Title: Identification and characterization of Eci3, a murine kidney‐specific Δ<sup>3</sup>, Δ<sup>2</sup>‐enoyl‐CoA isomerase
Abstract: The FASEB JournalVolume 28, Issue 3 p. 1365-1374 Research CommunicationFree to Read Identification and characterization of Eci3, a murine kidney-specific Δ3, Δ2-enoyl-CoA isomerase Michel van Weeghel, Michel van Weeghel Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorRob Ofman, Rob Ofman Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorCarmen A. Argmann, Carmen A. Argmann Department of Medical Biochemistry, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorJos P. N. Ruiter, Jos P. N. Ruiter Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorNike Claessen, Nike Claessen Department of Pathology, Academic Medical Center, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorSaskia V. Oussoren, Saskia V. Oussoren Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorRonald J. A. Wanders, Ronald J. A. Wanders Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The Netherlands Department of Pediatrics, Emma Children's Hospital, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorJan Aten, Jan Aten Department of Pathology, Academic Medical Center, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorSander M. Houten, Corresponding Author Sander M. Houten [email protected] Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The Netherlands Department of Pediatrics, Emma Children's Hospital, University of Amsterdam, Amsterdam, The NetherlandsCorrespondence: Department of Genetics and Genomic Sciences, Icahn Institute for Genomics and Multiscale Biology, Icahn School of Medicine at Mt. Sinai, 1425 Madison Ave., Box 1498, New York, NY 10029, USA. E-mail: [email protected]Search for more papers by this author Michel van Weeghel, Michel van Weeghel Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorRob Ofman, Rob Ofman Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorCarmen A. Argmann, Carmen A. Argmann Department of Medical Biochemistry, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorJos P. N. Ruiter, Jos P. N. Ruiter Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorNike Claessen, Nike Claessen Department of Pathology, Academic Medical Center, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorSaskia V. Oussoren, Saskia V. Oussoren Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorRonald J. A. Wanders, Ronald J. A. Wanders Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The Netherlands Department of Pediatrics, Emma Children's Hospital, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorJan Aten, Jan Aten Department of Pathology, Academic Medical Center, University of Amsterdam, Amsterdam, The NetherlandsSearch for more papers by this authorSander M. Houten, Corresponding Author Sander M. Houten [email protected] Department of Clinical Chemistry, Laboratory of Genetic Metabolic Diseases, University of Amsterdam, Amsterdam, The Netherlands Department of Pediatrics, Emma Children's Hospital, University of Amsterdam, Amsterdam, The NetherlandsCorrespondence: Department of Genetics and Genomic Sciences, Icahn Institute for Genomics and Multiscale Biology, Icahn School of Medicine at Mt. Sinai, 1425 Madison Ave., Box 1498, New York, NY 10029, USA. E-mail: [email protected]Search for more papers by this author First published: 16 December 2013 https://doi.org/10.1096/fj.13-240416Citations: 8 This article includes supplemental data. Please visit http://www.fasebj.org to obtain this information. Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract Oxidation of unsaturated fatty acids requires the action of auxiliary enzymes, such as Δ3, Δ2-enoyl-CoA isomerases. Here we describe a detailed biochemical, molecular, histological, and evolutionary characterization of Eci3, the fourth member of the mammalian enoyl-CoA isomerase family. Eci3 specifically evolved in rodents after gene duplication of Eci2. Eci3 is with 79% identity homologous to Eci2 and contains a peroxisomal targeting signal type 1. Subcellular fractionation of mouse kidney and immunofluorescence studies revealed a specific peroxisomal localization for Eci3. Expression studies showed that mouse Eci3 is almost exclusively expressed in kidney. By using immunohistochemistry, we found that Eci3 is not only expressed in cells of the proximal tubule, but also in a subset of cells in the tubulointerstitium and the glomerulus. In vitro, Eci3 catalyzed the isomerization of trans-3-nonenoyl-CoA to trans-2-nonenoyl-CoA equally efficient as Eci2, suggesting a role in oxidation of unsaturated fatty acids. However, in contrast to Eci2, in silico gene coexpression and enrichment analysis for Eci3 in kidney did not yield carboxylic acid metabolism, but diverse biological functions, such as ion transport (P=7.1E-3) and tissue morphogenesis (P= 1.0E-3). Thus, Eci3 picked up a novel and unexpected role in kidney function during rodent evolution.—van Weeghel, M., Ofman, R., Argmann, C. A., Ruiter, J. P. N., Claessen, N., Oussoren, S. V., Wanders, R. J. A., Aten, J., Houten, S. M. Identification and characterization of Eci3, a murine kidney-specific Δ3, Δ2-enoyl-CoA isomerase. FASEB J. 28, 1365–1374 (2014). www.fasebj.org Citing Literature Supporting Information Filename Description fsb2028003029-sup-0001.zipZip archive, 4.5 MB Supplementary material Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article. Volume28, Issue3March 2014Pages 1365-1374 RelatedInformation
Publication Year: 2013
Publication Date: 2013-12-16
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 9
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