fatty acid transport

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Characterization of Fatty Acid EXporters involved in fatty acid transport for oil accumulation in the green alga Chlamydomonas reinhardtii

Characterization of Fatty Acid EXporters involved in fatty acid transport for oil accumulation in the green alga Chlamydomonas reinhardtii

In a previous study, fatty acids C16:0, C18:0, C18:1 and C18:3 were shown to be substrates for transport by AtFAX1 when heterologously expressed in yeast cells [7]. In C. reinhardtii, CrLACSs can transport C16:0, C18:0, C18:1, C18:2 and C18:3 according to a functional analysis experiment in yeast strains [26]. To determine whether CrFAXs are involved in fatty acid transport, Crfax1 and Crfax2 cDNA was separately cloned into the yeast expression vector pYES2 and then electroporated into the yeast (S. cerevisiae) strain BY4741. C16:0, C18:0, C18:1, C18:2 and C18:3 were used as carbon sources in the medium, and both CrFAXs affected fatty acid uptake into yeast (Additional file 12: Figure S7). In comparison, CrFAX1 prefers C16:0, C18:0, and C18:2, and CrFAX2 prefers to be involved in C16:0, C18:1, C18:2 and C18:3 metabolism (Additional file 12: Figure S7). Although fur- ther yeast complementation research with yeast mutant fat1p is necessary to clarify the potential transport func- tion of CrFAXs, the present results showed that both CrFAXs may perform similar functions to AtFAX1. Fig. 6 Accumulation of the major polar membrane lipids species
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The Role of Unesterified Fatty Acid Transport in Chylomicron Metabolism

The Role of Unesterified Fatty Acid Transport in Chylomicron Metabolism

The metabolism of palmitic acid-i-C"4 has been compared after intravenous administration to dogs in the form of chylomicron triglyceride fatty acids TGFA and as the albumin-bound unester[r]

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Prohibitin/annexin 2 interaction regulates fatty acid transport in adipose tissue

Prohibitin/annexin 2 interaction regulates fatty acid transport in adipose tissue

was measured by EchoMRI-100T (Echo Medical Systems). Glucose tolerance test (6 mice/group) was performed with a glucometer (One Touch Ultra) upon injecting glucose (1 g/kg body weight) into over- night-fasted mice. A lipid tolerance test was performed based on a previously described protocol (53) upon injecting 5.71 μl/g body weight of 20% Intralipid (Sigma-Aldrich) into overnight-fasted mice. Indirect cal- orimetry and spontaneous locomotor activity studies were performed with OXYMAX (Columbus Instru- ments) Comprehensive Lab Animal Monitoring System (CLAMS) as described (22). Palmitic acid and lauric acids (Molecular Probes) were conjugated with a fluorophore IRDye 680CW (LI-COR) through the NHS reactive group. BODIPY-FL-C 12 (558/568 nm) was purchased from Molecular Probes. For injection, 400 nM of a probe was emulsified in 65 mg/ml BSA. Whole body imaging of FA biodistribution was performed with In-Vivo Multispectral System FX (KODAK); analysis of resected organs was performed with Pearl Impulse system (LI-COR). Steady-state plasma analyses were performed at the Baylor Mouse Metabolism Core (Houston, Texas, USA). Triglyceride quantification was performed using a colorimetric kit from Biovision. Quantification of phage particles homing to WAT was performed by i.v. (tail vein) injec- tion of 1 × 10 10 KGGRAKD-phage transforming units, and 6 hours later, recovery of phage from i.p. WAT
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Fatty Acid Binding Protein in Small Intestine IDENTIFICATION, ISOLATION, AND EVIDENCE FOR ITS ROLE IN CELLULAR FATTY ACID TRANSPORT

Fatty Acid Binding Protein in Small Intestine IDENTIFICATION, ISOLATION, AND EVIDENCE FOR ITS ROLE IN CELLULAR FATTY ACID TRANSPORT

FABP was isolated from rat intestine by gel filtration and isoelectric focusing. It showed a reaction of complete immunochemical identity with proteins in the 12,000 mol wt fatty acid- binding fractions of liver, myocardium, and adipose tissue supernates. (The presence of immunochemically nonidentical 12,000 mol wt FABP in these tissues is not excluded.) By quantitative radial immunodiffusion, supernatant FABP concentration in mucosa from proximal and middle thirds of jejuno-ileum significantly exceeded that in distal third,

