nEUROSTRESSPEP logo

DINeR

A Database for Insect Neuropeptide Research

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

Insect Neuropeptides - Diapause hormone

Introduction

Diapause Hormone (DH) is known to induce or inhibit of insect diapause, depending on species (Sato et al., 1994; Zhang et al., 2011) and is a peptide of pyrokinin type, encoded on a precursor with several peptides that have been given different functional names. In the following information is provided on DH and these other pyrokinin-type peptides. A pyrokinin was first identified from the cockroach Leucophaea maderae and named leucopyrokinin (LPK) because it has an N-terminal pyroglutamate and activates the cockroach hindgut (Holman et al., 1986). Later several other peptides were isolated with the characteristic C-terminus FXPRLamide and since no PK precursor gene was yet known these peptides were named after their functions: Pheromone Biosynthesis Activating Neuropeptides (PBAN), Diapause Hormone (DH), Melanization and Reddish Coloration Hormone (MRCH) and so on. This has caused some confusion and for simplicity we refer to these peptides as pyrokinins, based on the founding member of the family. Now that such genes have been identified in many insects it is possible to assign relationships. Pheromone biosynthesis activating neuropeptide (PBAN) and diapause hormone (DH) are N-terminally extended pyrokinins found primarily in Lepidoptera and have specific neuronal or hormonal functions. The PBAN precursors of Bombyx mori and Heliotis zea each encode five peptides with a FXPRLamide or FXPKLamide C-terminus, thus representing isoforms of pyrokinin/PBAN (Sato et al., 1993; Ma et al., 1994). In each of these precursors, one peptide corresponds to DH and another to PBAN; the remaining three are shorter pyrokinin-like peptides. Some earlier studies designated PKs as myotropins. In Drosophila two genes are known to encode PKs, the hugin and Capa genes (Meng et al., 2002; Kean et al., 2002). The hugin gene encodes hugin-PK (PK-2; SVPFKPRLamide) and hugin γ (pQLQSNGEPAYRVRTPRLamide), but only the former has been identified by mass spectrometry (Meng et al., 2002; Neupert et al., 2007). Of the two Drosophila genes the hugin gene is considered related to genes encoding PK/PBANs (Bader et al., 2007). There are three known receptors for PKs in Drosophila, the CAPA-PK receptor (CG9918) and two Hugin-PK receptors (CG8795 and CG8784) (Hauser et al., 2006).

Location

The pyrokinins (and PBAN, DH) are primarily produced by a small set of neurons in the subesophageal ganglion of insects investigated (Choi et al., 2001; Raina and Menn, 1993). A subset of these neurons are neurosecretory cells with axon terminations in neurohemal release sites, and thus responsible for hormonal release of PK type peptides. In Drosophila the Hugin-PK expressing neurons have been extensively investigated anatomically and functionally (Bader et al., 2007).

Function

The first identified functions of PKs in insects were myostimulatory activity on visceral muscle, including oviduct muscle (Holman et al., 1986). Later it was found that PBAN was regulating pheromone biosynthesis (Raina and Menn, 1993) and DH induction or inhibition of insect diapause, depending on species (Sato et al., 1994; Zhang et al., 2011). PKs were also found to be the long-sought pupariation factor in flies (Zdarek et al., 1997). The first analysis of the hugin gene suggested a role in the ecdysis process (Meng et al., 2002), later is was found that the Hugin expressing neurons receive gustatory inputs and regulate feeding (Melcher and Pankratz, 2005). There are no studies on the specific function of the CAPA-PK (PK1). The pyrokinins/PBANs have been extensively explored to develop biostable analogs to be used in insect pest control (Altstein et al., 2007).

