title: Instantaneous view of actomyosin structure in shortening muscle.
abstract: In the previous study), utilizing the rapid-freeze technique for electron microscopy, a new type of actomyosin assembly was reported to occur during isometric contraction. In this study, we have developed a new freezing apparatus which permits rapid freezing of the "isotonically-shortening" muscle at high shortening velocity, allowing simultaneous measurement of its tension and length. Using glycerinated rabbit skeletal muscle rapidly frozen with this system, we have compared the freeze-substituted images of the actomyosin assembly in the shortening muscle at various tension levels with those in isometrically-contracting muscle. The optical diffraction patterns obtained from whole A bands and from single actin filaments decorated with crossbridges have revealed that the unique actomyosin assembly formed in isometrically-contracting muscle is maintained even during high-velocity shortening under near-zero load.
authors.affiliation: Department of Ultrastructural Research, Tokyo Metropolitan Institute of Medical Science, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Tsukita
authors.forename: M
authors.initials: M
authors.lastname: Yano
mesh_terms: D000205:Actomyosin / Q000502:physiology*; D000818:Animals; D005615:Freezing; D007537:Isometric Contraction; D008854:Microscopy, Electron; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology / Q000648:ultrastructure*; D009210:Myofibrils / Q000648:ultrastructure; D011817:Rabbits
chemical_list: D000205:Actomyosin