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Short chain fatty acid transport in the intestine of a herbivorous teleost

Short chain fatty acid transport in the intestine of a herbivorous teleost

Time course of 0-1 mmol 1 ' [3H]acetate uptake by upper intestinal brush-border membrane vesicles of tilapia preloaded with 100 mmol 1~' acetate Ac, formate F, bicarbonate Bic or glucona[r]

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Review: Omega-3 fatty acids transport through the placenta

Review: Omega-3 fatty acids transport through the placenta

Abstract: The placenta is a temporary vital organ for sustaining the development of the fetus throughout gestation. Although the fatty acid composition delivered to the fetus is largely determined by maternal circulating levels, the placenta preferentially transfers physiologically important long-chain polyunsaturated fatty acids (LC-PUFAs), particularly omega-3 (n-3) FAs. The precise mechanisms governing these transfers were covered in a veil, but have started to be revealed gradually. Several evidences suggest fatty acid transport proteins (FATPs), placental specific membrane bound fatty acid binding proteins (pFABPpm) and fatty acid translocases (FAT/CD36) involved in LC-PUFAs uptake. Our studies have shown that the placental transfer of omega-3 FAs through the trophoblast cells is largely contributed by fatty acid binding protein 3 (FABP3). Recently there are considerable interests in the potential for dietary omega-3 FAs as a therapeutic intervention for fetal disorders. In fact, prenatal supply of omega-3 FAs is essential for brain and retinal development. Recent findings suggest a potential opportunity of omega-3 FA interventions to decrease the incidence of type 2 diabetes in future generations. In this review, we discuss the molecular mechanism of transportation of omega-3 FAs through the placenta and how omega-3 FAs deficiency/supplementation impact on fetal development.
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Betaine affects muscle lipid metabolism via regulating the fatty acid uptake and oxidation in finishing pig

Betaine affects muscle lipid metabolism via regulating the fatty acid uptake and oxidation in finishing pig

Results: Betaine addition to the diet significantly increased the concentration of free fatty acids (FFA) in muscle (P < 0.05). Furthermore, the levels of serum cholesterol and high-density lipoprotein cholesterol were decreased (P < 0.05) and total cholesterol content was increased in muscle (P < 0.05) of betaine fed pigs. Experiments on genes involved in fatty acid transport showed that betaine increased expression of lipoprotein lipase(LPL), fatty acid translocase/cluster of differentiation (FAT/CD36), fatty acid binding protein (FABP3) and fatty acid transport protein (FATP1) (P < 0.05). The abundance of fatty acid transport protein and fatty acid binding protein were also increased by betaine (P < 0.05). As for the key factors involved in fatty acid oxidation, although betaine supplementation didn ’ t affect the level of carnitine and malonyl-CoA, betaine increased mRNA and protein abundance of carnitine palmitransferase-1(CPT1) and phosphorylated-AMPK (P < 0.05).
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PubMedCentral-PMC4921943.pdf

PubMedCentral-PMC4921943.pdf

Metabolic reprogramming of M F s offers a novel means of regulating in fl ammation, hence we hypothesized that metabolism of fatty acids by specific lipid trafficking proteins plays a critical role in suppressing ATM-mediated in fl ammation and maintaining glucose tolerance. Fatty acid transport protein 1 (FATP1, SLC27A1) is an ideal candidate for limiting pro-in fl ammatory activation: FATP1 is an acyl-CoA synthetase with af fi nity for long and very long chain fatty acids [24] e lending speci fi city to its function e which is important because some M F fatty acid transporters, such as CD36, are promiscuous [21,25]. FATP1 expression levels are highest in tissues characterized by active fatty acid uptake and lipid metabolism, such as adipose, heart, and skeletal muscle and is primarily localized to the plasma membrane, mito- chondria, and peroxisomes [26 e 28]. In adipocytes, FATP1 activity is regulated by insulin-mediated translocation that increases fatty acid uptake [29]. Studies of total-body Fatp1 knockout mice demonstrated that loss of FATP1 protected mice from the effects of HFD-induced obesity, insulin resistance, and intramuscular lipid accumulation [29,30]. Functional characterization of FATP1 and activation of fatty acids through its ACSL activity have been conducted in these tissues and cell types, but, to date, not in M F s [29 e 34]. Due to its complex expression pattern, the contribution of FATP1 to the development of insulin resistance is likely to be tissue- and cell-type speci fi c. In silico analysis of existing Immunological Genome “ ImmGen ” Project expression data suggested that Fatp1 is detected in M F s and plas- macytoid dendritic cells [35], but not other cells that may contribute to inflammation including monocytes, microglia, B cells, T cells, neu- trophils, and eosinophils.
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Conditions for oxygen and substrate transport in muscles in exercising mammals

