The identification of two myoinhibitory peptides, with sequence similarities to the galanins, isolated from the ventral nerve cord of Manduca sexta.
Two new myoinhibitory peptides, Mas-MIP I and Mas-MIP II, were identified from the ventral nerve cord of the adult tobacco hornworm, Manduca sexta. Sequences obtained by a combination of automated Edman degradation and electrospray mass spectrometry were, respectively, AWQDLNSAW and GWQDLNSAW. The native peptides were found to co-elute with synthetic C-terminal amides on a reverse phase HPLC system. When applied to isolated ilea (anterior hindgut) of adult M. sexta, both peptides were found to significantly reduce the rate of peristalsis, or abolish peristalsis entirely, at concentrations of 1 x 10(-9) M. Both peptides share sequence similarities with Lom-MIP, a previously identified myoinhibitory peptide from Locusta migratoria, and with the N-terminal portion of vertebrate peptides in the galanin family.
D000005:Abdomen / Q000294:innervation; D000595:Amino Acid Sequence; D000818:Animals; D019004:Galanin / Q000737:chemistry*; D007301:Insect Hormones / Q000737:chemistry*; D019476:Insect Proteins; D018402:Manduca / Q000737:chemistry*; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000502:physiology; D009479:Neuropeptides / Q000032:analysis* / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D007301:Insect Hormones; D019476:Insect Proteins; C096411:Mas-MIP I peptide; C096412:Mas-MIP II peptide; D009479:Neuropeptides; C073324:locustamyoinhibiting peptide, Locusta migratoria; D019004:Galanin