SeqLogo and Cladogram

Click above image to go to SeqLogo and Cladogram page

Suggested Reviews

  • Holman GM, Nachman RJ, Wright MS. 1990. Insect neuropeptides. Annu Rev Entomol 35:201-217.
    View Review
  • Rafaeli A. 2009. Pheromone biosynthesis activating neuropeptide (PBAN): regulatory role and mode of action. Gen Comp Endocrinol 162(1):69-78.
    View Review
  • Altstein M, Ben-Aziz O, Zeltser I, Bhargava K, Davidovitch M, Strey A, Pryor N, Nachman RJ. 2007. Inhibition of PK/PBAN-mediated functions in insects: discovery of selective and non-selective inhibitors. Peptides 28(3):574-584.
    View Review

References

  • Altstein M, Ben-Aziz O, Zeltser I, Bhargava K, Davidovitch M, Strey A, Pryor N, Nachman RJ. 2007. Inhibition of PK/PBAN-mediated functions in insects: discovery of selective and non-selective inhibitors. Peptides 28(3):574-584.
  • Bader R, Wegener C, Pankratz MJ. 2007. Comparative neuroanatomy and genomics of hugin and pheromone biosynthesis activating neuropeptide (PBAN). Fly (Austin) 1(4):228-231.
  • Choi MY, Rafaeli A, Jurenka RA. 2001. Pyrokinin/PBAN-like peptides in the central nervous system of Drosophila melanogaster. Cell Tissue Res 306(3):459-465.
  • Hauser F, Cazzamali G, Williamson M, Blenau W, Grimmelikhuijzen CJ. 2006. A review of neurohormone GPCRs present in the fruitfly Drosophila melanogaster and the honey bee Apis mellifera. Progr Neurobiol 80(1):1-19.
  • Holman GM, Cook BJ, Nachman RJ. 1986. Primary structure and synthesis of a blocked myotropic neuropeptide isolated from the cockroach, Leucophaea maderae. Comp Biochem Physiol C 85(1):219-224.
  • Kean L, Cazenave W, Costes L, Broderick KE, Graham S, Pollock VP, Davies SA, Veenstra JA, Dow JA. 2002. Two nitridergic peptides are encoded by the gene capability in Drosophila melanogaster. American journal of physiology Regulatory, integrative and comparative physiology 282(5):R1297-1307.
  • Ma PW, Knipple DC, Roelofs WL. 1994. Structural organization of the Helicoverpa zea gene encoding the precursor protein for pheromone biosynthesis-activating neuropeptide and other neuropeptides. Proc Natl Acad Sci U S A 91(14):6506-6510.
  • Melcher, C., Pankratz,M.J.,2005.Candidate gustatory interneurons modulating feeding behavior in the Drosophila brain. PloS Biol.3,e305.
  • Meng X, Wahlstrom G, Immonen T, Kolmer M, Tirronen M, Predel R, Kalkkinen N, Heino TI, Sariola H, Roos C. 2002. The Drosophila hugin gene codes for myostimulatory and ecdysis-modifying neuropeptides. Mech Dev 117(1-2):5-13.
  • Neupert S, Johard HA, Nässel DR, Predel R. 2007. Single-cell peptidomics of drosophila melanogaster neurons identified by Gal4-driven fluorescence. Anal Chem 79(10):3690-3694.
  • Raina AK, Menn JJ. 1993. Pheromone biosynthesis activating neuropeptide: from discovery to current status. Arch Insect Biochem Physiol 22(1-2):141-151.
  • Sato Y, Oguchi M, Menjo N, Imai K, Saito H, Ikeda M, Isobe M, Yamashita O. 1993. Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides. Proc Natl Acad Sci U S A 90(8):3251-3255.
  • Sato Y, Ikeda M, Yamashita O. 1994. Neurosecretory cells expressing the gene for common precursor for diapause hormone and pheromone biosynthesis-activating neuropeptide in the suboesophageal ganglion of the silkworm, Bombyx mori. General and comparative endocrinology 96(1):27-36.
  • Wei ZJ, Zhang TY, Sun JS, Xu AY, Xu WH, Denlinger DL. 2004. Molecular cloning, developmental expression, and tissue distribution of the gene encoding DH, PBAN and other FXPRL neuropeptides in Samia cynthia ricini. J Insect Physiol 50(12):1151-1161.
  • Zdarek J, Nachman RJ, Hayes TK. 1997. Insect neuropeptides of the pyrokinin/PBAN family accelerate pupariation in the fleshfly (Sarcophaga bullata) larvae. Annals of the New York Academy of Sciences 814:67-72.
  • Zhang Q, Nachman RJ, Kaczmarek K, Zabrocki J, Denlinger DL. 2011. Disruption of insect diapause using agonists and an antagonist of diapause hormone. Proc Natl Acad Sci U S A 108(41):16922-16926.