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PUFA levels in erythrocyte membrane phospholipids are differentially associated with colorectal adenoma risk.
Rifkin SB, Shrubsole MJ, Cai Q, Smalley WE, Ness RM, Swift LL, Zheng W, Murff HJ
(2017) Br J Nutr 117: 1615-1622
MeSH Terms: Adenoma, Arachidonic Acid, Biomarkers, Case-Control Studies, Colorectal Neoplasms, Diet, Eicosapentaenoic Acid, Erythrocyte Membrane, Female, Humans, Logistic Models, Male, Middle Aged, Odds Ratio, Phospholipids, Risk Factors, Tennessee
Show Abstract · Added April 3, 2018
Dietary intake of PUFA has been associated with colorectal neoplasm risk; however, results from observational studies have been inconsistent. Most prior studies have utilised self-reported dietary measures to assess fatty acid exposure which might be more susceptible to measurement error and biases compared with biomarkers. The purpose of this study was to determine whether erythrocyte phospholipid membrane PUFA percentages are associated with colorectal adenoma risk. We included data from 904 adenoma cases and 835 polyp-free controls who participated in the Tennessee Colorectal Polyp Study, a large colonoscopy-based case-control study. Erythrocyte membrane PUFA percentages were measured using GC. Conditional logistic regression was used to calculate adjusted OR for risk of colorectal adenomas with erythrocyte membrane PUFA. Higher erythrocyte membrane percentages of arachidonic acid was associated with an increased risk of colorectal adenomas (adjusted OR 1·66; 95 % CI 1·05, 2·62, P trend=0·02) comparing the highest tertile to the lowest tertile. The effect size for arachidonic acid was more pronounced when restricting the analysis to advanced adenomas only. Higher erythrocyte membrane EPA percentages were associated with a trend towards a reduced risk of advanced colorectal adenomas (P trend=0·05). Erythrocyte membrane arachidonic acid percentages are associated with an increased risk of colorectal adenomas.
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MeSH Terms
Dietary fatty acids modulate associations between genetic variants and circulating fatty acids in plasma and erythrocyte membranes: Meta-analysis of nine studies in the CHARGE consortium.
Smith CE, Follis JL, Nettleton JA, Foy M, Wu JH, Ma Y, Tanaka T, Manichakul AW, Wu H, Chu AY, Steffen LM, Fornage M, Mozaffarian D, Kabagambe EK, Ferruci L, Chen YD, Rich SS, Djoussé L, Ridker PM, Tang W, McKnight B, Tsai MY, Bandinelli S, Rotter JI, Hu FB, Chasman DI, Psaty BM, Arnett DK, King IB, Sun Q, Wang L, Lumley T, Chiuve SE, Siscovick DS, Ordovás JM, Lemaitre RN
(2015) Mol Nutr Food Res 59: 1373-83
MeSH Terms: Acetyltransferases, Acyltransferases, Adaptor Proteins, Signal Transducing, Carboxy-Lyases, Diet, Docosahexaenoic Acids, Eicosapentaenoic Acid, Erythrocyte Membrane, Fatty Acid Desaturases, Fatty Acids, Fatty Acids, Omega-3, Female, Humans, Male, Middle Aged, Polymorphism, Single Nucleotide
Show Abstract · Added April 23, 2015
SCOPE - Tissue concentrations of omega-3 fatty acids may reduce cardiovascular disease risk, and genetic variants are associated with circulating fatty acids concentrations. Whether dietary fatty acids interact with genetic variants to modify circulating omega-3 fatty acids is unclear. We evaluated interactions between genetic variants and fatty acid intakes for circulating alpha-linoleic acid, eicosapentaenoic acid, docosahexaenoic acid, and docosapentaenoic acid.
