Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.
Cardiac muscle has been extensively studied, but little information is available on the detailed macromolecular structure of its thick filament. To elucidate the structure of these filaments I have developed a procedure to isolate the cardiac thick filaments for study by electron microscopy and computer image analysis. This procedure uses chemical skinning with Triton X-100 to avoid contraction of the muscle that occurs using the procedures previously developed for isolation of skeletal muscle thick filaments. The negatively stained isolated filaments appear highly periodic, with a helical repeat every third cross-bridge level (43 nm). Computed Fourier transforms of the filaments show a strong set of layer lines corresponding to a 43-nm near-helical repeat out to the 6th layer line. Additional meridional reflections extend to at least the 12th layer line in averaged transforms of the filaments. The highly periodic structure of the filaments clearly suggests that the weakness of the layer lines in x-ray diffraction patterns of heart muscle is not due to an inherently more disordered cross-bridge arrangement. In addition, the isolated thick filaments are unusual in their strong tendency to remain bound to actin by anti-rigor oriented cross-bridges (state II or state III cross-bridges) under relaxing conditions.
Kensler
Robert W
RW
Department of Anatomy, University of Puerto Rico Medical School, Medical Sciences Campus, San Juan, Puerto Rico 00936-5067, USA. rkensler@rcm.upr.edu
D000199:Actins / Q000378:metabolism*; D000818:Animals; D003902:Detergents / Q000494:pharmacology; D005583:Fourier Analysis; D009206:Myocardium / Q000378:metabolism* / Q000473:pathology* / Q000648:ultrastructure; D017830:Octoxynol / Q000494:pharmacology; D011485:Protein Binding; D011817:Rabbits; D012984:Software
D000199:Actins; D003902:Detergents; D017830:Octoxynol