New metabolic activity of the nonsulfated sulfakinin Zopat-SK-1 in the insect fat body

Peptides. 2015 Jun:68:157-63. doi: 10.1016/j.peptides.2014.05.010. Epub 2014 May 29.

Abstract

Insect sulfakinins are multifunctional neuropeptides homologous to vertebrate gastrin/cholecystokin (CCK) neuropeptide hormones. We investigated the action of the nonsulfated sulfakinin Zopat-SK-1 (pETSDDYGHLRFa) on the levels of chosen metabolites in the Zophobas atratus beetle fat body. Samples of fat body were collected 2h and 24h after hormone injection. The administration of 20pmol of Zopat-SK-1 to feeding larvae significantly increased concentrations of lipids and proteins and decreased the content of glycogen in fat body tissue in the 24h experimental group. In contrast, the only increase in total lipid concentration in prepupal fat bodies was observed 24h after Zopat-SK-1 treatment. Simultaneously, changes in the quality and quantity of free sugars in the hemolymph were measured. In larval hemolymph, a marked increase in free sugar concentration and a decrease in glucose content were observed 24h and 2h after Zopat-SK-1 application, respectively. No changes in the prepupal stage were observed. For the first time we show potent metabolic activity of sulfakinin in the fat body tissue of an insect. Our findings imply a physiological function of the nonsulfated form of sulfakinin in energy storage and release processes in fat body tissue of larvae and prepupae was indicated. We suggest a role for sulfakinin signaling in the regulation of energy metabolism in insect tissues.

Keywords: Beetles; Carbohydrate and protein fat body metabolism; Lipid; Nonsulfated sulfakinin Zopat-SK-1; Sulfakinin; Zophobas atratus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbohydrate Metabolism
  • Coleoptera / metabolism*
  • Energy Metabolism
  • Fat Body / metabolism*
  • Glycogen / metabolism
  • Hemolymph / metabolism
  • Insect Proteins / physiology*
  • Larva / metabolism
  • Lipid Metabolism
  • Neuropeptides / physiology*
  • Organ Specificity

Substances

  • Insect Proteins
  • Neuropeptides
  • Glycogen