scholarly journals Long-Chain Acyl-CoA Synthetase is Associated with the Growth of Malassezia spp.

2019 ◽  
Vol 5 (4) ◽  
pp. 88 ◽  
Author(s):  
Tenagy ◽  
Kengo Tejima ◽  
Xinyue Chen ◽  
Shun Iwatani ◽  
Susumu Kajiwara
Keyword(s):  
Fatty Acid ◽  
Fungal Pathogen ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Long Chain Fatty Acids ◽  
Double Mutation ◽  
Triacsin C ◽  
Chain Acyl ◽  
Malassezia Spp ◽  
Long Chain

The lipophilic fungal pathogen Malassezia spp. must acquire long-chain fatty acids (LCFAs) from outside the cell. To clarify the mechanism of LCFA acquisition, we investigated fatty acid uptake by this fungus and identified the long-chain acyl-CoA synthetase (ACS) gene FAA1 in three Malassezia spp.: M. globosa, M. pachydermatis, and M. sympodialis. These FAA1 genes could compensate for the double mutation of FAA1 and FAA4 in Saccharomyces cerevisiae, suggesting that Malassezia Faa1 protein recognizes exogenous LCFAs. MgFaa1p and MpFaa1p utilized a medium-chain fatty acid, lauric acid (C12:0). Interestingly, the ACS inhibitor, triacsin C, affected the activity of the Malassezia Faa1 proteins but not that of S. cerevisiae. Triacsin C also reduced the growth of M. globosa, M. pachydermatis, and M. sympodialis. These results suggest that triacsin C and its derivatives are potential compounds for the development of new anti-Malassezia drugs.

scholarly journals Rat Long Chain Acyl-CoA Synthetase 5 Increases Fatty Acid Uptake and Partitioning to Cellular Triacylglycerol in McArdle-RH7777 Cells

2005 ◽  
Vol 281 (2) ◽  
pp. 945-950 ◽  
Author(s):  
Douglas G. Mashek ◽  
Michelle A. McKenzie ◽  
Cynthia G. Van Horn ◽  
Rosalind A. Coleman
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Chain Acyl ◽  
Long Chain

scholarly journals FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain acyl-CoA synthetase

2010 ◽  
Vol 299 (3) ◽  
pp. E384-E393 ◽  
Author(s):  
Alaric Falcon ◽  
Holger Doege ◽  
Amy Fluitt ◽  
Bernice Tsang ◽  
Nicki Watson ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Uptake ◽  
Fatty Acid Transport ◽  
Acid Uptake ◽  
Peroxisomal Enzyme ◽  
Multifunctional Protein ◽  
Hepatic Fatty Acid ◽  
Chain Acyl ◽  
Lcfa Uptake ◽  
Long Chain

Fatty acid transport protein (FATP)2, a member of the FATP family of fatty acid uptake mediators, has independently been identified as a hepatic peroxisomal very long-chain acyl-CoA synthetase (VLACS). Here we address whether FATP2 is 1) a peroxisomal enzyme, 2) a plasma membrane-associated long-chain fatty acid (LCFA) transporter, or 3) a multifunctional protein. We found that, in mouse livers, only a minor fraction of FATP2 localizes to peroxisomes, where it contributes to approximately half of the peroxisomal VLACS activity. However, total hepatic (V)LACS activity was not significantly affected by loss of FATP2, while LCFA uptake was reduced by 40%, indicating a more prominent role in hepatic LCFA uptake. This suggests FATP2 as a potential target for a therapeutic intervention of hepatosteatosis. Adeno-associated virus 8-based short hairpin RNA expression vectors were used to achieve liver-specific FATP2 knockdown, which significantly reduced hepatosteatosis in the face of continued high-fat feeding, concomitant with improvements in liver physiology, fasting glucose, and insulin levels. Based on our findings, we propose a model in which FATP2 is a multifunctional protein that shows subcellular localization-dependent activity and is a major contributor to peroxisomal (V)LACS activity and hepatic fatty acid uptake, suggesting FATP2 as a potential novel target for the treatment of nonalcoholic fatty liver disease.

scholarly journals Adipocyte-specific Inactivation of Acyl-CoA Synthetase Fatty Acid Transport Protein 4 (Fatp4) in Mice Causes Adipose Hypertrophy and Alterations in Metabolism of Complex Lipids under High Fat Diet

