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Projectin the Elastic Protein of the C-filaments

This chapter appears in the following book:

Nature's Versatile Engine: Insect Flight Muscle Inside and Out

Edited by: Jim O. Vigoreaux
ISBN: 0-387-25798-5
» Get more information about this book at landesbioscience.com «

Chapter authors:
Agnes Ayme-Southgate and Richard Southgate

In adult insects, the highly specialized indirect flight muscles (abbreviated as IFMs) are powerful muscles adapted for the rapid repeated contractions necessary for flight. These muscles are referred to as asynchronous muscles, because they undergo multiple rounds of contraction for each single nerve impulse, a property made possible by the stretch-activation mechanism.1-5 The stretch-activation mechanism is explained as a “delayed increase in tension due to stretch” that activates the muscle and results in contraction. The IFMs are attached to the cuticle (exoskeleton) and because they are organized as two sets of nearly perpendicular muscles, their length oscillate in response to the stretch activation-contraction cycles. The stretch activation mechanism has been shown to be an intrinsic property of the myofibrillar apparatus, 1 and is made possible by several special physiological adaptations, such as a high resting stiffness. To explain some of the IFMs’ properties, early models proposed the existence of an additional third filament system with elastic properties, which is usually referred to as the connecting or C-filament system. Electron microscopy studies of insect flight muscles revealed the presence of fine connections between the Z bands and the thick filaments.6-11 In particular, electron microscopy of stretched myofibrils or purified Z disks of insect flight muscles have shown the presence of filaments extending or “projecting” from the Z band towards the myosin filaments and just overlapping the tip of the A band.12,13 In honeybee IFMs, connecting filaments can be extended to well over ten times their normal rest length. When these muscles are stretched in rigor and then released, the recoil forces of the connecting filaments cause the sarcomere to shorten, leading to the crumpling of the thin filaments held in rigor.9 The search for component(s) of the C-filament system led to the identification and characterization of the protein, projectin. Saide unequivocally demonstrated by antibody staining and biochemical analysis that the third connecting filament of honeybee flight muscles is composed of projectin.12

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