Ghrelin effects on midgut tissue antioxidative defense and glutathioneS-transferase activity in Lymantria dispar (Lepidoptera)

Abstract

The aim of the study was to examine changes in Cu-Zn superoxide dismutase (SOD), catalase (CAT), their gel electrophoresis profiles, glutathione reductase (GR) activity, amount of glutathione (GSH), and the activity of glutathione S-transferase (GST) -phase II biotransformation enzyme in the midgut tissue of gypsy moth (Lymantria dispar L. (Lepidoptera: Lymantriidae)) larvae after ghrelin treatment. Four subpicomolar injections of ghrelin (0.3 pmol) or physiological saline (control) were applied every 24 h. The SOD, CAT, GR, GST activity, and amount of GSH were higher in the ghrelin-treated group than in the control. Electrophoresis gel bands of SOD and CAT had higher area and density in the treated group. The effects of ghrelin on the antioxidative defense and GST activity in insects were detected for the first time. The results provided evidence for possible application of insects as simple model systems in future studies of the role of ghrelin in the antioxidative protection of complex organisms.

Artificial light at night prolongs juvenile development time in the black field cricket, Teleogryllus commodus

“…Initially, exposure to ALAN may interfere with key hormones involved in appetite, satiety and growth rate (such as ghrelin, leptin, insulin, insulin-like growth factor (IGF), growth hormone and melatonin). Ghrelin stimulates appetite and potentially lead to increased weight gain in an environment where food is available ad libitum (Mataruga et al, 2012;Peric-Mataruga et al, 2009;Peric-Mataruga et al, 2015). The indolamine melatonin, in particular, is a powerful chemical driver of circadian rhythm, whose production is reduced in the presence of light at night (Pandi-Perumal et al, 2006;Poeggeler, 1993;Reiter, Poeggeler, Tan, Chen, & Manchester, 1993;Reiter, Tan, Osuna, & Gitto, 2000;Tan et al, 2010;Tan, Manchester, Terron, Flores, & Reiter, 2007;Vivienroels, Pevet, Beck, & Fevremontange, 1984).…”

Benzo[a]pyrene-induced changes in carboxylesterase, acetylcholinesterase and heat shock protein 70 of Lymantria dispar (Lepidoptera: Lymantriidae) from unpolluted and polluted forests

“…In all experimental groups, zymogram detection of AChE activity revealed discrete, barely visible lines on the gel corresponding to AChE, indicating moderate expression of this enzyme. It is very likely that this is a consequence of the high efficiency of the first line defense systems present in the midgut of L. dispar larvae [18,49] and the fact that PAHs are not natural, specific substrates for AChE. The concentrations of B[a]P present in host plant species for L. dispar larvae used in our experiment probably were not high enough to influence brain AChE activity in any way.…”