title: A survey of in situ sarcomere extension in mouse skeletal muscle.
abstract: The giant molecule titin/connectin was demonstrated to connect the ends of thick filaments with the Z-disks and thus to provide an elastic connection that seems to be responsible for passive tension in striated muscle. To investigate the physiological limits of I-band titin extension in skeletal muscle, we have measured sarcomere lengths of a number of mouse postural and clonal muscles in situ under the constraints imposed by the skeletal, ligamentous and tendinous components of the motile apparatus. These values now give upper limits for the extension of the I-band and therefore for the maximal degree of titin extension under physiological constraints. We find that I-band extension in all muscles investigated does not exceed a factor of approximately 2.5 in situ, which is well below values obtainable in isolated fibre preparations. Approach to the yield-point is therefore prevented by extramuscular mechanisms. Sarcomere lengths near the tendinous junction and within the muscle are virtually identical in extended muscle, suggesting that a major function of titin in intact muscle is to ensure uniform sarcomere lengths over the entire muscle length and thus to prevent localized myofibril overstretch during isometric contraction.
authors.affiliation: European Molecular Biology Laboratory, Structural Biology Division, Heidelberg, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Goulding
authors.forename: B
authors.initials: B
authors.lastname: Bullard
authors.forename: M
authors.initials: M
authors.lastname: Gautel
mesh_terms: D000818:Animals; D005260:Female; D051379:Mice; D008807:Mice, Inbred BALB C; D008854:Microscopy, Electron; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology* / Q000648:ultrastructure; D016658:Psoas Muscles / Q000502:physiology / Q000648:ultrastructure; D012518:Sarcomeres / Q000502:physiology* / Q000648:ultrastructure