ArticleBiochimie2011
Molecular cloning and characterization of neutral ceramidase homologue from the red flour beetle, Tribolium castaneum.
Article in Biochimie, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Insect Lipids: Structure, Classification and Function.Advances in experimental medicine and biology · 2026Review
- Alkaline ceramidase (Frontiers in physiology · 2023Article
- Neutral Ceramidase Is Required for the Reproduction of Brown Planthopper,Frontiers in physiology · 2021Article
- A neutral ceramidase, NlnCDase, is involved in the stress responses of brown planthopper, Nilaparvata lugens (Stål).Scientific reports · 2018Article
- Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase.Insect molecular biology · 2013Article
- Triangulated mal-signaling in Alzheimer's disease: roles of neurotoxic ceramides, ER stress, and insulin resistance reviewed.Journal of Alzheimer's disease : JAD · 2012Review
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Ceramidase plays an important role in regulating the metabolism of sphingolipids, such as ceramide, sphingosine (SPH), and sphingosine-1-phosphate (S1P), by controlling the hydrolysis of ceramide. Here we report the cloning and biochemical characterization of a neutral ceramidase from the red flour beetle Tribolium castaneum which is an important storage pest. The Tribolium castaneum neutral ceramidase (Tncer) is a protein of 696 amino acids. It shares a high degree of similarity in protein sequence to neutral ceramidases from various species. Tncer mRNA levels are higher in the adult stage than in pre-adult stages, and they are higher in the reproductive organs than in head, thorax, and midgut. The mature ovary has higher mRNA levels than the immature ovary. Tncer is localized to the plasma membrane. It uses various ceramides (D-erythro-C(6), C(12), C(16), C(18:1), and C(24:1)-ceramide) as substrates and has an abroad pH optimum for its in vitro activity. Tncer has an optimal temperature of 37 °C for its in vitro activity. Its activity is inhibited by Fe(2+). These results suggest that Tncer has distinct biochemical properties from neutral ceramidases from other species.
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