Title: Isolation and characterization of schistostatin-2(11-18) from the desert locust, Schistocerca gregaria: A truncated analog of schistostatin-2
Authors: Veelaert, Dirk
Devreese, B
Vanden Broeck, Jozef
Yu, CG
Schoofs, Liliane
VanBeeumen, J
Tobe, SS
De Loof, Arnold # ×
Issue Date: Dec-1996
Publisher: Elsevier/North-Holland
Series Title: Regulatory Peptides vol:67 issue:3 pages:195-199
Abstract: An octapeptide was isolated from 7000 brains of the desert locust, Schistocerca gregaria by screening of HPLC fractions using a RIA for Dip-AST-2 (allatostatin-2 from the cockroach). Maldi-TOF-MS revealed a mass of 921.4 Da. The primary structure of the peptide is LPVYNFGL-NH2. It is identical to the C-terminal portion of schistostatin-2 from Schistocerca gregaria. Therefore, it was designated Scg-AST-2(11-18). The chromatographic properties of the synthetic peptide are identical to these of the native peptide. The peptide is a truncated product of Scg-AST-2, suggesting that an endopeptidase which cleaves between Arg and Leu is present in the brain complex of S. gregaria. Although, Scg-AST-2(11-18) contains the same C-terminus as Dip-AST-2, it has no inhibitory activity on the corpora allata (CA) of 2-day-old virgin females of D. punctata. This suggests that Scg-AST-2(11-18) may be the result of a proteolytic inactivation mechanism and/or that it may be involved in stage-dependent down regulation of allatostatic activity. To our knowledge, Scg-AST-2 is the first isolated peptide which has the active core of the allatostatin peptide family but nevertheless shows no activity in this bioassay.
ISSN: 0167-0115
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Animal Physiology and Neurobiology Section - miscellaneous
Department of Biology - miscellaneous
× corresponding author
# (joint) last author

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