Conditions for oxygen and substrate transport in muscles in exercising mammals

Lactate, glucose and fatty acid transport in exercising muscles The sustained performance in submaximal exercise depends critically on delivery of exogenous fuel to working muscle cells [r]

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Arachidonic acid as a bioactive molecule

Arachidonic acid as a bioactive molecule

The need for protein-mediated transport of long-chain fatty acids into the cell is hotly debated, and the reviews make interesting reading (e.g., refs. 4–9). One line of argument is that the rates of flip-flop of free fatty acids across lipid bilayers are sufficiently fast that protein transfer mechanisms are not required to explain phys- iological uptake (7, 8). On the other hand, there is evi- dence that several proteins facilitate long-chain fatty acid uptake (e.g., ref. 6). There is also evidence of sat- urability of fatty acid uptake and of competitive inhi- bition, which would appear to suggest that specific fatty acid receptors or transporters are involved. The counter argument is that these findings may be explained by physical limits to the uptake process relat- ed to the partitioning of fatty acids between albumin and the cell membranes (8). Proponents of the fatty acid transport systems concede that simple diffusion may account for a portion of the observed rates of fatty acid uptake (4, 5). It is also agreed that this may become the major mechanism if cells are suddenly flooded with high micromolar concentrations of fatty acids, as could occur under experimental conditions. The proponents of passive diffusion seem prepared to give less ground at this stage, noting that passive transfer is fast enough
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Annual life stage regulation of lipid metabolism and storage and association with PPARs in a migrant species: the gray catbird (Dumetella carolinensis)

Annual life stage regulation of lipid metabolism and storage and association with PPARs in a migrant species: the gray catbird (Dumetella carolinensis)

Our findings parallel the findings of McFarlan et al. (2009), who found an increase in FABPpm (mRNA and protein) and heart-type fatty acid binding protein (H-FABP) in the muscles of white- throated sparrows ( Zonotrichia albicollis ) during migratory periods. Guglielmo et al. (2002) also found an increase in H-FABP expression in the flight muscles of the western sandpiper ( Calidris mauri ) during migration compared with tropical overwintering and pre-migration. H-FABP, as well as adipocyte fatty acid binding protein (FABP4), mediate fatty acid transport within the cytosol and are in partial control of the metabolic fate of fatty acids within the cell (Bordoni et al., 2006). However, we found no significant seasonal variation in FABP4 expression in either the liver or adipose tissues. The inconsistency of our findings with those of McFarlan et al. (2009) and Guglielmo et al. (2002) regarding intracellular FABP is likely a result of differences in requirements for intracellular fatty acid transport between the tissues measured. Relative to liver and adipose, flight muscles may demand a much more dramatic increase in intracellular fatty acid transport to fuel the aerobic challenge of migration.
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Serum lipids as an indicator for the alteration of liver function in patients with hepatitis B

Serum lipids as an indicator for the alteration of liver function in patients with hepatitis B

5 ml intravenous blood samples from HBV-positive patients and healthy controls (HBV-negative) were collected after 14 h overnight fasting. Serum was separated and stored at − 40 °C until analyzed for lipid profile and fatty acids by micro-lab 300 and gas chromatograph 8700 (Perkin – Elmer Ltd). FAs were analyzed as TFA and FFA. TFA, as well as FFA contents of the samples, were analyzed as per reported method [11]. Peaks were identified by authentic standards supplied by Fluka Chemika (Buchs, Switzerland). Analytical grade reagents and solvents were utilized throughout the study. The peak area was used to calculate FA composition as a relative ratio of the total FA.
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When fats commit crimes: fatty acid metabolism, cancer stemness and therapeutic resistance

