Molecular characterization of the inhibitory myotropic peptide leucomyosuppressin

Peptides. 1997;18(1):157-63. doi: 10.1016/s0196-9781(96)00237-9.

Abstract

The myoinhibitory peptide leucomyosuppressin (LMS) (pQDVDHVFLRFamide) has been identified and characterized at the molecular level in the cockroach Diploptera punctata through analysis of the organization of both brain cDNA and genomic DNA. Processing of the precursor predicted from DNA sequence would release a single LMS peptide. The organization of the precursor appears to be conserved in other insects and may reflect a functional organization for this subfamily of extended FLRFamides. The expression of the LMS gene appears in numerous cells of the pars-intercerebralis of the cockroach protocerebellum as well as in numerous endocrine cells of the midgut.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Brain / metabolism
  • Cockroaches / chemistry*
  • Genes, Insect
  • In Situ Hybridization
  • Insect Hormones / chemistry
  • Molecular Sequence Data
  • Neuropeptides / chemistry*
  • Neuropeptides / genetics
  • Oligopeptides / chemistry
  • Protein Precursors / chemistry
  • Protein Precursors / metabolism
  • Protein Processing, Post-Translational

Substances

  • Insect Hormones
  • Neuropeptides
  • Oligopeptides
  • Protein Precursors
  • leucomyosuppressin
  • phenylalanyl-leucyl-arginyl phenylalaninamide