Effects of tannic acid on trypsin and leucine aminopeptidase activities in gypsy moth larval midgut

• Published in: Archives of biological sciences Vol. 65; no. 4; pp. 1405 - 1413
• Main Authors: Mrdakovic, Marija, Peric-Mataruga, Vesna, Ilijin, Larisa, Vlahovic, Milena, Todorovic, Dajana, Nenadovic, Vera, Lazarevic, Jelica
• Format: Journal Article
• Language: English
• Published: University of Belgrade, University of Novi Sad 2013
• Subjects: digestive enzymes; gypsy moth; phenotypic plasticity; tannic acid
• ISSN: 0354-4664; 1821-4339
• DOI: 10.2298/ABS1304405M

The effects of allelochemical stress on genetic variations in the specific
activities of gypsy moth digestive enzymes (trypsin and leucine
aminopeptidase) and relative midgut mass (indirect measure of food
consumption), as well as variability in their plasticity, were investigated
in fifth instar gypsy moths originating from two populations with different
trophic adaptations (oak and locust-tree forests). Thirty-two full-sib
families from the Quercus population and twenty-six full-sib families from
the Robinia population were reared on an artificial diet with or without
supplementation with tannic acid. Between population differences were
observed as higher average specific activity of trypsin and relative midgut
mass in larvae from the Robinia population. Significant broad-sense
heritabilities were observed for the specific activity of trypsin in the
control state, and for specific activity of leucine aminopeptidase in a
stressful environment. Significantly lower heritability for relative midgut
mass was recorded in larvae from the Robinia population reared under
stressful conditions. Significant variability of trypsin plasticity in larvae
from both populations and significant variability of leucine aminopeptidase
plasticity in larvae from the Robinia population point to the potential for
the evolution of enzyme adaptive plastic responses to the presence of
stressor. Non-significant across-environment genetic correlations do not
represent a constraint for the evolution of enzyme plasticity.