Biochemical aspects of flight and flightlessness in Gryllus: flight fuels, enzyme activities and electrophoretic profiles of flight muscles from flight-capable and flightless morphs.
Female Gryllus assimilis subjected to 4.5-7.7h continuous tethered flight had significantly lower amounts of total lipid, triglyceride and total soluble carbohydrate compared with unflown controls. A much greater amount of total lipid (6.3mg) was used during flight compared with carbohydrate (0.14mg). Flown individuals also had substantially reduced amounts of injected, radiolabeled [(14)C]-oleic acid. Activities of lipid, carbohydrate and amino acid catabolizing enzymes in flight muscles of G. assimilis and its wing-polymorphic congener, G. firmus, were very similar to activities in insects which primarily utilize lipid to power flight. By contrast, enzyme activities were very different from those in insects which primarily or exclusively use carbohydrate or proline as a flight fuel. These results strongly implicate lipid as the major flight fuel in Gryllus. Previous studies have shown that lipid levels are higher in flight-capable (long-winged) G. firmus that have small ovaries compared with flightless (short-winged) females that have large ovaries. Results of the present and previous studies collectively indicate that elevated lipid in long-winged G. firmus represents an energetic cost of flight capability which reduces (trade-offs with) reproduction in Gryllus. In G. firmus, mass-specific activities of nearly all enzymes were considerably reduced in underdeveloped, and to a lesser degree in histolyzed muscle, compared with fully-developed flight muscle. An important exception was alanine aminotransferase, whose activity was the highest in histolyzed muscle, and which may be involved in the catabolism of amino acids derived from muscle degradation. Despite the dramatic differences in enzyme activity, electrophoretic profiles of soluble flight-muscle proteins differed only subtly between fully-developed and underdeveloped or histolyzed flight muscles.
Zera
A J.
AJ
School of Biological Sciences, University of Nebraska, P.O. Box 880118, Lincoln, USA
Sall
J
J
Otto
K
K