{"database":"biostudies-arrayexpress","file_versions":[],"scores":null,"additional":{"submitter":["Single Cell Omics Platform CBMR"],"organism":["Mus musculus"],"software":["Subread v1.6.4"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/E-MTAB-15752"],"description":["This study aimed to investigate the overlap between hepatic NAT and the bile acid synthesis to identify additional enzymes involved in NAT synthesis in the liver. We sequenced livers high-fat fed mice the were either wild-type or with a single-amino acid substitution in fatty acid amide hydrolase (FAAH S268D), as described in https://doi.org/10.1073/pnas.1916288116."],"repository":["biostudies-arrayexpress"],"sample_protocol":["Sequencing - Libraries were quality-controlled using a Bioanalyzer instrument (Agilent Technologies) and subjected to 51-bp paired-end sequencing on a NovaSeq 6000 system (Illumina).","Library Construction - Total RNA sequencing libraries were prepared using the Illumina TruSeq Stranded total RNA Gold protocol (Illumina). The total RNA was depleted of rRNA by RiboZero beads, fragmented, and cDNA was synthesized using SuperScript III Reverse Transcriptase (Thermo Fisher Scientific). cDNA was adenylated to prime for adapter ligation and after a clean-up using AMPure beads (Beckman coulter), DNA fragments were amplified using PCR followed by a final clean-up.","Nucleic Acid Extraction - RNA was isolated and purified with RNeasy kit (Quiagen)","Sample Collection - Livers of WT and FAAH-S268D mice that were fed for 3 days a HFD were used for RNA sequencing."],"figure_sub":["Organization","MINSEQE Score","Assays and Data","Processed Data","MAGE-TAB Files"],"data_protocol":["Data Transformation - Uploaded data is raw reads, each row is a gene and each column is a sample. No normalization has been performed.","Sequence Alignment - FASTQ-files were analyzed using the Subread suite of software v1.6.4. Reads were aligned using the Subjunc tool against mm10 and the GENCODE vM21 gene model using default parameters.  Reads were summarized to genes using featureCounts counting only uniquely mapped reads where both ends map, are overlapping a single feature, are mapped in a reverse-stranded manner and where both end map to the same chromosome."],"omics_type":["Metabolomics","Unknown","Transcriptomics","Genomics","Proteomics"],"instrument_platform":["Illumina NovaSeq 6000"],"pubmed_abstract":["N-acyl taurines (NAT) are endogenous, bioactive conjugates of fatty acids and taurine with roles in carbohydrate and lipid metabolism. In the liver, NATs are synthesized by bile acid-CoA:amino acid N-acyltransferase (BAAT), which also conjugates bile acids to taurine or glycine, suggesting an overlapping hepatic synthesis pathway. BAAT catalyzes the transfer of an acyl-chain from an activated coenzyme A (CoA) to taurine, but the hepatic enzyme responsible for synthesizing the acyl-CoA remains unknown. Using liver transcriptomics in mice unable to hydrolyze NATs, we identified Slc27a5, which encodes the acyl-CoA synthetase, fatty acid transport protein 5 (FATP5), as a potential regulator of hepatic NAT synthesis. In vivo knockdown of the enzyme confirmed that FATP5 is necessary for hepatic NAT synthesis and upstream of BAAT, likely through its acyl-CoA synthetase activity. The dual function of this enzyme in activating both fatty acids and bile acids for conjugation identifies a functional overlap between the hepatic NAT and bile acid production pathway."],"study_type":["RNA-seq of coding RNA"],"species":["Mus musculus"],"pubmed_title":["The bile acid CoA ligase, FATP5, is necessary for NAT synthesis in the liver"],"pubmed_authors":["Katharina Barbara Kuentzel, Samuel Addison Jack Trammel, Anna Skaab Hassing, Kathleen Tchoukoua, Matthew Gillum, Benny Garfinkel, Ivan Bradić, Martin Røssel Larsen, Trisha Jean Grevengoed","Trisha Grevengoed","Katharina Kuentzel","Single Cell Omics Platform CBMR"],"additional_accession":[]},"is_claimable":false,"name":"The bile acid CoA ligase, FATP5, is necessary for NAT synthesis in the liver","description":"This study aimed to investigate the overlap between hepatic NAT and the bile acid synthesis to identify additional enzymes involved in NAT synthesis in the liver. We sequenced livers high-fat fed mice the were either wild-type or with a single-amino acid substitution in fatty acid amide hydrolase (FAAH S268D), as described in https://doi.org/10.1073/pnas.1916288116.","dates":{"release":"2026-03-02T00:00:00Z","modification":"2026-03-03T07:22:53.074Z","creation":"2025-10-16T11:14:03.575Z"},"accession":"E-MTAB-15752","cross_references":{"ENA":["ERP182292"],"EFO":["EFO_0002944","EFO_0004170","EFO_0004917","EFO_0005518","EFO_0003816","EFO_0003738","EFO_0004184"],"doi":["10.1016/j.jlr.2026.101012"]}}