title: X-ray diffraction studies of the thick filament in permeabilized myocardium from rabbit.
abstract: Low angle x-ray diffraction patterns from relaxed permeabilized rabbit cardiac trabeculae and psoas muscle fibers were compared. Temperature was varied from 25 degrees C to 5 degrees C at 200 mM and 50 mM ionic strengths (mu), respectively. Effects of temperature and mu on the intensities of the myosin layer lines (MLL), the equatorial intensity ratio I(1,1)/I(1,0), and the spacing of the filament lattice are similar in both muscles. At 25 degrees C, particularly at mu = 50 mM, the x-ray patterns exhibited up to six orders of MLL and sharp meridional reflections, signifying that myosin heads (cross-bridges) are distributed in a well-ordered helical array. Decreasing temperature reduced MLL intensities but increased I(1,1)/I(1,0). Decreases in the MLL intensities indicate increasing disorder in the distribution of cross-bridges on the thick filaments surface. In the skeletal muscle, order/disorder is directly correlated with the hydrolysis equilibrium of ATP by myosin, [M.ADP.P(i)]/[M.ATP]. Similar effects of temperature on MLL and similar biochemical ATP hydrolysis pathway found in both types of muscles suggest that the order/disorder states of cardiac cross-bridges may well be correlated with the same biochemical and structural states. This implies that in relaxed cardiac muscle under physiological conditions, the unattached cross-bridges are largely in the M.ADP.P(i) state and with the lowering of the temperature, the equilibrium is increasingly in favor of [M.ATP] and [A.M.ATP]. There appear to be some differences in the diffraction patterns from the two muscles, however. Mainly, in the cardiac muscle, the MLL are weaker, the I(1,1)/I(1,0) ratio tends to be higher, and the lattice spacing D(10), larger. These differences are consistent with the idea that under a wide range of conditions, a greater fraction of cross-bridges is weakly bound to actin in the myocardium.
authors.affiliation: National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, Maryland, USA.
authors.forename: Sengen
authors.initials: S
authors.lastname: Xu
authors.forename: Donald
authors.initials: D
authors.lastname: Martyn
authors.forename: Jessica
authors.initials: J
authors.lastname: Zaman
authors.forename: Leepo C
authors.initials: LC
authors.lastname: Yu
mesh_terms: D000199:Actins / Q000648:ultrastructure*; D000818:Animals; D002478:Cells, Cultured; D008968:Molecular Conformation; D032383:Myocytes, Cardiac / Q000648:ultrastructure*; D009218:Myosins / Q000648:ultrastructure*; D010539:Permeability; D011487:Protein Conformation; D011817:Rabbits; D012518:Sarcomeres / Q000648:ultrastructure*; D014961:X-Ray Diffraction
chemical_list: D000199:Actins; D009218:Myosins