351. Molecular identification of SGPP-5, a novel pacifastin-like peptide precursor in the desert locust.
- Author
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Simonet G, Claeys I, Van Soest S, Breugelmans B, Franssens V, De Loof A, and Vanden Broeck J
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Female, Gene Expression, Grasshoppers genetics, Male, Molecular Sequence Data, Peptides analysis, Peptides metabolism, Protein Precursors analysis, Protein Precursors genetics, Protein Precursors metabolism, Proteins chemistry, RNA, Messenger analysis, Sequence Alignment, Serine Proteinase Inhibitors analysis, Serine Proteinase Inhibitors metabolism, Tissue Distribution, Grasshoppers metabolism, Peptides genetics, Serine Proteinase Inhibitors genetics
- Abstract
Recently, a new serine protease inhibitor family has been described in arthropods. Eight members were purified from locusts and 13 peptides have been identified by cDNA cloning. The peptides share a conserved cysteine array (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-6)-Cys-Thr-Xaa(3)-Cys) with nine inhibitory domains (PLDs) of the light chain of the crayfish protease inhibitor, pacifastin. A molecular identification of a pacifastin-related precursor (SGPP-5) with three novel PLD-related peptides is presented in this study. This is a first report, identifying the presence of a SGPP-transcript in the brain, fore- and hindgut, including a 100-fold difference in fat body SGPP-transcript level of male as compared with female locust.
- Published
- 2004
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