METHODS AND RESULTS - We conducted meta-analyses (N = 11 668) evaluating interactions between dietary fatty acids and genetic variants (rs174538 and rs174548 in FADS1 (fatty acid desaturase 1), rs7435 in AGPAT3 (1-acyl-sn-glycerol-3-phosphate), rs4985167 in PDXDC1 (pyridoxal-dependent decarboxylase domain-containing 1), rs780094 in GCKR (glucokinase regulatory protein), and rs3734398 in ELOVL2 (fatty acid elongase 2)). Stratification by measurement compartment (plasma versus erthyrocyte) revealed compartment-specific interactions between FADS1 rs174538 and rs174548 and dietary alpha-linolenic acid and linoleic acid for docosahexaenoic acid and docosapentaenoic acid.
CONCLUSION - Our findings reinforce earlier reports that genetically based differences in circulating fatty acids may be partially due to differences in the conversion of fatty acid precursors. Further, fatty acids measurement compartment may modify gene-diet relationships, and considering compartment may improve the detection of gene-fatty acids interactions for circulating fatty acid outcomes.
© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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16 MeSH Terms
Ex vivo red blood cell hemolysis assay for the evaluation of pH-responsive endosomolytic agents for cytosolic delivery of biomacromolecular drugs.
Evans BC, Nelson CE, Yu SS, Beavers KR, Kim AJ, Li H, Nelson HM, Giorgio TD, Duvall CL
(2013) J Vis Exp : e50166
MeSH Terms: Cytosol, Drug Carriers, Drug Delivery Systems, Endosomes, Erythrocyte Membrane, Erythrocytes, Hemolysis, Humans, Hydrogen-Ion Concentration, Lipid Bilayers, Lysosomes, Macromolecular Substances
Show Abstract · Added August 29, 2013
Phospholipid bilayers that constitute endo-lysosomal vesicles can pose a barrier to delivery of biologic drugs to intracellular targets. To overcome this barrier, a number of synthetic drug carriers have been engineered to actively disrupt the endosomal membrane and deliver cargo into the cytoplasm. Here, we describe the hemolysis assay, which can be used as rapid, high-throughput screen for the cytocompatibility and endosomolytic activity of intracellular drug delivery systems. In the hemolysis assay, human red blood cells and test materials are co-incubated in buffers at defined pHs that mimic extracellular, early endosomal, and late endo-lysosomal environments. Following a centrifugation step to pellet intact red blood cells, the amount of hemoglobin released into the medium is spectrophotometrically measured (405 nm for best dynamic range). The percent red blood cell disruption is then quantified relative to positive control samples lysed with a detergent. In this model system the erythrocyte membrane serves as a surrogate for the lipid bilayer membrane that enclose endo-lysosomal vesicles. The desired result is negligible hemolysis at physiologic pH (7.4) and robust hemolysis in the endo-lysosomal pH range from approximately pH 5-6.8.
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12 MeSH Terms
Determination of structural models of the complex between the cytoplasmic domain of erythrocyte band 3 and ankyrin-R repeats 13-24.
Kim S, Brandon S, Zhou Z, Cobb CE, Edwards SJ, Moth CW, Parry CS, Smith JA, Lybrand TP, Hustedt EJ, Beth AH
(2011) J Biol Chem 286: 20746-57
MeSH Terms: Anion Exchange Protein 1, Erythrocyte, Ankyrin Repeat, Ankyrins, Crystallography, X-Ray, Cytoskeleton, Erythrocyte Membrane, Humans, Models, Molecular, Protein Structure, Quaternary
Show Abstract · Added May 30, 2013
The adaptor protein ankyrin-R interacts via its membrane binding domain with the cytoplasmic domain of the anion exchange protein (AE1) and via its spectrin binding domain with the spectrin-based membrane skeleton in human erythrocytes. This set of interactions provides a bridge between the lipid bilayer and the membrane skeleton, thereby stabilizing the membrane. Crystal structures for the dimeric cytoplasmic domain of AE1 (cdb3) and for a 12-ankyrin repeat segment (repeats 13-24) from the membrane binding domain of ankyrin-R (AnkD34) have been reported. However, structural data on how these proteins assemble to form a stable complex have not been reported. In the current studies, site-directed spin labeling, in combination with electron paramagnetic resonance (EPR) and double electron-electron resonance, has been utilized to map the binding interfaces of the two proteins in the complex and to obtain inter-protein distance constraints. These data have been utilized to construct a family of structural models that are consistent with the full range of experimental data. These models indicate that an extensive area on the peripheral domain of cdb3 binds to ankyrin repeats 18-20 on the top loop surface of AnkD34 primarily through hydrophobic interactions. This is a previously uncharacterized surface for binding of cdb3 to AnkD34. Because a second dimer of cdb3 is known to bind to ankyrin repeats 7-12 of the membrane binding domain of ankyrin-R, the current models have significant implications regarding the structural nature of a tetrameric form of AE1 that is hypothesized to be involved in binding to full-length ankyrin-R in the erythrocyte membrane.
