Supercontraction in crayfish muscle: correlation with a peculiar actin localization.
Crayfish muscle, like muscles from some other invertebrates, can supercontract. This muscle shortening is characterized by an overlap of thin filaments with crossing of thick filaments through the Z discs. In intact muscle cells, supercontraction does not seem to induce irreversible structural modifications in the tissue. Isolated crayfish myofibrils in the relaxed state cannot be distinguished from vertebrate myofibrils under light microscope, either by phase contrast or by immunofluorescence, with antiactin antibodies, actin being localized in the I bands. However, when isolated crayfish myofibrils are supercontracted, irreversible dammage occurs, most thin filaments being lost. Actin becomes then hardly detectable, being visible, by immunofluorescence, either in the Z discs or evenly distributed in the whole myofibril. During myofibril supercontraction, high amounts of denatured actin, become soluble as shown by SDS-PAGE, by double immunodiffusion, and by DNAse inhibition.
D000199:Actins / Q000302:isolation & purification*; D000818:Animals; D003400:Astacoidea / Q000033:anatomy & histology* / Q000502:physiology; D005399:Fishes / Q000033:anatomy & histology / Q000502:physiology; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology / Q000648:ultrastructure*; D009210:Myofibrils / Q000032:analysis*; D013045:Species Specificity
D000199:Actins