scholarly journals Modulation of long-chain Acyl-CoA synthetase on the development, lipid deposit and cryosurvival of in vitro produced bovine embryos

PLoS ONE ◽  
2019 ◽  
Vol 14 (8) ◽  
pp. e0220731 ◽  
Author(s):  
Roniele Santana Valente ◽  
Tamie Guibu de Almeida ◽  
Mayra Fernanda Alves ◽  
Janine de Camargo ◽  
Andrea Cristina Basso ◽  
...  
Keyword(s):  
Bovine Embryos ◽  
Chain Acyl ◽  
Long Chain ◽  
Lipid Deposit

Substrate preferences of long-chain acyl-CoA synthetase and diacylglycerol acyltransferase contribute to enrichment of flax seed oil with α-linolenic acid

2018 ◽  
Vol 475 (8) ◽  
pp. 1473-1489 ◽  
Author(s):  
Yang Xu ◽  
Roman Holic ◽  
Darren Li ◽  
Xue Pan ◽  
Elzbieta Mietkiewska ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Linolenic Acid ◽  
Seed Oil ◽  
Diacylglycerol Acyltransferase ◽  
Acyl Donor ◽  
Flax Seed ◽  
Chain Acyl ◽  
Long Chain

Seed oil from flax (Linum usitatissimum) is enriched in α-linolenic acid (ALA; 18:3Δ9cis,12cis,15cis), but the biochemical processes underlying the enrichment of flax seed oil with this polyunsaturated fatty acid are not fully elucidated. Here, a potential process involving the catalytic actions of long-chain acyl-CoA synthetase (LACS) and diacylglycerol acyltransferase (DGAT) is proposed for ALA enrichment in triacylglycerol (TAG). LACS catalyzes the ATP-dependent activation of free fatty acid to form acyl-CoA, which in turn may serve as an acyl-donor in the DGAT-catalyzed reaction leading to TAG. To test this hypothesis, flax LACS and DGAT cDNAs were functionally expressed in Saccharomyces cerevisiae strains to probe their possible involvement in the enrichment of TAG with ALA. Among the identified flax LACSs, LuLACS8A exhibited significantly enhanced specificity for ALA over oleic acid (18:1Δ9cis) or linoleic acid (18:2Δ9cis,12cis). Enhanced α-linolenoyl-CoA specificity was also observed in the enzymatic assay of flax DGAT2 (LuDGAT2-3), which displayed ∼20 times increased preference toward α-linolenoyl-CoA over oleoyl-CoA. Moreover, when LuLACS8A and LuDGAT2-3 were co-expressed in yeast, both in vitro and in vivo experiments indicated that the ALA-containing TAG enrichment process was operative between LuLACS8A- and LuDGAT2-3-catalyzed reactions. Overall, the results support the hypothesis that the cooperation between the reactions catalyzed by LACS8 and DGAT2 may represent a route to enrich ALA production in the flax seed oil.

Differential inhibition of long-chain acyl-CoA hydrolases by hypolipidemic drugs in vitro

1992 ◽  
Vol 43 (3) ◽  
pp. 639-644 ◽  
Author(s):  
R.M. Sánchez ◽  
M. Alegret ◽  
T. Adzet ◽  
M. Merlos ◽  
J.C. Laguna
Keyword(s):  
Differential Inhibition ◽  
Chain Acyl ◽  
Hypolipidemic Drugs ◽  
Long Chain

scholarly journals Acyl-Coenzyme A Dehydrogenases Are Localized on GLUT4-Containing Vesicles via Association with Insulin-Regulated Aminopeptidase in a Manner Dependent on Its Dileucine Motif

2002 ◽  
Vol 16 (5) ◽  
pp. 1049-1059 ◽  
Author(s):  
Hideki Katagiri ◽  
Tomoichiro Asano ◽  
Tetsuya Yamada ◽  
Toshifumi Aoyama ◽  
Yasushi Fukushima ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Coenzyme A ◽  
Amino Acid Residues ◽  
Glutathione S Transferase ◽  
Medium Chain ◽  
Dileucine Motif ◽  
Chain Acyl ◽  
Acyl Coenzyme A ◽  
Long Chain