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9 MeSH Terms
Defects in postabsorptive plasma homeostasis of fatty acids in sickle cell disease.
Buchowski MS, Swift LL, Akohoue SA, Shankar SM, Flakoll PJ, Abumrad N
(2007) JPEN J Parenter Enteral Nutr 31: 263-8
MeSH Terms: Adolescent, Adult, Anemia, Sickle Cell, Case-Control Studies, Erythrocyte Membrane, Fasting, Fatty Acids, Nonesterified, Female, Humans, Infusions, Parenteral, Lipid Metabolism, Male, Middle Aged, Phospholipids, Postprandial Period, Triglycerides
Show Abstract · Added December 10, 2013
BACKGROUND - The chronic hemolytic anemia experienced by sickle cell disease (SCD) patients leads to adverse effects on oxygen transport by the blood and to a decrease in oxygen availability for peripheral tissues. Limited tissue oxygen availability has the potential to modify events of intracellular metabolism and, thus, alter lipid homeostasis.
METHODS - The impact of SCD on plasma fatty acid homeostasis was determined in 8 African American SCD patients and in 6 healthy African American control subjects under postabsorptive conditions and during a 3-hour IV infusion of a nutrient solution containing lipid, glucose, and amino acids.
RESULTS - SCD patients had higher fasting levels of plasma nonesterified fatty acids (NEFA), triglycerides, and phospholipids than healthy controls. Similarly, SCD patients had higher fasting levels of fatty acids in plasma triglycerides and phospholipids than healthy controls. Infusion of nutrients resulted in equivalent plasma NEFA profiles, total NEFA, and triglycerides in SCD patients and controls. However, the plasma phospholipid concentrations and fatty acid composition of plasma triglycerides and phospholipids were significantly higher in SCD patients; in particular, plasma pools of oleic acid were consistently increased in SCD. Plasma free oleic acid levels were elevated basally, leading to increased oleic acid content in triglycerides and phospholipids both post absorptively and during nutrient infusion.
CONCLUSIONS - There is an underlying defect in lipid metabolism associated with SCD best manifested during the fasting state. This abnormality in lipid homeostasis has the potential to alter red blood cell (RBC) membrane fluidity and function in SCD patients.
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16 MeSH Terms
Cytoplasmic remodeling of erythrocyte raft lipids during infection by the human malaria parasite Plasmodium falciparum.
