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0302 Molecular cloning and characteriation of neutral ceramidase homoluge from the red flour beetle (Tribolium castaneum)

Monday, December 13, 2010: 10:08 AM
Sunrise (Town and Country Hotel and Convention Center)
Ying Zhou , Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
Xianwen Lin , Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
Qiong Yang , Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
Yanru Zhang , Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
Jingqun Yuan , Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
Xinda Lin , College of Life Sciences, China Jiliang University, Hangzhou, Zhejiang, China
Jiaan Chen , Institute of Insect Sciences, Zhejiang University, Hangzhou, Zhejiang, China
Cungui Mao , Department of Medicine and Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC
Zengrong Zhu , Institute of Insect Sciences, Zhejiang University, Hangzhou, China
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 ceramides. Here we report the cloning and biochemical characterization of a neutral ceramidase from the red flour beetle Tribolium castaneum. 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-C6, C12, C16, C18:1, and C24:1-ceramide) as substrates and has an abroad pH optimum for its in vitro activity. Tncer has an optimal temperature of 37 degree centigree for its in vitro activity. Its activity is inhibited by Fe2+>. These results suggest that Tncer has distinct biochemical properties from neutral ceramidases from other species.

doi: 10.1603/ICE.2016.49284

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