2011 ◽  
Vol 286 (41) ◽  
pp. 35578-35587 ◽  
Author(s):  
Lena-Solveig Lenz ◽  
Jana Marx ◽  
Walee Chamulitrat ◽  
Iris Kaiser ◽  
Hermann-Josef Gröne ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
High Fat Diet ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Long Chain Fatty Acids ◽  
High Fat ◽  
Complex Lipids ◽  
Long Chain ◽  
Chain Fatty Acids

Fatp4 exhibits acyl-CoA synthetase activity and is thereby able to catalyze the activation of fatty acids for further metabolism. However, its actual function in most tissues remains unresolved, and its role in cellular fatty acid uptake is still controversial. To characterize Fatp4 functions in adipocytes in vivo, we generated a mouse line with adipocyte-specific inactivation of the Fatp4 gene (Fatp4A−/−). Under standard conditions mutant mice showed no phenotypical aberrance. Uptake of radiolabeled palmitic and lignoceric acid into adipose tissue of Fatp4A−/− mice was unchanged. When exposed to a diet enriched in long chain fatty acids, Fatp4A−/− mice gained more body weight compared with control mice, although they were not consuming more food. Pronounced obesity was accompanied by a thicker layer of subcutaneous fat and greater adipocyte circumference, although expression of genes involved in de novo lipogenesis was not changed. However, the increase in total fat mass was contrasted by a significant decrease in various phospholipids, sphingomyelin, and cholesteryl esters in adipocytes. Livers of Fatp4-deficient animals under a high fat diet exhibited a higher degree of fatty degeneration. Nonetheless, no evidence for changes in insulin sensitivity and adipose inflammation was found. In summary, the results of this study confirm that Fatp4 is not crucial for fatty acid uptake into adipocytes. Instead, under the condition of a diet enriched in long chain fatty acids, adipocyte-specific Fatp4 deficiency results in adipose hypertrophy and profound alterations in the metabolism of complex lipids.

Membrane permeation and intracellular trafficking of long chain fatty acids: insights fromEscherichia coliand 3T3-L1 adipocytes

1995 ◽  
Vol 73 (5-6) ◽  
pp. 223-234 ◽  
Author(s):  
Dev Mangroo ◽  
Bernardo L. Trigatti ◽  
Gerhard E. Gerber
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Uptake ◽  
Chain Fatty Acid ◽  
Acid Uptake ◽  
Long Chain Fatty Acids ◽  
Long Chain Fatty Acid ◽  
Long Chain ◽  
Chain Fatty Acids

Long chain fatty acids are important substrates for energy production and lipid synthesis in prokaryotes and eukaryotes. Their cellular uptake represents an important first step leading to metabolism. This step is induced in Escherichia coli by growth in medium containing long chain fatty acids and in murine 3T3-L1 cells during differentiation to adipocytes. Consequently, these have been used extensively as model systems to study the cellular uptake of long chain fatty acids. Here, we present an overview of our current understanding of long chain fatty acid uptake in these cells. It consists of several distinct steps, mediated by a combination of biochemical and physico-chemical processes, and is driven by conversion of long chain fatty acids to acyl-CoA by acyl-CoA synthetase. An understanding of long chain fatty acid uptake may provide valuable insights into the roles of fatty acids in the regulation of cell signalling cascades, in the regulation of a variety of metabolic and transport processes, and in a variety of mammalian pathogenic conditions such as obesity and diabetes.Key words: acyl-CoA synthetase, adipocyte, Escherichia coli, fatty acid, transport, uptake.

Abstract 5381: Insulin-Stimulated Glucose Oxidation is Increased in Hearts from High Fat Diet-Induced Obese Mice Lacking Malonyl CoA Decarboxylase

Circulation ◽  
2008 ◽  
Vol 118 (suppl_18) ◽  
Author(s):  
John Edward R Ussher ◽  
Timothy R Koves ◽  
Jagdip S Jaswal ◽  
Christopher B Newgard ◽  
Jason R Dyck ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Glucose Oxidation ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Myocardial Fatty Acid ◽  
Malonyl Coa ◽  
Mitochondrial Fatty Acid ◽  
Chain Acyl ◽  
Wet Weight ◽  
Long Chain

