been linked to the onset of Alzheimer’s Disease. Recent studies indicate that the disordered tau aggregates, or oligomers, are more toxic than the ordered fibrils found in the intracellular neurofibrillary tangles of tau. At present, details of tau oligomer interactions with lipid rafts, a model of neuronal membranes, are not known. Using molecular dynamics simulations, the lipid-binding events, membrane-damage, and protein folding of tau oligomers on various lipid raft surfaces were investigated. Tau oligomers preferred to bind t

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Mahmood, Akhtar, Jian-su Shao, and David H. Alpers. "Rat enterocytes secrete SLPs containing alkaline phosphatase and cubilin in response to corn oil feeding." American Journal of Physiology-Gastrointestinal and Liver Physiology 285, no. 2 (2003): G433—G441. http://dx.doi.org/10.1152/ajpgi.00466.2002.

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Surfactant-like particles (SLP) are unilamellar secreted membranes associated with the process of lipid absorption and isolated previously only from the apical surface of enterocytes. In this paper, the intracellular membrane has been isolated from corn oil-fed animals, identified by its content of the marker protein intestinal alkaline phosphatase (IAP). Another brush-border protein, cubilin, and its anchoring protein megalin have been identified as components of extracellular SLP, but only cubilin is present to any extent in intracellular SLP. During fat absorption, IAP is modestly enriched

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Lee, Eun Byul, Pil Soo Sung, Jung-Hee Kim, Dong Jun Park, Wonhee Hur, and Seung Kew Yoon. "microRNA-99a Restricts Replication of Hepatitis C Virus by Targeting mTOR and De Novo Lipogenesis." Viruses 12, no. 7 (2020): 696. http://dx.doi.org/10.3390/v12070696.

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In this study, we investigated the role of microRNA-99a (miR-99a) in hepatitis C virus (HCV) replication and lipogenesis in hepatocytes. Cell-culture-derived HCV (HCVcc) infection caused down-regulation of miR-99a in Huh-7 cells, and the relative levels of miR-99a were significantly lower in the sera of the HCV-infected patients than in those of healthy controls. Transfection of miR-99a-5p mimics resulted in a decrease in the intracellular and secreted HCV RNA levels. It also caused a decreased mammalian target of rapamycin (mTOR) protein level and phosphorylation of its downstream targets in

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Aw, Yvette C., Andrew J. Brown, Jia-Wei Wu, and Hongyuan Yang. "ORP1L, ORP1S, and ORP2: Lipid Sensors and Transporters." Contact 3 (January 2020): 251525642095681. http://dx.doi.org/10.1177/2515256420956818.

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Lipid transfer proteins are crucial for intracellular cholesterol trafficking at sites of membrane contact. In the OSBP/ORPs (oxysterol binding protein and OSBP-related proteins) family of lipid transfer proteins, ORP1L, ORP1S and ORP2 play important roles in cholesterol transport. ORP1L is an endosome/lysosome-anchored cholesterol sensor which may also move cholesterol bidirectionally at the interface between the endoplasmic reticulum and the endosome/lysosome. ORP2 delivers cholesterol to the plasma membrane, driven by PI(4,5)P2 hydrolysis. ORP1S may also transport cholesterol to the plasma

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34

Moore, David T., Patrik Nygren, Kathleen Molnar, Kathleen Boesze-Battaglia, Joel S. Bennett та William F. DeGrado. "Protein-Protein and Protein-Lipid Interactions Modulate αIIbβ3 Inside-out Signaling." Blood 114, № 22 (2009): 152. http://dx.doi.org/10.1182/blood.v114.22.152.152.

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Abstract Abstract 152 Integrins are ubiquitously expressed α/β heterodimers that mediate cell-cell and cell-extracellular matrix interactions. The platelet integrin αIIbβ3 binds soluble fibrinogen following platelet activation, an event necessary for the formation of platelet aggregates. Integrins reside on plasma membranes in a highly regulated and dynamic equilibrium between inactive resting states and active ligand binding conformations. An essential feature of this equilibrium is the association and dissociation of integrin transmembrane (TM) and cytoplasmic domains. Thus, when integrins a

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35

Prattes, S., G. Horl, A. Hammer, et al. "Intracellular distribution and mobilization of unesterified cholesterol in adipocytes: triglyceride droplets are surrounded by cholesterol-rich ER-like surface layer structures." Journal of Cell Science 113, no. 17 (2000): 2977–89. http://dx.doi.org/10.1242/jcs.113.17.2977.

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In addition to their central role in triglyceride storage, fat cells are a primary depot of unesterified cholesterol (FC) in the body. In comparison, peripheral cells contain very little FC. This difference in adipocytes versus peripheral tissues is inconsistent with the current theory of cholesterol homeostasis. Attempting to resolve this discrepancy, we examined intracellular storage sites of FC in murine 3T3-F442A adipocytes. Using the cholesterol-binding antibiotic, filipin, in combination with high resolution fluorescence microscopy, intense fluorescent staining characteristically decorat

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36

Sacchettini, J. C., S. M. Hauft, S. L. Van Camp, D. P. Cistola, and J. I. Gordon. "Developmental and structural studies of an intracellular lipid binding protein expressed in the ileal epithelium." Journal of Biological Chemistry 265, no. 31 (1990): 19199–207. http://dx.doi.org/10.1016/s0021-9258(17)30644-0.

