Effects of FABP4 variation on milk fatty-acid composition for dairy cattle grazed on pasture in late lactation

2020 ◽  
Vol 87 (1) ◽  
pp. 32-36
Author(s):  
Yunhai Li ◽  
Huitong Zhou ◽  
Long Cheng ◽  
Miriam Hodge ◽  
Jenny Zhao ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Milk Fat ◽  
Fatty Acid Binding Protein ◽  
Milk Fatty Acid ◽  
Long Chain Fatty Acids ◽  
Fatty Acid Binding ◽  
Holstein Friesian ◽  
Fat Composition ◽  
Chain Fatty Acids

AbstractThis research communication describes associations between variation in the fatty acid binding protein 4 gene (FABP4) and milk fat composition in New Zealand Holstein-Friesian × Jersey cross dairy cows. After correcting for the effect of the amino acid substitution p.K232A in diacylglycerol O-acyltransferase 1 (DGAT1), which is associated with variation in many milk fatty acid (FA) component levels, the effect of FABP4 c.328A/G on milk FA levels was typically small. For the five genotypes analysed, the AB cows produced more medium-chain fatty acids than CC cows (P < 0.05), and more C14:0 FA than AA and AC cows (P < 0.05). The AA and AC cows produced less C22:0 FA (P < 0.01) than the BC cows, and the AC cows produced more C24:0 FA (P < 0.05) than was produced by the BC cows. Cows of genotype CC produce more long-chain fatty acids than cows of genotype BC (P < 0.05).

Titration and Exchange Studies of Liver Fatty Acid-Binding Protein with13C-Labeled Long-Chain Fatty Acids†

Biochemistry ◽  
2002 ◽  
Vol 41 (17) ◽  
pp. 5453-5461 ◽  
Author(s):  
Hsin Wang ◽  
Yan He ◽  
Christopher D. Kroenke ◽  
Sarala Kodukula ◽  
Judith Storch ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Long Chain Fatty Acids ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Up-regulation of the expression of the gene for liver fatty acid-binding protein by long-chain fatty acids

1996 ◽  
Vol 319 (2) ◽  
pp. 483-487 ◽  
Author(s):  
Claire MEUNIER-DURMORT ◽  
Hélène POIRIER ◽  
Isabelle NIOT ◽  
Claude FOREST ◽  
Philippe BESNARD
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Fold Increase ◽  
Long Chain Fatty Acids ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Fabp Gene ◽  
Long Chain

The role of fatty acids in the expression of the gene for liver fatty acid-binding protein (L-FABP) was investigated in the well-differentiated FAO rat hepatoma cell line. Cells were maintained in serum-free medium containing 40 µM BSA/320 µM oleate. Western blot analysis showed that oleate triggered an approx. 4-fold increase in the cytosolic L-FABP level in 16 h. Oleate specifically stimulated L-FABP mRNA in time-dependent and dose-dependent manners with a maximum 7-fold increase at 16 h in FAO cells. Preincubation of FAO cells with cycloheximide prevented the oleate-mediated induction of L-FABP mRNA, showing that protein synthesis was required for the action of fatty acids. Run-on transcription assays demonstrated that the control of L-FABP gene expression by oleate was, at least in part, transcriptional. Palmitic acid, oleic acid, linoleic acid, linolenic acid and arachidonic acid were similarly potent whereas octanoic acid was inefficient. This regulation was also found in normal hepatocytes. Therefore long-chain fatty acids are strong inducers of L-FABP gene expression. FAO cells constitute a useful tool for studying the underlying mechanism of fatty acid action.

