Trehalose 6-phosphate synthase genes of the blue crab, Callinectes sapidus the molecular structure, the expression, its enzyme activity and relationship to hemolymph trehalose levels


Meeting Abstract

P1.156  Sunday, Jan. 4  Trehalose 6-phosphate synthase genes of the blue crab, Callinectes sapidus: the molecular structure, the expression, its enzyme activity and relationship to hemolymph trehalose levels CHUNG, J. Sook*; SHI, Q.; University of Maryland Biotechnology Institute, Baltimore chung@comb.umbi.umd.edu

Trehalose in ectoderms functions in energy metabolism and protection in extreme environmental conditions. We structurally characterized trehalose 6-phosphate synthase (TPS) from hemocytes of the blue crab, Callinectes sapidus. C. sapidus HemoTPS, like insect TPS, encodes both TPS and trehalose phosphate phosphatase domains. Trehalose seems to be a major sugar, as it shows higher level than glucose in hemocytes, hepatopancreas and hemolymph. Increases in HemoTPS expression, TPS enzyme activity in hemocytes, and hemolymph trehalose levels were determined 24 h after lipopolysaccharide challenge. The TPS gene has a wide tissue distribution in C. sapidus, suggesting multiple biosynthetic sites. A correlation between TPS activity in hemocytes and hemolymph trehalose levels was found during the molt cycle. Feeding and exercise showed immediate changes in this sugar levels in hemolymph and hepatopancreas. The current study provides the evidence of the presence of trehalose and TPS gene in hemocytes and hepatopancrease of C. sapidus and implicates its functional roles in energy metabolism and physiological adaptation.

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