Mj. Loeb et al., STRUCTURE-FUNCTION ANALYSIS LYMANTRIA TESTIS ECDYSIOTROPIN - A SEARCHFOR THE ACTIVE CORE, Archives of insect biochemistry and physiology, 38(1), 1998, pp. 11-18
A structure-function study was performed on the synthetic 21 residue n
europeptide, Lymantria testis ecdysiotropin (LTE), originally isolated
from brains of Lymantria dispar pupae. The peptide induces ecdysteroi
d synthesis by testis sheaths of various lepidopteran species. LTE, as
well as synthetic LTE 1-11, 11-21, and 11-15, stimulated synthesis in
larval and pupal testes of Lymantria dispar at concentrations of 10(-
9) to 10(15) M; LTE 16-21 was weakly active, and an elongated LEU-LTE
was inhibitory to synthesis at all but extremely low concentrations (1
0(15)M). Since the sequence and polarity of residues in LTE 1-11, 11-1
5, and 11-21 are quite different, several parts of the molecule must a
ctivate receptors which initiate the cascade, resulting in ecdysiogene
sis in Lepidopteran testes. (C) 1998 Wiley-Liss, Inc.