The identification of two myoinhibitory peptides, with sequence similarities to the galanins, isolated from the ventral nerve cord of Manduca sexta

M B Blackburn; R M Wagner; J P Kochansky; D J Harrison; P Thomas-Laemont; A K Raina

doi:10.1016/0167-0115(95)00034-9

The identification of two myoinhibitory peptides, with sequence similarities to the galanins, isolated from the ventral nerve cord of Manduca sexta

Regul Pept. 1995 Jun 27;57(3):213-9. doi: 10.1016/0167-0115(95)00034-9.

Authors

M B Blackburn¹, R M Wagner, J P Kochansky, D J Harrison, P Thomas-Laemont, A K Raina

Affiliation

¹ Insect Neurobiology and Hormone Laboratory, USDA, Beltsville, MD 20705, USA.

PMID: 7480870
DOI: 10.1016/0167-0115(95)00034-9

Abstract

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.

MeSH terms

Abdomen / innervation
Amino Acid Sequence
Animals
Galanin / chemistry*
Insect Hormones / chemistry*
Insect Proteins*
Manduca / chemistry*
Molecular Sequence Data
Muscle Contraction / physiology
Neuropeptides / analysis*
Neuropeptides / chemistry*
Sequence Homology, Amino Acid

Substances

Insect Hormones
Insect Proteins
Mas-MIP I peptide
Mas-MIP II peptide
Neuropeptides
locustamyoinhibiting peptide, Locusta migratoria
Galanin