Abstract Insulin-regulated aminopeptidase (IRAP, also termed vp165) is known to be localized on the GLUT4-containing vesicles and to be recruited to the plasma membrane after stimulation with insulin. The cytoplasmic region of IRAP contains two dileucine motifs and acidic regions, one of which (amino acid residues 55–82) is reportedly involved in retention of GLUT4-containing vesicles. The region of IRAP fused with glutathione-S-transferase [GST-IRAP(55–82)] was incubated with lysates from 3T3-L1 adipocytes, leading to identification of long-chain, medium-chain, and short-chain acyl-coenzyme A dehydrogenases (ACDs) as the proteins associated with IRAP. The association was nearly abolished by mutation of the dileucine motif of IRAP. Immunoblotting of fractions prepared from sucrose gradient ultracentrifugation and vesicles immunopurified with anti-GLUT4 antibody revealed these ACDs to be localized on GLUT4-containing vesicles. Furthermore, 3-mercaptopropionic acid and hexanoyl-CoA, inhibitors of long-chain and medium-chain ACDs, respectively, induced dissociation of long-chain acyl-coenzyme A dehydrogenase and/or medium-chain acyl-coenzyme A dehydrogenase from IRAP in vitro as well as recruitment of GLUT4 to the plasma membrane and stimulation of glucose transport activity in permeabilized 3T3-L1 adipocytes. These findings suggest that ACDs are localized on GLUT4-containing vesicles via association with IRAP in a manner dependent on its dileucine motif and play a role in retention of GLUT4-containing vesicles to an intracellular compartment.

scholarly journals PPARδ activation induces hepatic long-chain acyl-CoA synthetase 4 expression in vivo and in vitro

2015 ◽  
Vol 1851 (5) ◽  
pp. 577-587 ◽  
Author(s):  
Chin Fung Kelvin Kan ◽  
Amar Bahadur Singh ◽  
Bin Dong ◽  
Vikram Ravindra Shende ◽  
Jingwen Liu
Keyword(s):  
Chain Acyl ◽  
Long Chain

In vitro characterization and in vivo expression of human very-long chain acyl-CoA dehydrogenase

2006 ◽  
Vol 88 (4) ◽  
pp. 351-358 ◽  
Author(s):  
J. Lawrence Merritt ◽  
Dietrich Matern ◽  
Jerry Vockley ◽  
Jan Daniels ◽  
Tien V. Nguyen ◽  
...  
Keyword(s):  
In Vitro Characterization ◽  
In Vivo Expression ◽  
Chain Acyl ◽  
Long Chain

Fatty acid oxidation by isolated perfused working hearts of aged rats.

1977 ◽  
Vol 232 (3) ◽  
pp. E258 ◽  
Author(s):  
G M Abu-Erreish ◽  
J R Neely ◽  
J T Whitmer ◽  
V Whitman ◽  
D R Sanadi
Keyword(s):  
Adenine Nucleotide ◽  
Acid Oxidation ◽  
Tissue Mass ◽  
Chain Acyl ◽  
Pressure Development ◽  
Heart Preparation ◽  
Old Rats ◽  
Total Carnitine ◽  
Long Chain

It has been reported that mitochondria isolated from hearts of old rats have lower respiratory activity than mitochondria from young rats. In order to determine the physiological correlates of these changes, the metabolism of hearts from young and old rats has been compared in a perfused working heart preparation. The oxidation of [14C]palmitate to 14CO2, oxygen consumption, and nucleotide levels were measured under different cardiac workloads. The hearts from old animals performed less cardiac work and utilized less oxygen and palmitate in proportion to tissue mass, but the ratio of oxygen consumed to pressure developed was unaltered. There was a small but significant decrease in cardiac efficiency expressed as the ratio between the rate of oxygen consumed and ventricular pressure development. Tissue levels of total carnitine and long-chain acylcarnitine derivatives were greatly reduced in the older heart without significant change in free CoA, acetyl-CoA, or long-chain acyl-CoA. The adenine nucleotide levels were not significantly different in the two groups. The results appear consistent with the in vitro studies on isolated mitochondria.

