Molecular cloning and expression of rat liver bile acid CoA ligase

Falany, Charles N.; Xie, Xiaowei; Wheeler, James B.; Wang, Jin; Smith, Michelle; He, Dongning; Barnes, Stephen

doi:10.1194/jlr.m200260-jlr200

Cited by 31 publications

(29 citation statements)

References 29 publications

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“…BAL activities are associated with rat BAL protein (16) and human very long chain acyl-CoA synthase homolog 2 (VLACSR-H2) protein (17), but enzymatic analysis of BAL protein has not been performed in the mouse. Because the mouse very long chain acyl-CoA synthase-related (VLACSR) gene, which is highly expressed only in liver (18) as well as rat BAL and human VLACSR-H2 genes, has a high homology to these proteins (16), it was reasonable to assume that the VLACSR gene might be the mouse homolog for the BAL gene. On the other hand, BAT genes have been cloned from mouse (19), rat (20), and human (21).…”

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Hepatocyte Nuclear Factor 4α Is a Central Regulator of Bile Acid Conjugation

Inoue

et al. 2004

Journal of Biological Chemistry

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Hepatocyte nuclear factor 4␣ (HNF4␣) has an important role in regulating the expression of liver-specific genes. Because bile acids are produced from cholesterol in liver and many enzymes involved in their biosynthesis are preferentially expressed in liver, the role of HNF4␣ in the regulation of bile acid production was examined. In mice, unconjugated bile acids are conjugated with taurine by the liver-specific enzymes, bile acid-CoA ligase and bile acid-CoA:amino acid N-acyltransferase (BAT). Mice lacking hepatic HNF4␣ expression exhibited markedly decreased expression of the very long chain acyl-CoA synthase-related gene (VLACSR), a mouse candidate for bile acid-CoA ligase, and BAT. This was associated with markedly elevated levels of unconjugated and glycine-conjugated bile acids in gallbladder. HNF4␣ was found to bind directly to the mouse VLACSR and BAT gene promoters, and the promoter activities were dependent on HNF4␣-binding sites and HNF4␣ expression. In conclusion, HNF4␣ plays a central role in bile acid conjugation by direct regulation of VLACSR and BAT in vivo.

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Hepatocyte Nuclear Factor 4α Is a Central Regulator of Bile Acid Conjugation

Inoue

et al. 2004

Journal of Biological Chemistry

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“…Our laboratories have previously purified BAT activity from human liver (3) and cloned a cDNA encoding human BAT (hBAT) from a human liver cDNA library (4). Human BAT (hBAT) expressed in bacterial and COS cells utilizes both glycine and taurine as substrates (4). Additionally, our laboratories have cloned and expressed mouse BAT (mBAT) and determined its chromosomal location (5).…”

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“…The conjugation of bile acids with glycine or taurine is a two-step process involving the successive action of the enzymes bile acid CoA ligase (BAL) and bile acid CoA:amino acid N -acyltransferase (BAT). Our laboratories have previously purified BAT activity from human liver (3) and cloned a cDNA encoding human BAT (hBAT) from a human liver cDNA library (4). Human BAT (hBAT) expressed in bacterial and COS cells utilizes both glycine and taurine as substrates (4).…”

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confidence: 99%

Rat liver bile acid CoA:amino acid N-acyltransferase

Barnes

Falany

2003

Journal of Lipid Research

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Bile acid CoA:amino acid N -acyltransferase (BAT) is responsible for the amidation of bile acids with the amino acids taurine and glycine. Rat liver BAT (rBAT) cDNA was isolated from a rat liver ZAP cDNA library and expressed in Sf9 insect cells using a baculoviral vector. rBAT displayed 65% amino acid sequence homology with human BAT (hBAT) and 85% homology with mouse BAT (mBAT). Similar to hBAT, expressed rBAT was capable of forming both taurine and glycine conjugates with cholyl-CoA. mBAT, which is highly homologous to rBAT, forms only taurine conjugated bile acids ( Falany, C. N., H. Fortinberry, E. H. Leiter, and S. Barnes. 1997. Cloning and expression of mouse liver bile acid CoA: Amino acid N-acyltransferase. J. Lipid Res. 38: 86-95). Immunoblot analysis of rat tissues detected rBAT only in rat liver cytosol following homogenization and ultracentrifugation. Subcellular localization of rBAT detected activity and immunoreactive protein in both cytosol and isolated peroxisomes. Rat bile acid CoA ligase (rBAL), the enzyme responsible for the formation of bile acid CoA esters, was detected only in rat liver microsomes. Treatment of rats with clofibrate, a known peroxisomal proliferator, significantly induced rBAT activity, message, and immunoreactive protein in rat liver. Peroxisomal membrane protein-70, a marker for peroxisomes, was also induced by clofibrate, whereas rBAL activity and protein amount were not affected.In summary, rBAT is capable of forming both taurine and glycine bile acid conjugates and the enzyme is localized primarily in peroxisomes in rat liver. -He, D., S. Barnes, and C. N. Falany. Rat liver bile acid CoA:amino acid N -acyltransferase: expression, characterization, and peroxisomal localization.

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“…As mentioned above, acyl adenylate is an active intermediate in the metabolic reaction that converts carboxylic acid to the corresponding thioester. Rat liver bile acid CoA ligase has been cloned, and it shows affinity for deoxycholate binding (34). Furthermore, acyl-CoA synthetase, also known as ACS-5, which can produce bile acid acyl adenylates as intermediates, has been purified from rat intestinal epithelial cells and proliferating preadipocytes (35).…”

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confidence: 99%

A Nonenzymatic Modification of the Amino-terminal Domain of Histone H3 by Bile Acid Acyl Adenylate

Mano

Kasuga

Kobayashi

et al. 2004

Journal of Biological Chemistry

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Although it has been proposed that the secondary bile acids, deoxycholic acid and lithocholic acid, increase the number of aberrant crypt foci in the colon and may act as colon tumor promoters, there is little evidence detailing their mechanism of action. Histones play an important role in controlling gene expression, and the posttranslational modification of histones plays a role in regulation of intracellular signal transduction. In particular, the amino-terminal tail domain of histone H3 is sensitive to several posttranslational modifications, and acetylation of this domain changes its electrostatic environment and results in the loss of native folding. Therefore, we studied the modification of ⑀-amino groups on human histone H3 by deoxycholyl adenylate, which is an active intermediate in deoxycholyl thioester biosynthesis. After incubation of recombinant human histone H3 with a smaller amount of acyl adenylate, followed by enzymatic digestion, the peptide fragment mixtures were analyzed by matrix-assisted laser desorption ionization mass spectrometry. These data showed the formation of only one adduct fragment, which corresponded to amino acids 3-8 with a deoxycholate adduct, suggesting that the ⑀-amino group of Lys 4 had the highest reactivity. This novel modification, formation of a bile acid adduct on the histone H3 amino-terminal tail domain through an active acyl adenylate, may relate to the carcinogenesis-promoting effects of secondary bile acids.

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Molecular cloning and expression of rat liver bile acid CoA ligase

Cited by 31 publications

References 29 publications

Hepatocyte Nuclear Factor 4α Is a Central Regulator of Bile Acid Conjugation

Hepatocyte Nuclear Factor 4α Is a Central Regulator of Bile Acid Conjugation

Rat liver bile acid CoA:amino acid N-acyltransferase

A Nonenzymatic Modification of the Amino-terminal Domain of Histone H3 by Bile Acid Acyl Adenylate

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