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37

Lai, Hong-Yue, Ling-Wei Hsu, Hsin-Hwa Tsai, et al. "CCAAT/enhancer-binding protein delta promotes intracellular lipid accumulation in M1 macrophages of vascular lesions." Cardiovascular Research 113, no. 11 (2017): 1376–88. http://dx.doi.org/10.1093/cvr/cvx134.

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38

Sakai, Juro, and Robert B. Rawson. "The sterol regulatory element-binding protein pathway: control of lipid homeostasis through regulated intracellular transport." Current Opinion in Lipidology 12, no. 3 (2001): 261–66. http://dx.doi.org/10.1097/00041433-200106000-00004.

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39

Marcelino, Anna Marie C., Robert G. Smock, and Lila M. Gierasch. "Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family." Proteins: Structure, Function, and Bioinformatics 63, no. 2 (2006): 373–84. http://dx.doi.org/10.1002/prot.20860.

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40

Zhang, Chaoyi, Qianli Zhang, Zhihong Huang, and Quan Jiang. "Adropin inhibited tilapia hepatic glucose output and triglyceride accumulation via AMPK activation." Journal of Endocrinology 246, no. 2 (2020): 109–22. http://dx.doi.org/10.1530/joe-20-0077.

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Adropin plays a role in the maintenance of energy homeostasis, insulin resistance prevention, and impaired glucose tolerance. However, the molecular mechanisms by which adropin affects hepatic glucose and lipid metabolism in vitro are not entirely understood. This study intended to examine the roles and underlying mechanisms of adropin in glucose and lipid metabolism in Nile tilapia. In primary cultured tilapia hepatocytes, adropin significantly attenuated oleic acid (OA)-induced glucose output and reduced the activities and mRNA expression of cytosolic phosphoenolpyruvate carboxykinase (PEPCK

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41

THUMSER, Alfred E. A., and David C. WILTON. "The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein." Biochemical Journal 320, no. 3 (1996): 729–33. http://dx.doi.org/10.1042/bj3200729.

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The physiological role of liver fatty acid-binding protein (L-FABP) has yet to be clarified. An important feature of this member of the family of intracellular lipid-binding proteins is the wide range of compounds that have been identified as potential physiological ligands. By using recombinant L-FABP, the binding of cholesterol, bile salts and their derivatives has been investigated under conditions that allow a direct comparison of the binding affinities of these ligands for fatty acids. The results demonstrate an inability of L-FABP to bind cholesterol, although the anionic derivative, cho

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42

GUTIÉRREZ-GONZÁLEZ, Luis H., Christian LUDWIG, Carsten HOHOFF, et al. "Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP)." Biochemical Journal 364, no. 3 (2002): 725–37. http://dx.doi.org/10.1042/bj20020039.

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Human epidermal-type fatty acid-binding protein (E-FABP) belongs to a family of intracellular 14–15kDa lipid-binding proteins, whose functions have been associated with fatty acid signalling, cell growth, regulation and differentiation. As a contribution to understanding the structure—function relationship, we report in the present study features of its solution structure and backbone dynamics determined by NMR spectroscopy. Applying multi-dimensional high-resolution NMR techniques on unlabelled and 15N-enriched recombinant human E-FABP, the 1H and 15N resonance assignments were completed. On

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43

McDermott, Mark, Michael J. O. Wakelam, and Andrew J. Morris. "Phospholipase D." Biochemistry and Cell Biology 82, no. 1 (2004): 225–53. http://dx.doi.org/10.1139/o03-079.

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Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals. Although enzymes with broader selectivity are found in some of the lower organisms, the plant, yeast, and mammalian enzymes are selective for phosphatidylcholine. The two mammalian phospholipase D isoforms are regulated by protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families. Mammalian and ye

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Hofer, Peter, Ulrike Taschler, Renate Schreiber, Petra Kotzbeck, and Gabriele Schoiswohl. "The Lipolysome—A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation." Metabolites 10, no. 4 (2020): 147. http://dx.doi.org/10.3390/metabo10040147.

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The catabolism of intracellular triacylglycerols (TAGs) involves the activity of cytoplasmic and lysosomal enzymes. Cytoplasmic TAG hydrolysis, commonly termed lipolysis, is catalyzed by the sequential action of three major hydrolases, namely adipose triglyceride lipase, hormone-sensitive lipase, and monoacylglycerol lipase. All three enzymes interact with numerous protein binding partners that modulate their activity, cellular localization, or stability. Deficiencies of these auxiliary proteins can lead to derangements in neutral lipid metabolism and energy homeostasis. In this review, we sum

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45

Antonny, Bruno, Joëlle Bigay, and Bruno Mesmin. "The Oxysterol-Binding Protein Cycle: Burning Off PI(4)P to Transport Cholesterol." Annual Review of Biochemistry 87, no. 1 (2018): 809–37. http://dx.doi.org/10.1146/annurev-biochem-061516-044924.

