A periodic cytoskeletal lattice in striated muscle.
The axial periodicities of electron density in striated muscle fibers extend over four orders of magnitude, ranging from the sarcomere repeat (2000-3000 nm) to a residue repeat in the alpha-helix of structural proteins (0.15 nm). A prevailing idea about the regular arrangement of structures in the contractile apparatus maintains that long-range axial spacings, related to the organization of sarcomere repeats, are essentially independent of the short-range periodicities with molecular dimensions. This is a central theme of the sliding filament hypothesis but is only supported by evidence from measured spacings near the upper and lower limits in the spectrum of dimensions, leaving a wide gap in resolved structural information extending from about 460 down to 50 nm. Several independent morphological methods show an electron-dense cross-striation of low amplitude with a pseudo-period of 230 nm, out of phase with the sarcomere repeat, in myofibrils of frog twitch fibers. Averaged images of embedded muscle fibers indicate that the sarcomere repeat contains five symmetrical pairs of these striations, which are coordinated with discrete repeats of the major molecular periods in the thick and thin filaments, in register within A and I bands. The pseudo-period therefore correlates short-range molecular repeats in the filaments with long-range registry of the sarcomere repeats in myofibrils. This raises the interesting possibility that the 230-nm pseudo-periodicity identifies a replicated axial structure in myofibrils that integrates the organization of the major structural proteins into the sarcomere repeat. The density distribution in sarcomeres of isolated unstained myofibrils also establishes that symmetrical pairs of striations with intrinsically low amplitudes are independently distorted out of uniform register in stretched sarcomeres. This behavior is consistent with the properties of N lines. The out-of-phase arrangement of 230-nm striations in the sarcomere repeat of twitch fibers should produce special diffraction effects in the region of the gap in the spectrum of periodicities recorded from muscle, with maxima at spacings extending from 200 to 80 nm. Correspondence between the diffraction spectrum of myofibril models containing a 230-nm spaced axial pseudo-period and the observed very low-angle X-ray diffraction spacings from living muscle (Huxley and Brown, 1967) suggests that the 230-nm pseudo-periodicity is a regular detectable component of striated muscle, resembling the structure of naturally occurring leptomeric fibrils in extrafusal and intrafusal fibers (Karlson and Andersson-Cedergren, 1968).(ABSTRACT TRUNCATED AT 400 WORDS)
D000818:Animals; D002467:Cell Nucleus / Q000648:ultrastructure; D003599:Cytoskeleton / Q000648:ultrastructure*; D006801:Humans; D009124:Muscle Proteins / Q000502:physiology*; D009132:Muscles / Q000648:ultrastructure*; D009210:Myofibrils / Q000648:ultrastructure*; D012518:Sarcomeres / Q000648:ultrastructure*
D009124:Muscle Proteins