Murphy SC, Fernandez-Pol S, Chung PH, Prasanna Murthy SN, Milne SB, Salomao M, Brown HA, Lomasney JW, Mohandas N, Haldar K
(2007) Blood 110: 2132-9
MeSH Terms: Animals, Annexin A5, Blotting, Western, Cell Membrane, Cytoplasm, Endocytosis, Erythrocyte Membrane, Erythrocytes, Flow Cytometry, Green Fluorescent Proteins, Humans, Isoenzymes, Liposomes, Malaria, Mass Spectrometry, Membrane Microdomains, Parasitemia, Phosphatidylethanolamines, Phosphatidylglycerols, Phosphatidylinositol 4,5-Diphosphate, Phosphatidylinositols, Phospholipase C delta, Plasmodium falciparum, Primaquine, Type C Phospholipases, Vacuoles
Show Abstract · Added March 21, 2013
Studies of detergent-resistant membrane (DRM) rafts in mature erythrocytes have facilitated identification of proteins that regulate formation of endovacuolar structures such as the parasitophorous vacuolar membrane (PVM) induced by the malaria parasite Plasmodium falciparum. However, analyses of raft lipids have remained elusive because detergents interfere with lipid detection. Here, we use primaquine to perturb the erythrocyte membrane and induce detergent-free buoyant vesicles, which are enriched in cholesterol and major raft proteins flotillin and stomatin and contain low levels of cytoskeleton, all characteristics of raft microdomains. Lipid mass spectrometry revealed that phosphatidylethanolamine and phosphatidylglycerol are depleted in endovesicles while phosphoinositides are highly enriched, suggesting raft-based endovesiculation can be achieved by simple (non-receptor-mediated) mechanical perturbation of the erythrocyte plasma membrane and results in sorting of inner leaflet phospholipids. Live-cell imaging of lipid-specific protein probes showed that phosphatidylinositol (4,5) bisphosphate (PIP(2)) is highly concentrated in primaquine-induced vesicles, confirming that it is an erythrocyte raft lipid. However, the malarial PVM lacks PIP(2), although another raft lipid, phosphatidylserine, is readily detected. Thus, different remodeling/sorting of cytoplasmic raft phospholipids may occur in distinct endovacuoles. Importantly, erythrocyte raft lipids recruited to the invasion junction by mechanical stimulation may be remodeled by the malaria parasite to establish blood-stage infection.
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26 MeSH Terms
Erythrocyte G protein-coupled receptor signaling in malarial infection.
Harrison T, Samuel BU, Akompong T, Hamm H, Mohandas N, Lomasney JW, Haldar K
(2003) Science 301: 1734-6
MeSH Terms: Adrenergic beta-2 Receptor Agonists, Adrenergic beta-2 Receptor Antagonists, Adrenergic beta-Agonists, Adrenergic beta-Antagonists, Alprenolol, Animals, Catecholamines, Cyclic AMP, Erythrocyte Membrane, Erythrocytes, GTP-Binding Protein alpha Subunits, Gs, Humans, Malaria, Membrane Microdomains, Mice, Parasitemia, Peptide Fragments, Plasmodium berghei, Plasmodium falciparum, Propranolol, Purinergic P1 Receptor Agonists, Purinergic P1 Receptor Antagonists, Receptors, Adrenergic, beta-2, Receptors, Purinergic P1, Signal Transduction, Stereoisomerism, Vacuoles
Show Abstract · Added December 10, 2013
Erythrocytic mechanisms involved in malarial infection are poorly understood. We have found that signaling via the erythrocyte beta2-adrenergic receptor and heterotrimeric guanine nucleotide-binding protein (Galphas) regulated the entry of the human malaria parasite Plasmodium falciparum. Agonists that stimulate cyclic adenosine 3',5'-monophosphate production led to an increase in malarial infection that could be blocked by specific receptor antagonists. Moreover, peptides designed to inhibit Galphas protein function reduced parasitemia in P. falciparum cultures in vitro, and beta-antagonists reduced parasitemia of P. berghei infections in an in vivo mouse model. Thus, signaling via the erythrocyte beta2-adrenergic receptor and Galphas may regulate malarial infection across parasite species.
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27 MeSH Terms
Thioredoxin reductase reduces lipid hydroperoxides and spares alpha-tocopherol.
May JM, Morrow JD, Burk RF
(2002) Biochem Biophys Res Commun 292: 45-9
MeSH Terms: Animals, Erythrocyte Membrane, Ferricyanides, Humans, Kinetics, Lipid Peroxidation, Lipid Peroxides, Lipoxygenase, Liver, Oxidation-Reduction, Rats, Thioredoxin-Disulfide Reductase, alpha-Tocopherol
Show Abstract · Added December 10, 2013
We investigated whether and how rat liver thioredoxin reductase spares alpha-tocopherol in biomembranes. Purified hydroperoxides of beta-linoleoyl-gamma-palmitoylphosphatidylcholine were decreased 35% by treatment with thioredoxin reductase and 54% by thioredoxin reductase plus E. coli thioredoxin. Thioredoxin reductase also halved the amount of hydroperoxides that had been formed during photoperoxidation of liposomes composed of beta-linoleoyl-gamma-palmitoylphosphatidylcholine, and of emulsions of both cholesterol and cholesteryl linolenate. In erythrocyte ghosts, thioredoxin reductase spared alpha-tocopherol from oxidation by both soybean lipoxygenase and ferricyanide. Thioredoxin reductase also decreased F(2)-isoprostanes in ghosts oxidized by ferricyanide, suggesting that its ability to spare alpha-tocopherol relates to reduction of lipid hydroperoxides.