Inhibition of myocardial rotenone-insensitive NADH cytochrome c reductase by amphiphilic compounds

1984 ◽  
Vol 247 (6) ◽  
pp. H889-H894
Author(s):  
F. F. Kennett ◽  
T. E. Knauer ◽  
K. Owens ◽  
W. B. Weglicki
Keyword(s):  
Cytochrome C ◽  
Critical Micellar Concentration ◽  
Cytochrome C Reductase ◽  
Chain Acyl ◽  
Order Of Magnitude ◽  
Lipid Metabolites ◽  
Nadh Cytochrome ◽  
Coa Thioesters ◽  
Long Chain

Because myocardial ischemia is correlated with both an elevation of intracellular levels of amphiphilic lipid metabolites and a decrease in the rotenone-insensitive NADH cytochrome c reductase (RINCR), we investigated the effects in vitro of some amphiphilic lipid metabolites and synthetic detergents on the activity of RINCR-enriched subfractions of microsomes from isolated cardiac myocytes. RINCR activity was unaffected in vitro by the addition of lysophosphatidylethanolamine (up to 0.5 mM) but was inhibited (maximum 63%) by lysophosphatidylcholine (8 microM). Palmitoyl carnitine (up to 2 mM) was ineffective, but the coenzyme A thioesters of palmitate, stearate, oleate, and arachidonate were inhibitory at concentrations (less than 3 microM) below their critical micellar concentrations. Arachidonyl CoA was approximately one order of magnitude more inhibitory than the other long-chain acyl CoA thioesters. Kinetic analyses revealed the effect of arachidonyl CoA on RINCR activity to be exclusively an alteration of the Vmax with no change in the Km for cytochrome c. The inhibition of myocytic RINCR activity by long-chain acyl CoA may be unrelated to the bulk-phase detergency of this lipid amphiphile since the effects were observed at concentrations below the critical micellar concentration, and other lipid amphiphiles had no effect on RINCR activity. Inhibition of microsomal RINCR activity may result from localized disruption of the membrane microenvironment of the enzyme complex by penetration or dissolution of long-chain acyl CoA into the membrane. The pronounced sensitivity of myocytic RINCR activity to long-chain acyl CoA suggests a relationship between the decreased RINCR activity and the increased levels of this class of lipid metabolites observed in the ischemic myocardium.

scholarly journals Demonstration and characterization of phosphate transport in mammalian peroxisomes

2005 ◽  
Vol 389 (3) ◽  
pp. 717-722 ◽  
Author(s):  
Wouter F. Visser ◽  
Carlo W. van Roermund ◽  
Lodewijk Ijlst ◽  
Klaas J. Hellingwerf ◽  
Ronald J. A. Wanders ◽  
...  
Keyword(s):  
Small Molecules ◽  
Adenine Nucleotide ◽  
Phosphate Transport ◽  
Significant Extent ◽  
Peroxisomal Membrane ◽  
Chain Acyl ◽  
Long Chain

It is now well established that the peroxisomal membrane is not freely permeable to small molecules in vivo, which implies the existence of metabolite transporters in the peroxisomal membrane. A few putative peroxisomal metabolite transporters have indeed been identified, but the function of these proteins has remained largely unresolved so far. The only peroxisomal transporter characterized to a significant extent is the adenine nucleotide transporter, which is presumably required to sustain the activity of the intraperoxisomal very-long-chain-acyl-CoA synthetase. In addition to AMP, this acyl-CoA synthetase also produces pyrophosphate, which must be exported from the peroxisome. In the present study, we demonstrate that the peroxisomal membrane contains a transporter activity that facilitates the passage of phosphate and possibly pyrophosphate across the peroxisomal membrane. By reconstitution of peroxisomal membrane proteins in proteoliposomes, some kinetic parameters of the transporter could be established in vitro. The transporter can be distinguished from the mitochondrial phosphate transporter by its different sensitivity to inhibitors.

Sign in / Sign up

Export Citation Format

Share Document