When fats commit crimes: fatty acid metabolism, cancer stemness and therapeutic resistance

Similar to the expression patterns of lipogenic genes in cancer cells, several lipogenic genes are dysregulated in CSCs and are critical for CSC expansion and survival. However, how these genes are regulated in CSCs and why CSCs depend upon their lipogenic potential require fur- ther investigation. A recent study reported that glioma stem cells prefer to utilize glucose and acetate as carbon sources, compared with differentiated glioma cells [83]. In that study, FASN was concurrently expressed with glioma stem cell markers, including SOX2, CD133 and Nestin. In glioma stem cells, inhibition of FASN by the fatty acid synthesis inhibitor cerulenin decreases expres- sion of glioma stem cell markers and reduces the number of tumorspheres formed [83]. In pancreatic CSCs, FASN is up-regulated and the inhibition efficacy of cerulenin is greater on pancreatic CSCs than on pancreatic cancer cells [84]. In breast CSCs, down-regulation of FASN by metformin via the induction of miR-193b leads to inhi- bition of mammosphere formation [85]. The antioxidant- like plant polyphenol resveratrol also decreases FASN to promote apoptosis in breast CSCs [86]. Taken together, these studies suggest that FASN is involved in promoting CSC survival.
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Effects of enriched Artemia with n–3 long-chain polyunsaturated fatty acids on growth performance, stress resistance and fatty acid profile of
 Litopenaeus vannamei postlarvae

Effects of enriched Artemia with n–3 long-chain polyunsaturated fatty acids on growth performance, stress resistance and fatty acid profile of Litopenaeus vannamei postlarvae

It has been reported that n–3 LC-PUFA can increase tolerance in young stages of crustaceans and fish when exposed to different stress tests such as salinity (Palácios et al., 2004; Palácios and Racotta, 2007), temperature (Chim et al., 2001) and total ammonia (Cavalli et al., 2000; Martins et al., 2006) and physical stress (Ako et al., 1994). In the present study, PL fed Artemia enriched with commercial emulsions showed higher survival rates than the control group when exposed to freshwater stress test. In this context, Palácios et al (2004) demonstrated that, the beneficial effect of n–3 LC-PUFA supplementation in the diet on survival of L. vannamei post PL to low salinity stress test is related to modification of fatty acid composition of gills and to a larger gill area which increases the surface of ion transport and the number of Na + /K + -ATPase pumps. In fact, n–3 LC-PUFA possibly promotes an increase in the synthesis of new membranes in gills that would result in an increase in the surface, and can incorporate the most suitable fatty acid composition to counteract the effect of salinity changes
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Original Article Asiatic acid promotes liver fatty acid metabolism in diabetic models

Original Article Asiatic acid promotes liver fatty acid metabolism in diabetic models

Initially, this study assessed measures of obe- sity and diabetes in db/db mice after AA treat- ment. Before intervention, body weights were significantly higher in the model group than the normal group (Figure 1A). However, AA treat- ment mitigated the increase in body weight. Livers of the model group mice were heavier than those of the normal group mice (Figure 1B), but AA treatment also attenuated liver weight. The ratio of liver weight to body weight was also compared (Figure 1C). The ratio was elevated in the model group, which was attenu- ated by AA treatment. In addition, fasting serum glucose (Figure 1D), cholesterol (Figure 1E), TG (Figure 1F), and free fatty acid (Figure 1G) lev- els were all higher in the model group. In con- trast, AA treatment significantly decreased those parameters.
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Journal of Applied Pharmaceutical Science

Journal of Applied Pharmaceutical Science

The dichloromethane extracts of Cycas sancti-lasallei, a plant endemic to the Philippines, afforded squalene (1), β- sitosterol (2a), stigmasterol (2b), triglycerides (3), phytyl fatty acid esters (4), and β-sitosteryl fatty acid esters (5). Compounds 1-3 were reported to exhibit diverse biological activities, such as anticancer properties.

