Dr. Joanisse et Kb. Storey, ENZYME-ACTIVITY PROFILES IN AN OVERWINTERING POPULATION OF FREEZE-TOLERANT LARVAE OF THE GALL FLY, EUROSTA-SOLIDAGINIS, Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 164(3), 1994, pp. 247-255
The activity of some enzymes of intermediary metabolism, including enz
ymes of glycolysis, the hexose monophosphate shunt, and polyol cryopro
tectant synthesis, were measured in freeze-tolerant Eurosta solidagini
s larvae over a winter season and upon entry into pupation. Flexible m
etabolic rearrangement was observed concurrently with acclimatization
and development. Profiles of enzyme activities related to the metaboli
sm of the cryoprotectant glycerol indicated that fall biosynthesis may
occur from two possible pathways: 1. glyceraldehyde-phosphate --> gly
ceraldehyde --> glycerol, using glyceraldehyde phosphatase and NADPH-l
inked polyol dehydrogenase, or 2. dihydroxyacetone-phosphate --> glyce
rol-3-phosphate --> glycerol, using glycerol-3-phosphate dehydrogenase
and glycerol-3-phosphatase. Clearance of glycerol in the spring appea
red to occur by a novel route through the action of polyol dehydrogena
se and glyceraldehyde kinase. Profiles of enzyme activities associated
with sorbitol metabolism suggested that this polyol cryoprotectant wa
s synthesized from glucose-6-phosphate through the action of glucose-6
-phosphatase and NADPH-linked polyol dehydrogenase. Removal of sorbito
l in the spring appeared to occur through the action of sorbitol dehyd
rogenase and hexokinase. Glycogen phosphorylase activation ensured the
required flow of carbon into the synthesis of both glycerol and sorbi
tol. Little change was seen in the activity of glycolytic or hexose mo
nophosphate shunt enzymes over the winter. Increased activity of the c
l-glycerophosphate shuttle in the spring, indicated by greatly increas
ed glycerol-3-phosphate dehydrogenase activity, may be key to removal
and oxidation of reducing equivalents generated from polyol cryoprotec
tant catabolism.