OBJECTIVE - Diet-induced obesity (DIO) leads to an accumulation of intra-myocardial fatty acid metabolites that have been proposed to cause myocardial insulin resistance and dysfunction. Our goal was to determine the effect of DIO on myocardial fatty acid metabolite accumulation and how this is altered when mitochondrial fatty acid uptake is inhibited. This was achieved by using mice lacking malonyl CoA decarboxylase (MCD−/−), which have higher levels of malonyl CoA, an endogenous inhibitor of mitochondrial fatty acid uptake. METHODS - Wild type (WT) and MCD−/− mice were fed a low (4% kcal from lard) or high (60% kcal from lard) fat diet for 12 weeks to determine the effect of DIO on the intra-myocardial accumulation of long chain acylcarnitines, long chain acyl CoAs, triglycerides (TGs), and ceramides. A parallel feeding study was performed to assess myocardial function and energy metabolism in isolated working hearts in the absence/presence of insulin. RESULTS - We demonstrate that MCD−/− mice do not accumulate intramyocardial long chain acylcarnitines to the same extent as WT mice following DIO (0.56 ± 0.10 vs. 0.28 ± 0.07 pmol myristoylcarnitine/mg protein, P <0.05), but do accumulate similar amounts of long chain acyl CoAs (3.88 ± 0.34 vs. 4.35 ± 1.19 nmol/g wet weight). Interestingly, DIO only lead to an accumulation of TGs in the hearts of MCD−/− mice (3.29 ± 0.62 vs. 10.92 ± 3.72 μmol/g wet weight, P <0.05). Despite this elevation in TGs, MCD−/− mice showed increased insulin-stimulated glucose oxidation (2.46 ± 0.25 vs. 1.74 ± 0.18 fold increase, P <0.05) during aerobic isolated working heart perfusions and did not elicit any dysfunction. CONCLUSIONS - Our data reveal discordance between myocardial TG accumulation and glucose metabolism, suggesting that TG buffers against toxic lipids, and that inhibition of mitochondrial fatty acid oxidation does not cause myocardial dysfunction following DIO.

Caprenin 1. Digestion, Absorption, and Rearrangement in Thoracic Duct-Cannulated Rats

1991 ◽  
Vol 10 (3) ◽  
pp. 325-340 ◽  
Author(s):  
D. R. Webb ◽  
R. A. Sanders
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Female Rats ◽  
Acid Uptake ◽  
Long Chain Fatty Acids ◽  
Male And Female ◽  
Medium Chain ◽  
Male And Female Rats ◽  
Long Chain ◽  
Chain Fatty Acids

Caprenin (CAP) is a triglyceride that primarily contains caprylic (C8:0), capric (C10:0), and behenic (C22:0) acids. This study was undertaken to determine whether or not CAP is qualitatively digested, absorbed, and rearranged like other dietary fats and oils that contain these medium-chain and very long-chain fatty acids. In vitro results showed that neat CAP, coconut oil (CO) and peanut oil (PO) were hydrolyzed by porcine pancreatic lipase. All of the neat triglycerides also were digested in vivo by both male and female rats. This was shown by the recovery of significantly more extractable lymphatic fat than with fat-free control animals and by the recovery of orally administered triglyceride-derived fatty acids in lymph triglycerides. However, substantially more PO (74%) and CO (51%) were recovered in lymph relative to CAP (10%). These quantitative differences are consistent with the fatty acid composition of each triglyceride and primary routes of fatty acid uptake. The 24-h lymphatic recovery of CAP-derived C8:0, C10:0, and C22:0 averaged 3.9%, 17.8%, and 11.2%, respectively, for male and female rats. The C8:0 and C10:0 results approximated those obtained with CO (2.0% and 16.3%, respectively). In contrast, the 24-h absorbability of C22:0 in CAP was significantly less than that seen in PO (55.4%). Finally, there was no evidence of significant rearrangement of the positions of fatty acids on glycerol during digestion and absorption. Those fatty acids recovered in lymphatic fat tended to occupy the same glyceride positions that they did in the neat administered oils. However, the lymph fats recovered from all animals dosed with fat emulsions were enriched with endogenous lymph fatty acids. It is concluded that CAP is qualitatively digested, absorbed, and processed like any dietary fat or oil that contains medium-chain and very long-chain fatty acids.

AMPK-mediated increase in myocardial long-chain fatty acid uptake critically depends on sarcolemmal CD36

2007 ◽  
Vol 355 (1) ◽  
pp. 204-210 ◽  
Author(s):  
Daphna D.J. Habets ◽  
Will A. Coumans ◽  
Peter J. Voshol ◽  
Marion A.M. den Boer ◽  
Maria Febbraio ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Uptake ◽  
Chain Fatty Acid ◽  
Acid Uptake ◽  
Long Chain Fatty Acid ◽  
Long Chain
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