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To maintain an asymmetric distribution of ions across membranes, protein pumps displace ions against their concentration gradient by using chemical energy. Here, we describe a functionally analogous but topologically opposite process that applies to the lipid transfer protein (LTP) oxysterol-binding protein (OSBP). This multidomain protein exchanges cholesterol for the phosphoinositide phosphatidylinositol 4-phosphate [PI(4)P] between two apposed membranes. Because of the subsequent hydrolysis of PI(4)P, this counterexchange is irreversible and contributes to the establishment of a cholesterol

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46

Hanadate, Yuki, Yumiko Saito-Nakano, Kumiko Nakada-Tsukui, and Tomoyoshi Nozaki. "Identification and Characterization of the Entamoeba Histolytica Rab8a Binding Protein: A Cdc50 Homolog." International Journal of Molecular Sciences 19, no. 12 (2018): 3831. http://dx.doi.org/10.3390/ijms19123831.

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Membrane traffic plays a pivotal role in virulence in the enteric protozoan parasite Entamoeba histolytica. EhRab8A small GTPase is a key regulator of membrane traffic at the endoplasmic reticulum (ER) of this protist and is involved in the transport of plasma membrane proteins. Here we identified the binding proteins of EhRab8A. The Cdc50 homolog, a non-catalytic subunit of lipid flippase, was identified as an EhRab8A binding protein candidate by affinity coimmunoprecipitation. Binding of EhRab8A to EhCdc50 was also confirmed by reciprocal immunoprecipitation and blue-native polyacrylamide ge

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47

Ito, Jinichi, and Makoto Michikawa. "ApoA-I/HDL Generation and Intracellular Cholesterol Transport through Cytosolic Lipid-Protein Particles in Astrocytes." Journal of Lipids 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/530720.

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Exogenous apolipoprotein A-I (apoA-I) associates with ATP-binding cassette transporter A1 (ABCA1) on the cell surface of astrocytes like various peripheral cells and enhances the translocation of newly synthesized cholesterol from the endoplasmic reticulum/Golgi apparatus (ER/Golgi) to the cytosol. The cholesterol translocated to the cytosol is incorporated to cytosolic lipid-protein particles (CLPP) together with phospholipids and proteins such as sphingomyelin, phosphatidylcholine, caveolin-1, protein kinase Cα(PK-Cα), and cyclophilin A. The CLPP are high density lipoproteins- (HDL-)like cyt

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48

Schaletzki, Yvonne, Marie-Luise Kromrey, Susanne Bröderdorf, et al. "Several adaptor proteins promote intracellular localisation of the transporter MRP4/ABCC4 in platelets and haematopoietic cells." Thrombosis and Haemostasis 117, no. 01 (2017): 105–15. http://dx.doi.org/10.1160/th16-01-0045.

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SummaryThe multidrug resistance protein 4 (MRP4/ABCC4) has been identified as an important transporter for signalling molecules including cyclic nucleotides and several lipid mediators in platelets and may thus represent a novel target to interfere with platelet function. Besides its localisation in the plasma membrane, MRP4 has been also detected in the membrane of dense granules in resting platelets. In polarised cells it is localised at the basolateral or apical plasma membrane. To date, the mechanism of MRP4 trafficking has not been elucidated; protein interactions may regulate both the lo

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49

Li, Ben, Muzammil H. Syed, Hamzah Khan, Krishna K. Singh, and Mohammad Qadura. "The Role of Fatty Acid Binding Protein 3 in Cardiovascular Diseases." Biomedicines 10, no. 9 (2022): 2283. http://dx.doi.org/10.3390/biomedicines10092283.

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Fatty acid binding proteins (FABPs) are proteins found in the cytosol that contribute to disorders related to the cardiovascular system, including atherosclerosis and metabolic syndrome. Functionally, FABPs serve as intracellular lipid chaperones, interacting with hydrophobic ligands and mediating their transportation to sites of lipid metabolism. To date, nine unique members of the FABP family (FABP 1–9) have been identified and classified according to the tissue in which they are most highly expressed. In the literature, FABP3 has been shown to be a promising clinical biomarker for coronary

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50

Raychaudhuri, Sumana, Young Jun Im, James H. Hurley, and William A. Prinz. "Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein–related proteins and phosphoinositides." Journal of Cell Biology 173, no. 1 (2006): 107–19. http://dx.doi.org/10.1083/jcb.200510084.

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Sterols are moved between cellular membranes by nonvesicular pathways whose functions are poorly understood. In yeast, one such pathway transfers sterols from the plasma membrane (PM) to the endoplasmic reticulum (ER). We show that this transport requires oxysterol-binding protein (OSBP)–related proteins (ORPs), which are a large family of conserved lipid-binding proteins. We demonstrate that a representative member of this family, Osh4p/Kes1p, specifically facilitates the nonvesicular transfer of cholesterol and ergosterol between membranes in vitro. In addition, Osh4p transfers sterols more

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