Hypertrehalosaemic neuropeptides decrease levels of the glycolytic signal fructose 2,6-bisphosphate in cockroach fat body
In cockroach fat body, trehalogenesis and glycolysis compete for glucose phosphates as common substrates. During trehalogenesis, glycolysis is inhibited, although the mechanism responsible for this is not known. Incubation of the isolated fat body from the Argentine cockroach Blaptica dubia with an extract of the corpora cardiaca containing as little as 0.005 gland equivalents ml-1 of incubation medium increased the release of trehalose (anthrone-positive material) from the tissue by more than 100 %. The content of the glycolytic activator fructose 2,6-bisphosphate was decreased by up to 50 %. A decapeptide was isolated from the corpora cardiaca of B. dubia and shown to be identical to the naturally occurring Blaberus discoidalis hypertrehalosaemic peptide (Bld HrTH), which was also found in the corpora cardiaca. Synthetic Bld HrTH at 2 nmol l-1 and above increased trehalose production and decreased the content of fructose 2,6-bisphosphate to the same extent as did corpus cardiacum extract. The octapeptides Periplaneta americana cardioacceleratory hormones I and II (Pea CAH-I and Pea CAH-II) also had a significant effect on both parameters. Fructose 2,6-bisphosphate is a potent activator of phosphofructokinase from cockroach fat body if the enzyme is assayed at near-physiological concentrations of substrates and effectors. It is suggested that, because of the decrease in fructose 2,6-bisphosphate levels in the fat body, the activity of the key glycolytic enzyme phosphofructokinase is diminished. This can explain the inhibition of glycolytic flux by hypertrehalosaemic peptides which alters the balance of glucose metabolism in favour of trehalose formation.
Becker
A
Institut fur Zoologie, Johannes Gutenberg-Universitat, Saarstrasse 21, D-55099 Mainz, Germany. gwegener@mail.uni-mainz.de.
Wegener
G