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Identification and Characterization of a Sphingolipid Δ4-Desaturase Family
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Sphingolipids desaturated at the Delta4-position are important signaling molecules in many eukaryotic organisms, including mammals. In a bioinformatics approach, we now identified a new family of protein sequences from animals, plants, and fungi and characterized these sequences biochemically by expression in Saccharomyces cerevisiae. This resulted in the identification of the enzyme sphingolipid Delta4-desaturase (dihydroceramide desaturase) from Homo sapiens, Mus musculus, Drosophila melanogaster, and Candida albicans, in addition to a bifunctional sphingolipid Delta4-desaturase/C-4-hydroxylase from M. musculus. Among the sequences investigated are the Homo sapiens membrane lipid desaturase, the M. musculus degenerative spermatocyte, and the Drosophila melanogaster degenerative spermatocyte proteins. During spermatogenesis, but not oogenesis of des mutant flies, both cell cycle and spermatid differentiation are specifically blocked at the entry into the first meiotic division, leading to male sterility. This mutant phenotype can be restored to wild-type by complementation with a functional copy of the des gene (Endo, K., Akiyama, T., Kobayashi S., and Okada, M. (1996) Mol. Gen. Genet. 253, 157-165). These results suggest that Delta4-desaturated sphingolipids provide an early signal necessary to trigger the entry into both meiotic and spermatid differentiation pathways during Drosophila spermatogenesis.
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“Sphingosine-and phytosphingosine-type ceramides are generated either via desaturation between the 4 and 5 positions of the LCB moiety of dihydroceramides (DS ceramides) by the desaturase DEGS1, or via hydroxylation of the same moiety at the 4 position by the hydroxylase DEGS2 (49,50).”
From Comparative profiling and comprehensive quantification of stratum corneum ceramides in humans and mice by LC/MS/MS (2020) · cites this paper as [50]
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Metadata
- Authors
- Ternes, P., Franke, S., Zähringer, U., Sperling, P., & Heinz, E.
- Affiliations
- Universität Hamburg (DE)
- Research Center Borstel - Leibniz Lung Center (DE)
- Corresponding author
- Heinz, Ernst
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-07
- Volume
- 277
- Issue
- 28
- Pages
- 25512-25518
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1987888500
- Cited by
- 293
- References
- 46
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 17 · 2023: 24 · 2022: 12 · 2021: 15 · 2020: 9 · 2019: 11 · 2018: 12 · 2017: 8 · 2016: 11 · 2015: 10 · 2014: 9 · 2013: 9 · 2012: 8
- FWCI
- 5.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- Clemson University
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Lawrence Livermore National Laboratory
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
- Keywords
- dihydroceramide desaturase, spermatogenesis, meiotic entry, spermatid differentiation, male sterility, lipid signaling
- MeSH terms
- Animals, Base Sequence, Chromatography, High Pressure Liquid, Humans, Male, Molecular Sequence Data, Oxidoreductases, Phylogeny, Spermatogenesis, Sphingolipids, DNA Primers
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