Z protein in hepatic uptake and esterification of long-chain fatty acids

1975 ◽  
Vol 228 (6) ◽  
pp. 1634-1640 ◽  
Author(s):  
S Mishkin ◽  
L Stein ◽  
G Fleischner ◽  
Z Gatmaitan ◽  
IM Arias
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Hepatic Uptake ◽  
Perfused Liver ◽  
Long Chain Fatty Acids ◽  
Fatty Acid Binding ◽  
Liver Preparation ◽  
Z Protein ◽  
Long Chain ◽  
Chain Fatty Acids

Fatty acids radioactivity was bound to Z protein in liver after administration of['3H]oleate to rats or to a perfused rat liver preparation. Pretreatment withflavaspidic acid (340 mumol/kg), a potent inhibitor of fatty acid binding to hepatic Zprotein in vitri, effectively reduced oleate radioactivity bound to Z by 90.2 plusor minus 4.3% and 85.0 plus or minus 6.2% in the intact rat and perfused liver, respectively. In spite of this effect, pretreatment of rats with flavaspidic acid did notalter plasma clearance, hepatic uptake, and esterification of ['3H]oleate. In contrast, in the perfused liver preparation, infusion of flavaspidic acid (340 mumol/kg)or bromosulphalein (360 mumol/kg) increased uptake of ['3H]oleate at least twofold,and oleate esterification was decreased by 15-30%. These results suggest that the binding of long-chain fatty acids to Z protein is not an obligatory step in their uptakeby the liver and that Z protein may be involved in fatty acid esterification.

scholarly journals A Review of the Metabolic Origins of Milk Fatty Acids

2013 ◽  
Vol 5 (3) ◽  
pp. 270-274 ◽  
Author(s):  
Anamaria COZMA ◽  
Doina MIERE ◽  
Lorena FILIP ◽  
Sanda ANDREI ◽  
Roxana BANC ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Mammary Gland ◽  
Fatty Acid ◽  
Milk Fat ◽  
De Novo ◽  
Long Chain Fatty Acids ◽  
De Novo Synthesis ◽  
Ruminal Biohydrogenation ◽  
Long Chain ◽  
Chain Fatty Acids

Milk fat and its fatty acid profile are important determinants of the technological, sensorial, and nutritional properties of milk and dairy products. The two major processes contributing to the presence of fatty acids in ruminant milk are the mammary lipogenesis and the lipid metabolism in the rumen. Among fatty acids, 4:0 to 12:0, almost all 14:0 and about a half of 16:0 in milk fat derive from de novo synthesis within the mammary gland. De novo synthesis utilizes as precursors acetate and butyrate produced through carbohydrates ruminal fermentation and involves acetyl-CoA carboxylase and fatty acid synthetase as key enzymes. The rest of 16:0 and all of the long-chain fatty acids derive from mammary uptake of circulating lipoproteins and nonesterified fatty acids that originate from digestive absorption of lipids and body fat mobilization. Further, long-chain fatty acids as well as medium-chain fatty acids entering the mammary gland can be desaturated via Δ-9 desaturase, an enzyme that acts by adding a cis-9-double bond on the fatty acid chain. Moreover, ruminal biohydrogenation of dietary unsaturated fatty acids results in the formation of numerous fatty acids available for incorporation into milk fat. Ruminal biohydrogenation is performed by rumen microbial population as a means of protection against the toxic effects of polyunsaturated fatty acids. Within the rumen microorganisms, bacteria are principally responsible for ruminal biohydrogenation when compared to protozoa and anaerobic fungi.

scholarly journals Constitutive expression of a saturable transport system for non-esterified fatty acids in Xenopus laevis oocytes

1994 ◽  
Vol 297 (2) ◽  
pp. 315-319 ◽  
Author(s):  
S L Zhou ◽  
D Stump ◽  
L Isola ◽  
P D Berk
Keyword(s):  
Fatty Acids ◽  
Plasma Membrane ◽  
Fatty Acid ◽  
Fatty Acid Binding Protein ◽  
Xenopus Laevis Oocytes ◽  
Long Chain Fatty Acids ◽  
Membrane Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Long Chain

