[11] Fatty acid synthase from lactating bovine mammary gland

Kumar, Soma; Dodds, Peter F.

doi:10.1016/0076-6879(81)71013-9

Cited by 11 publications

(6 citation statements)

References 6 publications

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“…Particularly high yields were observed from liver Kim et al 1981 ;Muesing & Porter, 1975 ;Roncari, 1981), often from animals fed on a carbohydrate-based diet, and from fat producing glands, including the lactating mammary gland (Kumar & Dodds, 1981 ;Smith & Abraham, 1975) and the uropygial gland of birds (Kolattukudy et al 1981). High yields of purified human FAS were also obtained from a mammary epithelial cell line (Thompson et al 1981).…”

Section: Purification and Crystallization Of Animal Fasmentioning

confidence: 99%

“…The animal FAS multienzyme has traditionally been natively purified from a variety of animal tissues (Arslanian & Wakil, 1975; Dils & Carey, 1975; Jenik & Porter, 1981; Kawaguchi et al 1981; Kim et al 1981; Kolattukudy et al 1981; Kumar & Dodds, 1981; Muesing & Porter, 1975; Roncari, 1981; Smith & Abraham, 1975). Particularly high yields were observed from liver (Arslanian & Wakil, 1975; Kim et al 1981; Muesing & Porter, 1975; Roncari, 1981), often from animals fed on a carbohydrate-based diet, and from fat producing glands, including the lactating mammary gland (Kumar & Dodds, 1981; Smith & Abraham, 1975) and the uropygial gland of birds (Kolattukudy et al 1981). High yields of purified human FAS were also obtained from a mammary epithelial cell line (Thompson et al 1981).…”

Section: Animal Fasmentioning

confidence: 99%

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Structure and function of eukaryotic fatty acid synthases

Maier

Leibundgut

Boehringer

et al. 2010

Quart. Rev. Biophys.

120

127

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Abstract. In all organisms, fatty acid synthesis is achieved in variations of a common cyclic reaction pathway by stepwise, iterative elongation of precursors with two-carbon extender units. In bacteria, all individual reaction steps are carried out by monofunctional dissociated enzymes, whereas in eukaryotes the fatty acid synthases (FASs) have evolved into large multifunctional enzymes that integrate the whole process of fatty acid synthesis. During the last few years, important advances in understanding the structural and functional organization of eukaryotic FASs have been made through a combination of biochemical, electron microscopic and X-ray crystallographic approaches. They have revealed the strikingly different architectures of the two distinct types of eukaryotic FASs, the fungal and the animal enzyme system. Fungal FAS is a 2Á6 MDa a 6 b 6 heterododecamer with a barrel shape enclosing two large chambers, each containing three sets of active sites separated by a central wheel-like structure. It represents a highly specialized micro-compartment strictly optimized for the production of saturated fatty acids. In contrast, the animal FAS is a 540 kDa X-shaped homodimer with two lateral reaction clefts characterized by a modular domain architecture and large extent of conformational flexibility that appears to contribute to catalytic efficiency.

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Section: Purification and Crystallization Of Animal Fasmentioning

confidence: 99%

Section: Animal Fasmentioning

confidence: 99%

Structure and function of eukaryotic fatty acid synthases

Maier

Leibundgut

Boehringer

et al. 2010

Quart. Rev. Biophys.

120

127

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“…FAS activity in CaCo-2 cytosol was assayed as described by Kumar and Dodds [37]. Briefly, CaCo-2 cells were homogenized in 100 mM potassium phosphate buffer, pH 7, 0.1 mM Na-EDTA and 1 mM dithiothreitol.…”

Section: Fas Assaymentioning

confidence: 99%

Polyunsaturated fatty acids decrease the expression of sterol regulatory element-binding protein-1 in CaCo-2 cells: effect on fatty acid synthesis and triacylglycerol transport

