ArticleThe Journal of biological chemistry2009
A novel mitochondrial sphingomyelinase in zebrafish cells.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.
- Meta-Analysis of QTL Mapping and GWAS Reveal Candidate Genes for Heat Tolerance in Small Yellow Croaker,International journal of molecular sciences · 2025Pooled it
- Fasting the mitochondria to prevent neurodegeneration: the role of ceramides.Frontiers in neuroscience · 2025Review
- Regulation of cellular and systemic sphingolipid homeostasis.Nature reviews. Molecular cell biology · 2024Review
- Zebra-Sphinx: Modeling Sphingolipidoses in Zebrafish.International journal of molecular sciences · 2023Review
- Compartmentalization of Sphingolipid metabolism: Implications for signaling and therapy.Pharmacology & therapeutics · 2022Review
- The Role of Sphingolipid Signaling in Oxidative Lung Injury and Pathogenesis of Bronchopulmonary Dysplasia.International journal of molecular sciences · 2022Review
- Acid and Neutral Sphingomyelinase Behavior in Radiation-Induced Liver Pyroptosis and in the Protective/Preventive Role of rMnSOD.International journal of molecular sciences · 2020Article
- Ceramide and Ischemia/Reperfusion Injury.Journal of lipids · 2018Review
- Sphingolipids in mitochondria.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Lactosylceramide contributes to mitochondrial dysfunction in diabetes.Journal of lipid research · 2016Article
- Critical determinants of mitochondria-associated neutral sphingomyelinase (MA-nSMase) for mitochondrial localization.Biochimica et biophysica acta · 2015Article
- Neutral sphingomyelinase and breast cancer research.Journal of menopausal medicine · 2015Review
- Stress-induced ceramide generation and apoptosis via the phosphorylation and activation of nSMase1 by JNK signaling.Cell death and differentiation · 2015Article
- Sphingolipids and mitochondrial function, lessons learned from yeast.Microbial cell (Graz, Austria) · 2014Review
- Bioanalysis of eukaryotic organelles.Chemical reviews · 2013Review
- Sphingolipid metabolism and neutral sphingomyelinases.Handbook of experimental pharmacology · 2013Review
- Induction of autophagy by amino acid starvation in fish cells.Marine biotechnology (New York, N.Y.) · 2012Article
- Article
- Novel pathway of ceramide production in mitochondria: thioesterase and neutral ceramidase produce ceramide from sphingosine and acyl-CoA.The Journal of biological chemistry · 2011Article
- Identification of novel anionic phospholipid binding domains in neutral sphingomyelinase 2 with selective binding preference.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sphingolipids are important signaling molecules in many biological processes, but little is known regarding their physiological roles in the mitochondrion. We focused on the biochemical characters of a novel sphingomyelinase (SMase) and its function in mitochondrial ceramide generation in zebrafish embryonic cells. The cloned SMase cDNA encoded a polypeptide of 545 amino acid residues (putative molecular weight, 61,300) containing a mitochondrial localization signal (MLS) and a predicted transmembrane domain. The mature endogenous enzyme was predicted to have a molecular weight of 57,000, and matrix-assisted laser de sorption ionization time-of-flight mass spectrometry analysis indicated that the N-terminal amino acid residue of the mature enzyme was Ala-36. The purified enzyme optimally hydrolyzed [(14)C]sphingomyelin in the presence of 10 mm Mg(2+) at pH 7.5. In HEK293 cells that overexpressed SMase cDNA, the enzyme was localized to the mitochondrial fraction, whereas mutant proteins lacking MLS or both the MLS and the transmembrane domain were absent from the mitochondrial fraction. Endogenous SMase protein co-localized with a mitochondrial cytostaining marker. Using a protease protection assay, we found that SMase was distributed throughout the intermembrane space and/or the inner membrane of the mitochondrion. Furthermore, the overexpression of SMase in HEK293 cells induced ceramide generation and sphingomyelin hydrolysis in the mitochondrial fraction. Antisense phosphorothioate oligonucleotide-induced knockdown repressed ceramide generation and sphingomyelin hydrolysis in the mitochondrial fraction in zebrafish embryonic cells. These observations indicate that SMase catalyzes the hydrolysis of sphingomyelin and generates ceramide in mitochondria in fish cells.
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Registered trials
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