(C)2002 Elsevier Science (USA).
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13 MeSH Terms
Recycling of the ascorbate free radical by human erythrocyte membranes.
May JM, Qu Z, Cobb CE
(2001) Free Radic Biol Med 31: 117-24
MeSH Terms: Ascorbic Acid, Electron Spin Resonance Spectroscopy, Erythrocyte Membrane, Ferricyanides, Free Radicals, Humans, In Vitro Techniques, NAD, NADH, NADPH Oxidoreductases, Oxidation-Reduction
Show Abstract · Added December 10, 2013
Reduction of the ascorbate free radical (AFR) at the plasma membrane provides an efficient mechanism to preserve the vitamin in a location where it can recycle alpha-tocopherol and thus prevent lipid peroxidation. Erythrocyte ghost membranes have been shown to oxidize NADH in the presence of the AFR. We report that this activity derives from an AFR reductase because it spares ascorbate from oxidation by ascorbate oxidase, and because ghost membranes decrease steady-state concentrations of the AFR in a protein- and NADH-dependent manner. The AFR reductase has a high apparent affinity for both NADH and the AFR (< 2 microM). When measured in open ghosts, the reductase is comprised of an inner membrane activity (both substrate sites on the cytosolic membrane face) and a trans-membrane activity that mediates extracellular AFR reduction using intracellular NADH. However, the trans-membrane activity constitutes only about 12% of the total measured in ghosts. Ghost AFR reductase activity can also be differentiated from NADH-dependent ferricyanide reductase(s) by its sensitivity to the detergent Triton X-100 and insensitivity to enzymatic digestion with cathepsin D. This NADH-dependent AFR reductase could serve to recycle ascorbic acid at a crucial site on the inner face of the plasma membrane.
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2 Members
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10 MeSH Terms
Troglitazone protects human erythrocytes from oxidant damage.
May JM, Qu ZC
(2000) Antioxid Redox Signal 2: 243-50
MeSH Terms: Antioxidants, Cells, Cultured, Chromans, Dose-Response Relationship, Drug, Erythrocyte Membrane, Erythrocytes, Free Radicals, Humans, Lipid Peroxides, Liposomes, Oxidative Stress, Thiazoles, Thiazolidinediones, Time Factors, Troglitazone, Vitamin E
Show Abstract · Added December 10, 2013
The antidiabetic drug troglitazone contains the active chromanol ring of alpha-tocopherol, which should give it antioxidant properties within cells. In these studies, the antioxidant effects of troglitazone were tested in human erythrocytes and in their ghosts. Troglitazone bound to erythrocyte ghosts in a linear manner and was retained even after centrifugation washes. In response to an oxidant stress generated by a water-soluble free radical initiator, troglitazone that was bound to erythrocyte ghosts was oxidized, but induced a lag-phase in the disappearance of endogenous alpha-tocopherol and in the appearance of lipid hydroperoxides. Troglitazone also delayed loss of endogenous alpha-tocopherol and hemolysis in washed intact erythrocytes in response to free radical-induced extracellular oxidant stress. To mimic exposure of erythrocytes to lipid hydroperoxides in vivo, erythrocytes were incubated with phospholipid liposomes that contained small amounts of preformed lipid hydroperoxides. This induced an oxidant stress in both the liposomes and cells. Troglitazone in concentrations above 4 microM almost completely prevented further appearance of lipid hydroperoxides in the liposomes, and also completely preserved alpha-tocopherol in the erythrocytes. The present results suggest that troglitazone will help to prevent peroxidative damage to erythrocytes in areas of excessive oxidant stress in the vascular bed.
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16 MeSH Terms