DINeR

A Database for Insect Neuropeptide Research

Search the database for information about the various species and neuropeptides of interest

Insect Neuropeptides - Myosuppressin

Introduction

The first myosuppressin was isolated from the cockroach Leucophaea maderae using a hindgut contraction assay to test purified extract (Holman et al., 1986). The purified peptide was designated leucomyosuppressin (LMS) since it inhibited spontaneous contractions in the cockroach hindgut. Due to the common FLRFamide C-terminus the myosuppressins are also known as FLRFamides. Myosuppressins have subsequently been isolated as fairly well conserved decapeptides (X1DVX2HX3 –FLRFamide; X=variable) from numerous insects and the first precursor gene was cloned from the cockroach Diploptera punctata (Donly et al., 1993; Bendena et al., 1997). The Drosophila myosuppressin (DMS), with the sequence TDVDHVFLRFamide, was isolated biochemically (Nichols 1992) and a precursor gene (CG6440) encoding this peptide in a single copy identified later (Hewes and Taghert, 2001; Vanden Broek 2001). Two GPCRs responding to DMS have been identified in Drosophila, CG8985 and CG13803 (Egerod et al., 2003). Note that in insects the myosuppressins are encoded on distinct precursor genes and, thus, the grouping together with so called FMRFamides or FMRFamide-related peptides (FaRPs) encoded on at least 4 other genes is not functtioally relevant.

Location

In DrosophilaDMS is expressed in a small number of neurons in the pars intercerebralis (PI) and other parts of the brain, including optic lobes (Nichols 2003; Park et al., 2008). The crop, anterior gut and dorsal vessel (heart) are supplied by DMS immunolabeled axon terminations (Dickerson et al. 2012). Also in other insects the distribution of myosuppressins is restricted to few neurons. In the cockroach Diploptera punctata, for instance, LMS expressing neurons were found in brain (PI neurons) and optic lobes and frontal ganglion (Donly et al., 1993).

Function

Myosuppressins inhibit heart and visceral muscle in locusts (Orchard et al., 2001) and Drosophila (Dickerson et al. 2012) and ecdysone production in silkworm larvae (Yamanaka et al 2005). Extended FLRFamides have been detected in midgut endocrine cells of Locusta migratoria and Manduca sextaand expression levels fluctuate with nutritional status and parasite infection (see Orchard et al., 2001).

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Suggested Reviews

  • Orchard, I., Lange, A.B., and Bendena, W.G. (2001). FMRFamide-related peptides: a multifunctional family of structurally related neuropeptides in insects. Adv Insect Physiol 28, 267-329.
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  • Nichols, R. (2003). Signaling pathways and physiological functions of Drosophila melanogaster FMRFamide-related peptides. Annu Rev Entomol 48, 485-503.
    View Review
  • Walker, R.J., Papaioannou, S., and Holden-Dye, L. (2009). A review of FMRFamide- and RFamide-like peptides in metazoa. Invertebrate Neurosci 9, 111-153.
    View Review

References

  • Bendena, W.G., Donly, B.C., Fuse, M., Lee, E., Lange, A.B., Orchard, I., and Tobe, S.S. (1997). Molecular characterization of the inhibitory myotropic peptide leucomyosuppressin. Peptides 18, 157-163.
  • Dickerson, M., McCormick, J., Mispelon, M., Paisley, K., and Nichols, R. (2012). Structure-activity and immunochemical data provide evidence of developmental- and tissue-specific myosuppressin signaling. Peptides 36, 272-279.
  • Donly, B.C., Ding, Q., Tobe, S.S., and Bendena, W.G. (1993). Molecular cloning of the gene for the allatostatin family of neuropeptides from the cockroach Diploptera punctata. Proc Natl Acad Sci U S A 90, 8807-8811.
  • Egerod, K., Reynisson, E., Hauser, F., Cazzamali, G., Williamson, M., and Grimmelikhuijzen, C.J. (2003). Molecular cloning and functional expression of the first two specific insect myosuppressin receptors. Proc Natl Acad Sci U S A 100, 9808-9813.
  • Hewes, R.S., and Taghert, P.H. (2001). Neuropeptides and neuropeptide receptors in the Drosophila melanogaster genome. Genome Res 11, 1126-1142.
  • Holman, G.M., Cook, B.J., and Nachman, R.J. (1986 ). Isolation, primary structure and synthesis of leucomyosupressin, an insect neuropeptide that inhibits spontaneous contractions of the cockroach hindgut. Comp Biochem Physiol 85C 329-333.
  • Nichols, R. (2003). Signaling pathways and physiological functions of Drosophila melanogaster FMRFamide-related peptides. Annu Rev Entomol 48, 485-503.
  • Orchard, I., Lange, A.B., and Bendena, W.G. (2001). FMRFamide-related peptides: a multifunctional family of structurally related neuropeptides in insects. Adv Insect Physiol 28, 267-329.
  • Park, D., Veenstra, J.A., Park, J.H., and Taghert, P.H. (2008). Mapping peptidergic cells in Drosophila: where DIMM fits in. PLoS ONE 3, e1896.
  • Vanden Broeck, J. (2001). Neuropeptides and their precursors in the fruitfly, Drosophila melanogaster. Peptides 22, 241-254.
  • Nichols, R. (1992). Isolation and structural characterization of Drosophila TDVDHVFLRFamide and FMRFamide-containing neural peptides. J Mol Neurosci 3, 213-218.
  • Yamanaka, N., Hua, Y.J., Mizoguchi, A., Watanabe, K., Niwa, R., Tanaka, Y., and Kataoka, H. (2005). Identification of a novel prothoracicostatic hormone and its receptor in the silkworm Bombyx mori. J Biol Chem 280, 14684-14690.
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