Field

Born

Murthy

et al. 2002

Biochemical Journal

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Regulation of sterol regulatory element-binding proteins (SREBPs) by fatty acid flux was investigated in CaCo-2 cells. Cells were incubated with 1 mM taurocholate with or without 250 microM 18:0, 18:1, 18:2, 20:4, 20:5 or 22:6 fatty acids. Fatty acid synthase (FAS) and acetyl-CoA carboxylase mRNA levels and gene and protein expression of SREBPs were estimated. 18:2, 20:4, 20:5 and 22:6 fatty acids decreased the amount of mature SREBP-1 and mRNA levels of SREBP-1c, SREBP-1a, FAS and acetyl-CoA carboxylase. SREBP-2 gene or mature protein expression was not altered. Liver X receptor (LXR) activation by T0901317 increased gene expression of SREBP-1c, SREBP-1a, FAS and acetyl-CoA carboxylase without altering SREBP-2. 20:5, but not 18:1, prevented the full expression of SREBP-1c mRNA by T0901317. T0901317 increased SREBP-1 mass without altering the mass of mature SREBP-2. Although only 18:2, 20:4, 20:5 and 22:6 suppressed SREBP-1, acetyl-CoA carboxylase and FAS expression, all fatty acids decreased the rate of fatty acid synthesis. T0901317 increased endogenous fatty acid synthesis yet did not increase secretion of triacylglycerol-rich lipoproteins. In CaCo-2 cells, polyunsaturated fatty acids decrease gene and protein expression of SREBP-1 and FAS mRNA, probably through interference with LXR activity. Since all fatty acids decreased fatty acid synthesis, mechanisms other than changes in SREBP-1c expression must be entertained. Increased endogenous fatty acid synthesis does not promote triacylglycerol-rich lipoprotein secretion.

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“…Total protein extraction was performed according to Kumar and Dodds (1981). Briefly, 5 g of the longissimus muscle and subcutaneous adipose tissue samples from each steer (n = 20 per genotype) were homogenized in 38 mL of phosphate-bicarbonate buffer (0.1M and pH: 8.0), then centrifuged at 20,000 g for 10 min, and the supernatant was transferred to a polypropylene tube which underwent ultracentrifugation at 105,000 g for 1 hour.…”

Section: Protein Extraction By Ultracentrifugationmentioning

confidence: 99%

“…The FASN activity assay was carried out following the method described by Kumar and Dodds (1981). Briefly, the FASN activity was assessed indirectly by measuring the decrease in the absorbance of NADPH at 340 nm by spectrophotometry in a 24 well plate in presence of Acetyl-CoA, Malonyl-CoA, and NADPH.…”

Section: Enzyme Activity Testmentioning

confidence: 99%

A Non-Synonymous Single Nucleotide Polymorphism in FASN Gene Alters FASN Enzyme Activity in Subcutaneous and Intramuscular Adipose Tissue in Holstein Friesian Steers

Cancino-Baier

Muñoz

Quiñones

et al. 2021

Annals of Animal Science

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The FASN enzyme plays a key role in fatty acids synthesis as the main long-chain fatty acid synthesizer. A non-synonymous SNP (single nucleotide polymorphism) (g.17925A>G) located in the thioesterase domain of this enzyme and an effect in fat deposition has been observed, but has not been evaluated in this breed and, moreover, the reason whereby this occurs remains unclear. The objective of this study was to evaluate the effect of this SNP on the activity of FASN enzyme in subcutaneous and intramuscular adipose tissue from Holstein Friesian steers. To achieve this, 196 animals were sampled in a local abattoir, genotyped for the FASN g.17924A>G SNP and characterized for fatty acid profile. Then a sub sample of 20 animals per genotype were selected to extract the total protein from subcutaneous and intramuscular adipose tissue to estimate the FASN enzyme activity. The FASN activity for each genotyped animal was assessed indirectly by measuring the decrease in the absorbance of NADPH at 340 nm by spectrophotometry in a 24 well plate in the presence of Acetyl-CoA, Malonyl-CoA, and NADPH. To assess the impact of SNP induced amino acid changes in FASN protein structure, in-silico simulations were performed. Our results indicated that FASN g.17924A>G SNP induces a change in the enzyme activity in subcutaneous adipose tissue, which is higher when the AA genotype is present and lower in the presence of the AG genotype. The in-silico analysis of the amino acid substitution shows that there was a structural change in the dimeric form of the protein between genotypes. Moreover, the global energy between subunits is lower and more favorable when the AA genotype is present and higher and less favorable for the AG genotype. It was also found that the fatty acid profile of subcutaneous adipose tissue was affected when the AG genotype was present, decreasing the C16:0 fatty acid levels and increasing the C18:0 fatty acid levels. The FASN g.17924A>G SNP alters the FASN enzyme structure and activity, leading to a variation in the fatty acid composition of subcutaneous adipose tissue in Holstein Friesian steers. Implications: This SNP could be considered as a tool to improve the fat deposition or marbling and the fatty acid profile in cattle.

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[11] Fatty acid synthase from lactating bovine mammary gland

Cited by 11 publications

References 6 publications

Structure and function of eukaryotic fatty acid synthases

Structure and function of eukaryotic fatty acid synthases

Polyunsaturated fatty acids decrease the expression of sterol regulatory element-binding protein-1 in CaCo-2 cells: effect on fatty acid synthesis and triacylglycerol transport

A Non-Synonymous Single Nucleotide Polymorphism in FASN Gene Alters FASN Enzyme Activity in Subcutaneous and Intramuscular Adipose Tissue in Holstein Friesian Steers

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