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Review Article Recent progress of lysophosphatidylcholine acyltransferases in metabolic disease and cancer

Review Article Recent progress of lysophosphatidylcholine acyltransferases in metabolic disease and cancer

reported LPCAT3 had distinct substrate prefer- ences that were strikingly consistent with a role in PC remodeling and modulating the fatty acid composition of PC. LPCAT3 preferred lysoPCs with saturated fatty acid at sn-1 position and exhibited acyl donor preference towards lino- leoyl-CoA and arachidonoyl-CoA. Furthermore, LPCAT3 was active in mediating 1-O-alkyl-sn- glycero-3-phosphocholine acylation with long- chain fatty acyl-CoAs to generate 1-O-alkyl-PC, another very important constituent of mamma- lian membrane systems. These properties were the precisely known attributes of LPCAT that were previously ascribed to the isoform involved in Lands’ cycle and thus strongly suggested that LPCAT3 was involved in PL remodeling to achieve appropriate membrane lipid fatty acid composition. Zhao Y. et al. [2] reported that membranes from HEK293 cells overexpressing LPCAT3 showed significantly increased LPCAT activity with a substrate preference toward unsaturated fatty acids. RNA interference- mediated knockdown of LPCAT3 in human hep- atoma Huh7 cells resulted in the virtually com- plete loss of membrane LPCAT activity, suggesting that LPCAT3 was primarily respon- sible for hepatic LPCAT activity. Furthermore, PPARα agonists dose-dependently regulated LPCAT3 in the liver in a PPAR alpha-dependent fashion, implicating the role of LPCAT3 in lipid homeostasis. The studies identified LPCAT3 as a key factor in lipoprotein production and pro- vided an invaluable tool for future investiga- Figure 1. Schematic diagram of the association between LPCATs and meta-
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Genetic analysis of oleic acid and linoleic acid content in relation to oil quality in groundnut

Genetic analysis of oleic acid and linoleic acid content in relation to oil quality in groundnut

Near Infrared Reflectance Spectroscopy (NIRS) is a more rapid nondestructive technique for screening of large population of seed for analysis of desirable changes in the fatty acid composition, protein and oil (Velasco and Becker, 1998; Biskupek-Korell and Moschner, 2007). Well matured dried kernels were used for fatty acid estimation using Near Infrared Reflectance Spectroscopy (model 6500). NIR diffuse reflectance spectra were collected by a monochromator NIR spectrometer model 6500 (Foss NIRS systems, France) with the range from 400 to 2500 nm, which consisted of a light source of tungsten halogen lamps of 50W, 12 volts. The spectrometer was equipped with silicon detector. For NIRS analysis, single seed was placed in a special adapter about 3 mm thick, with a diameter of 37 mm and a central hole of 6 mm. Before spectra acquisition, a reference spectrum was collected from a standard check cell (IH-0324A, Infrasoft International, LLC, France).
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A study of the polypeptides of porcine serum low density lipoproteins : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry, Massey University, New Zealand

A study of the polypeptides of porcine serum low density lipoproteins : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry, Massey University, New Zealand

The rate of VLDL release is influenced by the requirement for triglyceride transport from the liver, which i s dependent on the rate of fatty acid synthesis in the liv er and the level o[r]

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Role of carnitine in disease

Role of carnitine in disease

L -carnitine (ALCA) fed to aged rats was shown to reverse age-related declines in tissue L -carnitine levels and also reversed a number of age-related changes in liver mito- chondrial function; however, high doses of ALCA increased liver mitochondrial oxidant production [143]. Liu et al. demonstrated that memory loss in old rats is associated with brain mitochondrial decay and RNA/ DNA oxidation. Partial reversal was obtained by feeding acetyl-L-carnitine and/or R-alpha -lipoic acid [144]. ALCA, together with alpha-lipoic acid, was shown to improve mitochondrial energy metabolism and decrease oxidative stress leading to improved memory in aged rats [144,145]. Several studies have reported that supplement- ing rats with both L -carnitine and alpha-lipoic acid halts age-related increases in reactive oxygen species (ROS), lipid peroxidation, protein carbonylation, and DNA strand breaks in heart, skeletal muscle and brain, con- comitant with improvement in mitochondrial enzyme and respiratory chain activities [146-149]. In a clinical trial of Levocarnitine-treated elderly patients [150], there was significant improvement in total fat mass, total mus- cle mass, total cholesterol, LDL-C, HDL-C, triglycerides, apoA1, and apoB with concomitant decreases in physical and mental fatigue. These data suggest that administra- tion of levocarnitine to healthy elderly subjects may result
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