In the presence of 150 microM BSA, uptake of [3H]oleate by Xenopus laevis oocytes was a saturable function of the unbound oleate concentration (Vmax. 110 +/- 4 pmol/h per oocyte; Km 193 +/- 11 nM unbound oleate). Oleate uptake was three orders of magnitude faster than that of another test substance, [35S]bromosulphophthalein, and was competitively inhibited by 55 nM unbound palmitate (Vmax. 111 +/- 14 pmol/h per oocyte; Km 424 +/- 63 nM unbound oleate) (P < 0.01). Oleate uptake was also inhibited by antibodies to a 43 kDa rat liver plasma-membrane fatty acid-binding protein, a putative transporter of long-chain fatty acids in mammalian cells; uptake of the medium-chain fatty acid [14C]octanoate was unaffected. Immunofluorescence and immunoblotting demonstrated that the antiserum reacted with a single 43 kDa protein on the oocyte surface. Hence a protein related to the mammalian plasma-membrane fatty acid-binding protein may play a role in saturable uptake of long-chain fatty acids by Xenopus oocytes.

The effect of a blend of dietary unesterified and saturated long-chain fatty acids on the performance of dairy cows in mid-lactation

1990 ◽  
Vol 41 (1) ◽  
pp. 129 ◽  
Author(s):  
KR King ◽  
CR Stockdale ◽  
TE Trigg
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Dairy Cows ◽  
Milk Fat ◽  
Chain Fatty Acid ◽  
Long Chain Fatty Acids ◽  
Long Chain Fatty Acid ◽  
Long Chain ◽  
Chain Fatty Acids

This experiment studied the effects of feeding a supplement of a blend of unesterified and saturated long-chain fatty acids on the productivity of dairy cows in mid-lactation. Twenty-three cows in their fourth month of lactation were individually fed ad libitum, a mixed balanced ration based on maize silage, lucerne hay and rolled grain. Varying quantities, up to 1020 g cow-1 day-1 of the fatty acid supplement, were mixed into the ration. Yields of milk and milk products were linearly related to total long-chain fatty acid intake. Milk fat content increased linearly while milk protein content averaged 3.59 (s.d. � 0.15)%. The marginal returns from feeding 1 kg of the supplement were 3.3 kg milk, 0.33 kg fat and 0.07 kg protein. The proportions of C 10:0, C12:0 and C 14:0 fatty acids in milk were decreased, while those of C 18:0 and C18:1 were increased as the result of feeding long-chain fatty acids. The concentration of lipid in plasma was increased, but acetate and D-(3)-hydroxybutyrate levels in blood remained unchanged with increased levels of dietary long-chain fatty acid. Efficiency of milk production was increased by 11% from feeding 1 kg of the supplement. In vivo digestibilities of dry matter, neutral and acid detergent fibres, and dietary long-chain fatty acids were unaffected by supplement.

scholarly journals A continuous fluorescence displacement assay for the measurement of phospholipase A2 and other lipases that release long-chain fatty acids

1990 ◽  
Vol 266 (2) ◽  
pp. 435-439 ◽  
Author(s):  
D C Wilton
Keyword(s):  
Fatty Acids ◽  
Enzyme Activity ◽  
Fatty Acid ◽  
Phospholipase A2 ◽  
Long Chain Fatty Acids ◽  
Fatty Acid Binding ◽  
Displacement Assay ◽  
Hydrolysis Of ◽  
Long Chain ◽  
Chain Fatty Acids

1. A new continuous fluorescence assay for phospholipase A2 is described which involves the displacement of the highly fluorescent fatty-acid probe 11-(dansylamino)undecanoic acid from rat liver fatty-acid-binding protein by long-chain fatty acids released as a result of phospholipase A2-catalysed hydrolysis of phospholipids. The initial rate of decrease in fluorescence is linearly related to enzyme activity. 2. The assay will detect enzyme activity down to about 10 pmol/min per ml and gives a linear response up to about 10 nmol/min per ml. 3. The assay will work with all phospholipids that have been tested including phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol and phosphatidylglycerol. Substrates carrying a net negative charge showed the highest rates of hydrolysis. 4. The assay will work, in principle, with an enzyme catalysing the release of long-chain fatty acids from a fatty-acylated substrate. This has been confirmed with pancreatic lipase and cholesterol esterase.

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