دورية أكاديمية
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Functional characterization of enzymes catalyzing ceramide phosphoethanolamine biosynthesis in mice.

التفاصيل البيبلوغرافية
العنوان: Functional characterization of enzymes catalyzing ceramide phosphoethanolamine biosynthesis in mice.
المؤلفون: Bickert A; Molecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany., Ginkel C; Molecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany., Kol M; Molecular Cell Biology Division, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany., vom Dorp K; Institute of Molecular Physiology and Biotechnology of Plants, University of Bonn, 53115 Bonn, Germany., Jastrow H; Imaging Center Essen, Electron Microscopy Unit, University Hospital University of Duisburg-Essen, 45147 Essen, Germany., Degen J; Molecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany., Jacobs RL; Departments of Agricultural, Food, and Nutritional Science, Molecular and Cell Biology of Lipids, University of Alberta, T6G 2S2 Edmonton, Canada., Vance DE; Biochemistry, University of Alberta, T6G 2S2 Edmonton, Canada., Winterhager E; Department of Molecular Biology, University of Duisburg-Essen, 45147 Essen, Germany., Jiang XC; Department of Anatomy and Cell Biology, SUNY Downstate Medical Center, Brooklyn, NY 11203., Dörmann P; Institute of Molecular Physiology and Biotechnology of Plants, University of Bonn, 53115 Bonn, Germany., Somerharju P; Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, Finland., Holthuis JC; Molecular Cell Biology Division, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany., Willecke K; Molecular Genetics, Life, and Medical Sciences Institute University of Bonn, 53115 Bonn, Germany.
المصدر: Journal of lipid research [J Lipid Res] 2015 Apr; Vol. 56 (4), pp. 821-35. Date of Electronic Publication: 2015 Feb 09.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: United States NLM ID: 0376606 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1539-7262 (Electronic) Linking ISSN: 00222275 NLM ISO Abbreviation: J Lipid Res Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York] : Elsevier
Original Publication: Memphis, Lipid Research, inc.
مواضيع طبية MeSH: Biocatalysis*, Sphingomyelins/*biosynthesis , Transferases (Other Substituted Phosphate Groups)/*metabolism, Animals ; Brain/cytology ; Brain/enzymology ; Brain/metabolism ; Catalytic Domain ; Cell Survival ; Enzyme Activation ; Exons/genetics ; Gene Deletion ; Gene Expression Regulation, Enzymologic ; Liver/cytology ; Liver/enzymology ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Organ Specificity ; Phosphatidylethanolamine N-Methyltransferase/metabolism ; Point Mutation ; Protein Transport ; Sphingomyelins/metabolism ; Transferases (Other Substituted Phosphate Groups)/chemistry ; Transferases (Other Substituted Phosphate Groups)/deficiency ; Transferases (Other Substituted Phosphate Groups)/genetics
مستخلص: Besides bulk amounts of SM, mammalian cells produce small quantities of the SM analog ceramide phosphoethanolamine (CPE). Little is known about the biological role of CPE or enzymes responsible for CPE production. Heterologous expression studies revealed that SM synthase (SMS)2 is a bifunctional enzyme producing both SM and CPE, whereas SMS-related protein (SMSr) serves as monofunctional CPE synthase. Acute disruption of SMSr catalytic activity in cultured cells causes a rise in endoplasmic reticulum (ER) ceramides, fragmentation of ER exit sites, and induction of mitochondrial apoptosis. To address the relevance of CPE biosynthesis in vivo, we analyzed the tissue-specific distribution of CPE in mice and generated mouse lines lacking SMSr and SMS2 catalytic activity. We found that CPE levels were >300-fold lower than SM in all tissues examined. Unexpectedly, combined inactivation of SMSr and SMS2 significantly reduced, but did not eliminate, tissue-specific CPE pools and had no obvious impact on mouse development or fertility. While SMSr is widely expressed and serves as the principal CPE synthase in the brain, blocking its catalytic activity did not affect ceramide levels or secretory pathway integrity in the brain or any other tissue. Our data provide a first inventory of CPE species and CPE-biosynthetic enzymes in mammals.
(Copyright © 2015 by the American Society for Biochemistry and Molecular Biology, Inc.)
التعليقات: Erratum in: J Lipid Res. 2017 Apr;58(4):820. (PMID: 28365667)
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معلومات مُعتمدة: MOP5182 Canada Canadian Institutes of Health Research
فهرسة مساهمة: Keywords: brain lipids; enzyme inactivation; genetics; mass spectrometry; sphingolipids; sphingomyelin synthase; sphingomyelin synthase-related protein; sterile α motif domain-containing protein 8; transgenic mice
المشرفين على المادة: 0 (Sphingomyelins)
112130-78-6 (ceramide phosphoethanolamine)
EC 2.1.1.17 (Phosphatidylethanolamine N-Methyltransferase)
EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups))
EC 2.7.8.27 (Sgms2 protein, mouse)
تواريخ الأحداث: Date Created: 20150211 Date Completed: 20151218 Latest Revision: 20210217
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC4373740
DOI: 10.1194/jlr.M055269
PMID: 25667419
قاعدة البيانات: MEDLINE
الوصف
تدمد:1539-7262
DOI:10.1194/jlr.M055269